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UniProt_function_text_descriptions

like 3

A0A0R4IDX9

NINJ1_DANRE

Ninjurin-1 (Nerve injury-induced protein 1)

MASEAMELNGGVNRRDDPGARPQQGRMSRNTPLNMNHYANKKSAAESMLDIALLMANASQLKTVLELGPSFSFYIPLITLISISLTLQIIVGILLIFIVKWNLNDSSKHYILNLLENIVTALVFIVVVVNVFITAFGVQRPDDKTS

Homophilic transmembrane adhesion molecule involved in various processes such as inflammation, cell death, axonal growth, cell chemotaxis and angiogenesis (By similarity). Promotes cell adhesion by mediating homophilic interactions via its extracellular N-terminal region (By similarity). Involved in the progression of the inflammatory stress by promoting cell-to-cell interactions between immune cells and endothelial cells (By similarity). Acts as a mediator of both programmed and necrotic cell death (By similarity). Plays a key role in the induction of plasma membrane rupture during programmed and necrotic cell death: oligomerizes in response to death stimuli to mediate plasma membrane rupture (cytolysis), leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response (By similarity). Acts as a regulator of angiogenesis (By similarity). Promotes the formation of new vessels by mediating the interaction between capillary pericyte cells and endothelial cells (By similarity). Also involved in striated muscle growth and differentiation.

A0A0R4IEW8

ELAV4_DANRE

ELAV-like protein 4 (Protein elrD)

MFEISRTLNAALLSNEGSTETQWRQADLPQLQGWAEKGLLTQPKMIISNMEPQVTNGPNSATANGPSSNSRSCPSPMQTGGSNDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGPTGGSRGVGFIRFDKRIEAEEAIKGLNGQKPSGAAEPITVKFANNPSQKTSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRFSPITIDSMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQLFGPFGAVNNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKTHKS

RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs (By similarity). Plays a role in the regulation of mRNA stability, alternative splicing and translation (By similarity). Binds to AU-rich element (ARE) sequences in the 3' untranslated region (3'UTR) of target mRNAs (By similarity). Mainly plays a role in neuron-specific RNA processing (By similarity). Required for the maturation of motor neuron axonal branches and dendrites.

A0A0R4IGV4

JAM2A_DANRE

Junctional adhesion molecule 2A (Jam2a) (Junctional adhesion molecule B) (JAM-B)

MLVCVSLLILIHSVPVSPVTVSSRNPKVEVHEFSDAELSCEFKTEKDTNPRIEWKRKDKEKDVSFVYYGERFVGPFQDRADIEGATVRLRRVTQADAGEYRCEVSAPSDSISLGETNVTLRVLVPPQTPSCDVPSSALTGSQVELRCRDRHSIPPAVYTWYKDNRALPIRHPNATYTVNEFTGVLIPQSHYNPGTVCQHCMYHPNYHIPNTQLTTTFQTHDLNVAAVVSAVVLVCVILFLCAFGVCLAHRQGYFSRHRGRSFWIPHCHGVTHISSQNLNPSEHTQHSGYSHPPKEPQDFKHTQSFML

Junctional adhesion protein that mediates heterotypic cell-cell interactions to regulate different cellular processes (By similarity). During myogenesis, it is involved in myocyte fusion through the binding of jam3b on neighboring myocytes.

A0A0R4IKJ1

CAPAM_DANRE

mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase (EC 2.1.1.62) (Cap-specific adenosine methyltransferase) (CAPAM) (zCAPAM) (Phosphorylated CTD-interacting factor 1)

MTSENHTTIKADSALVMSPTGSTSQAAPFSPSTSKPIQELPDELIQAGWSKCWSKRENRPYYFNRFTNQSLWEMPVLGQHDVISDPLGLNAAPASGEANADAGLGNGQRKRHPSEDASQAGPNSFKRPKVEIPATPTTPTVPISPSTPGVKPWVNTTTDEKQGQASTPAPAPYRPSVVYWDLDIQTNAVIRERAPADHLPPHPEIELQRAQLTTKLRQHYHELCSQREGIEPPRESFNRWLLERKVVDKGLDPLLPSECDPVISPSMFREIMNDIPIRLSRIKYKEEARKLLFKYAEAAKKMIDSRNATPESRKVVKWNVEDTMNWLRRDHSASKEDYMDRLEHLRKQCGPHVASVAKDSVEGICSKIYHISAEYVRRIRQAHLTLLKECNISVDGTESAEVQDRLVYCYPVRLSIPAPPQTRVELHFENDIACLRFKGEMVKVSRGHFNKLELLYRYSCIDDPRFEKFLSRVWCLIKRYQVMFGSGVNEGSGLQGSLPVPVFEALNKQFGVTFECFASPLNCYFKQFCSAFPDIDGFFGSRGPFLSFSPASGSFEANPPFCEELMDAMVTHFEDLLGRSSEPLSFIIFVPEWRDPPTPALTRMEASRFRRHQMTVPAFEHEYRSGSQHICKREEIYYKAIHGTAVIFLQNNAGFAKWEPTTERIQELLAAYKVSGRSLPSPGPSSTNTGEKDSKPAPERTAPSQDNSSPVDKTAQDTTNT

Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs.

A0A0R4IKU3

RECK_DANRE

Reversion-inducing cysteine-rich protein with Kazal motifs

MSGCLQILTVLLCCRFWALVFSQDQSCCVHHAADIPRCRDACEQLASIRSESRLRHLLHRLPSYCPETLSELWICINNSLPGASRKSDGWVGLGCCELAISAECRRDCKQASSKNDISKVCKKDTENPLYSCITKNEMGSVCCSYAGRHTTCREYCQAIFRTDSSPTVSQISAVKEYCQSVSPPLILCVENYTRLHPTHRPIDSLHCCDRAEEAHCQLACKRILRTLSTEQEIMDGLISECGSQPLPQDPLWQCFLGSAHPPANTDPESPPIAKMDSAKLHCCFKANTSICRNMCVEISTSWGTQSWQEFDQHCEYNPVEMDLITCLADVREPCQLGCKELSYCTNFNNRPTELFRSCNVQSDQGALNDFKLWSNGSIRMPLMNIPVLDIRRCRPEMWKTVACALQIKPCYSRSRGSVICRSDCVEILRQCGDRRRFAEAQTPERICDLLSPTDDPERCIPLNRYLTASELESSVEEVIHPCNPNPCPSSHLCHVNRKGCHVGHDCLPYYCVPGCKLGEASEFLVPADARLQVPVHSAQPGCYEVCVCGQSGRLENCAEMPCFDTSKSCQIAGQRRSHGSSFRVDCNPCSCFAGDAVCSSRQCVRSDSSEEDRRLFTGLPCGCADHFVPVCAGNGRTYPSACVARCVGFTDSQFVFGSCRSFDPCSPNPCQRNQRCVPRRQVCLTDLSEFPCPQYECVSRPSSCDQKLLDPVCDTDNMEHANLCVLNLRGKTLAYSGHCQDACRRPREVCAHNGESYSTVCEAFSERVAVDYQGRCHAVGLESEFGSDSGCNAVPCPPLASDACQPVTPPGACCPVCAGMLRILWNKAQMNIFAKLNRDQPVSLHDILKILRLHVSVPQCDIFGYLSINSEIIILIAPVDQQPTPLQIEACSKEAEKIDSLINSGSPTLVSHVPLSAFLSSELQLSSVRSSSCVSISVCVLLLLCSLILTLTSDL

Functions together with adgra2 to enable brain endothelial cells to selectively respond to Wnt7 signals (wnt7a or wnt7b). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. Adgra2 is then required to deliver reck-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor (By similarity).

A0A0R4IMY7

TRPM2_DANRE

Transient receptor potential cation channel subfamily M member 2

MDEAALEPTLVQTLAVSTAKGGRYLSLSPSFQRCSLASWIKENIKKKECCFYVEDGREGICKCGYPKVQHCDEAIKPEDYMGEQWDKHRHVRETPTDAFGDISFGGLGQKTGKYVRVSSDTSCENLYQLMTEQWKLRSPNLLISVTGGAKNFYIKTHLKDKFRRGLIKVAQTTGAWILTGGTHAGVMKHVGMAVRDYTLSSGSMEGQIVVIGVAPWGVIHNRSTLIHPEGRFPAYYSLDEQGQGRLSCLDINHTHFLLVDDGTQGHYGVEIELRARLEKLISKLSLGNRESGVTIPVVCVVLDGGPGTLNTIYNSMLNHTPCVVLEGSGRLADVIAHVASVPVSKVTMALINRLLKRFFMQEYKNFTELQIIEWTKKIQDILRMPHLLTVFRIDEDKNYDVDVAILQALLKASRSDEHAGRHCWERQLELAVAWNRVDIAESEIFTEESQWTSSDLHPAMFSALVGDKPEFVRLLLENGVCVREFLEREETLCELYSHLPSCFFLRKLAKRVQGGKMRRGQEPLPGSRKVCLSHVSEEVRHLLGSFTQPLYIASRYKPTKDDVRLKVPSKGALDLPCSGEEWSADTVWDPGRDLFLWAVVQNNRELAEIGWEQCRDCIAAALAASKILRKLAQESGEDDSEEATEMLELANHYEKQAIGVFSECHSWDAQRAQKLLIRISPSWGRSTCLWLALEAHDKSFIAHSGVQALLTQIWCGELSVDNPHWKVLLCMIFFPLIYTGFLTFRRDEDIQRQAERTEQQKLAMESVFAGQSDGKIKRHLRGFSQKSELKPLNCSSRLMSFLKSPQVKFYWNIASYFGFLWLFAVVLMIDFQTSPSWRELLLYVWLTSLVCEEIRQLYHDFDGSGFRRKAKMYIKDLWNILDVLSIVLFIAGLICRLQASDTVFYIGKVILCIDFIIFCLRLMAIFSISRTLGPKIIIVRRMMLDLFFFMFLLSIWVVAYGVAKQGILIENEERLNWIIRGAVYEPYITIFGNFPTNIDNTLFDISSCSVNASDPLKPKCPMLNADNTPVFPEWLTIMMLCVYLLFANILLLNLLIAIFNYTFQEVQDNTDTIWKFQRYELIKEYHSRPALPPPFILLSHLILFIRGVFLRDLPQRHKNFRQELEQTEEEELLSWEAYMKDNYLASTRQDESQSVEHRIHDTAEKVGAMSELLEREQEMVSATMAKRLARLEEQVSESAKALRWIIDALKSQGCKSKVQPPLMRSKSSDRDDGDSSGQETDDEEAPHMFARQLQYPDSTVRRFPVPEEKVSWEVNFSPYQPPVYNQQDSSESDTSALDKHRNPGGRTGIRGKGALNTLGPNHILHPIFTRWRDAEHKVLEFLAVWEDAEKRWALLGGPAQPDEPLAQVLERILGKKLNEKTKTLLKAGEEVYKGYVDDSRNTDNAWVETSIITLHCDKNTPLMADLNHMVESSLSSHQPLQWREVSSDACRCSYQREALRQIAHHHNTYF

Nonselective, voltage-independent cation channel that mediates Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic N-terminal region causes a conformation change the channel is primed but still requires Ca(2+) binding to trigger channel opening.

A0A0R4IVA4

CC14A_DANRE

Dual specificity protein phosphatase CDC14AB (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog AB)

MTLDNLKHSAILSTLFKMADDNDLLGASEFIKDRLYFATLRSKPKSTANTHYFSTDEEFVYENFYADFGPLNLAMLYRYCCKLNKKLKSFTLTRKRIVHYTSFDQRKRANAAVLIGAYAVIYLKKTPEEAYRALISGSNASYLPFRDASFGNCTYNLTVLDCLQGIRKALQHGFLNFETFDVNEYEHYERVENGDLNWITPGKLLAFSGPHPKSKVENGYPLHAPEAYFPYFRKHNVTTIVRLNKKIYDAKRFTDAGFDHYDLFFVDGSTPSDIITRRFLHICESTSGAVAVHCKAGLGRTGTLIGCYLMKHYRFTSAEAIAWIRICRPGSIIGPQQHYLEEKQASLWAHGDSLRSKQRQYQDRSVPQLISSMDNLSISTSIFKSHSLDRMEENDYAENDLGMTQGDKLRALKGRRQPRSATTGAIRVEDVKVHTRSPSQPLSRMKPPASSQGSISPLKSSKVPASSSSSSSSSSVSASAKRIGRSSSSSTNLKSTRLASSLGNLYEPNTESISSGKPPSPSSFTPHPVRTTYNYHYEVNNNNNQYSTTSSPSKSLGYNLNHSGPSGASANARLSAGEQGHQRNPPAGLSGLSTRHLSRSIPSLQSEYVQY

Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis.

A0A0R4IVV0

MTP_DANRE

Microsomal triglyceride transfer protein large subunit

MMPVAGLLLCVTAVLCTSALGAGPRLDNGKLYRYSYSTEVGLNRPTGSPGGNVGFRISSDVDINLAWRNPEIQDEQLLQVKISNIQVESAGKHSRKNNIFHGSSAESILGKVRLEALQRPFLVLWKMGKIRSLYAQKAEPATVKNLKRGVASMLMMQLKSGKMSEADASGKCLVEYKVNKHQVIRTKHLETCKSQETGFTTHSPVLGISGKCAAETVITLENGIIKSADAKETHVLSINARHKAATKVLSRQSLTLKAIEAGPAEVAGKDVAGVVKALDDKFLSVGVIVEKTKPKCKGCPNLMETWKAVRSQLEPNSLSKAEAPRSFLTLVHSLRKSSKSEILTVLQNCSKTALPQLVDAVTSAQTPSSLSAILEFLDFSKKDGLILQERFLYACGFASHPTESMLQSLLEVSQGKIGSTEIKESVVIIMGALLRKLCLKGACDLPAVLKVKELLLAGPDSTQEESEVQMYLLALKNALLPEGIPVLAKYAESEVGAYSTIAITALQRYDPALITAEVKKALNRIYHQNQRIYEKNVRAAAADVIMSSNPSYMEVKNLLLSIGHLPHEMNKYMLSKIQDVLRFQMPAYKLVRQVMKDMISHNYDRFSKTGSSSAYSGFMAETVDVTCTYNLDILYSGSGVLRRSNMNIYGQSNNALLHGLQVTIEAQGLESLIAATPDEGEEELESFAGMSALLFDVQLRPVTFFKGYSDLMSKMFSMSGDPINVVKGLILLTDHSQVIPLQSGLRASAEFQAGLSIDISGGMEFSLWYRESKTSVNNRGALVIIGNMTVDTDFVSAGVEVGFETEATLDFITTVQFSEYPFLVCMQMDKTTFPFRETVSKQEKLPTGQMFSRKRSRDQVVPGSEFPLHQENSNMCKKVFEPAW

Catalyzes the transport of triglyceride between phospholipid surfaces. Catalyzes the transport of cholesteryl ester, and phospholipid between phospholipid surfaces (By similarity). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B. Required for yolk lipid utilization and absorption of dietary lipids in larvae.

A0A0R4IXF6

KAT2A_DANRE

Histone acetyltransferase KAT2A (EC 2.3.1.48) (Histone glutaryltransferase KAT2A) (EC 2.3.1.-) (Histone succinyltransferase KAT2A) (EC 2.3.1.-) (Lysine acetyltransferase 2A)

MADPAAQSSAQPRLQQAQSSGPTGSNSNPGAGSSDPARPGLSQQQWSSQKKAQVRSFPRAKKLEKLGVFSSCKANDACKCNGWKNPNPPTAARMELQQQAASLTETCRSCGHSLAEHVSHLENVSEEEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMGKPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPKERQTMYELSKMFLLCLNYWKLETPSQFRQRAQKEDAAAYKVDYTRWLCYCHVPQSNDSLPRYETCQVFGRSLLKSIFTVTRRQLLEKFRVEKDKLPPEKRTLILTHFPKFLSMLEEEIYGENSPIWEADFTMPASEGTQLGHQTVLSPVSISGSPHSKGSSASALGVTGLDVASSEPTIGEKRKLPEALTLEDAKRIRVMGDIPMELVNEVMKTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLSQKSNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHGILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKRQKEIIKKLIERKQNQIRKVYPGLTCFKEGVRQIPVESIPGIRETGWKPSAKEKSKELKDPDLLYNMLKNLLAQIKTHPDAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLKNRYYVTKKLFIADLQRVITNCREYNPPDSEYCKSANTLEKFFYFKLKEAGLIDK

Protein lysine acyltransferase that can act as a acetyltransferase, glutaryltransferasesucc, succinyltransferase or malonyltransferase, depending on the context (By similarity). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes (By similarity). Succinylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation (By similarity). In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase (By similarity). Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles (By similarity). Acetylation of histones gives a specific tag for epigenetic transcription activation (By similarity). Also acetylates non-histone proteins, such as tbx5. Involved in heart and limb development by mediating acetylation of tbx5. Together with kat2b, required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac). Also acts as a histone glutaryltransferase: catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (By similarity).

A0A0R4IY06

PLAT1_DANRE

Phospholipase A and acyltransferase 1 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4)

MDNQQRRTDNMASGETDHLQCVEEPQPGDLIEIFRPAYQHWALYLGDGYIINLTPVDEGQATAVSSVKSVFSRKAVVRMQLLKEVVGADSYRINNKYDDDHTPLPVSEIIQRAQMLIGQEVSYDLLGSNCEHFVTLLRYGEGVSEQASRAIGAISLVTAAASAFSVLGLINTRSRNRPF

Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid. Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE) which serves as precursor for N-acylethanolamines (NAEs) (By similarity). Required for complete organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. Organelle membrane degradation is probably catalyzed by the phospholipase activity (By similarity).

A0A0R4IZ84

EST1A_DANRE

Telomerase-binding protein EST1A (EC 3.1.-.-) (Ever shorter telomeres 1A) (Nonsense mediated mRNA decay factor SMG6) (Smg-6 homolog)

MADELERVRISAAELRAQASSFNIHGDDVKDLREEGKKQRQRDSKRPDLQLYKPGVGHPNRRMDSVEGAGSDTLIQPDGFGNDPKMSDESPTSPGCSYMPGTGNEDYLNDHSKPETNHKTDGHIGGDKHKLVDENAVKIIERAGTPKSPKQSRKMRKPDRQIYQPGGRRSQGNKEVGASKELDRDRSREEEVDGKSIETPLKCEKEEKRKNRRGKNDRKKQASVETPSANKTENAVENISNKVSNLHLETVESKDRDRQDDTNQIKHSEEGRKIQTGGANRGMGEDKKKERGNGKSRPGKEKGNNQVFDKKEEGEAGGKASEAPHLEGRKQRNFGAKEASRDQNLNHEKQQGNRPKEKGKPSERTDSKRVNAASKRYSQSDIRRPRNRTYSTSSASSGTSMDGLAEAERLKAEGQQFSARTLERATGQREFVRGGQTRSRRRTARTLSSTDSLEENEVWEREGRRSRAAEEAKSSTRKEGGILRVSLDKREEQASRKSTRGRGRGILVLPAHTDLTQTPDPAPPLGGMRGGMGLGRGRGGRGGGTRRLWDPNNPDKKPALVSSQQSQHASQHQALYLQQGGCGPLHFLDTDDETVGSPPVRQGEFFQNQQAAAMAYYKFQNSDNPYCYPVSANSPNTPPRYPYPYQIPYQIPGSNGMYPASAMTSFYGPYGQGGPGYPSPTVSALTPEEAEVQTRGELGKFLRLADSQELQLSNLLSRERLSQEGLERMAQLRAELLTIYERVILTDIEFSDSQNVDQTLWKNVFYQVIERFRQLLKDQNSDTAPQIKTMLMTILEEGAVFFDSLLQKLQSVFQFKLQDYMDCMAIRARPLRKTVKYALISAQRCMICQGDIARYREQASESANYGKARSWYLKAQQIAPKNGRPYNQLALLAVYTKRKLDAVYYYMRSLAASNPILTAKESLMSLFEEAKRKADQVERRLKQDSDGSAHGPKGHTGGRRGEDAARVEIWIRPSEVSGTSRPTGSESGKDSEQDGELGALSASDLNKRFILSFLHAHGKLFTKVGMESFPAVANRVLLEFRALLQHSPSPLGSTRMLQIITINMFTIYNAQIRAKGQGETRSALEEQAISLGLAMFGLLVQRCTELLKETPTEPIPAEELGEFDEMDDEEGMVRVSVFPHDLRELLPSMKVWSDWMLGHPEKWNPPPCSMQGSPDVWQCLADLCNSFSRVYHGEVLLYKADADGEGDEELRVLQLEEDKMLSGFVPLLAAPQDACYTDQGTDAAIAADCKRVTVLKYFLEALCGQEEPLLAFKGGKYISMAAPLTPSINTENKAQEQEDDVIVEESSLSASEGEIDGEMEGDGSEDDIRELRARRHALAHKLAQQQKRRDKIQAVLQTGGQLEIEVRPFYLVPDTNGFIDHLEGLRKLLACGTYILVVPLIVITELDGLAKGQDSREGVGNGAHARQVQDRARAAVMFLEKAFESRDPSIRALTSRGNTLESIAFRSEDTSGQKGNNDDVILSCCLHYCQDKAKDFMPAERNGPVRLRREVVLLTDDRNLRVKALTRNVPVRDIPAFLIWAKVG

Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini (By similarity). Required for normal embryonic development.

A0A0R6Y3I5

G5K_LEIDO

Glutamate 5-kinase (LdG5K) (EC 2.7.2.11) (Gamma-glutamyl kinase)

MADILKSVKRIVVKVGSSILVDNQEIAAHRIEALCQFIADLQTKYEVILVTSGAVAAGYTKKEMDKSYVPNKQALASMGQPLLMHMYYTELQKHGILCAQMLLAAYDLDSRKRTINAHNTIEVLISHKVIPIINENDATALEELVFGDNDRLSALVAHHFKANLLVILSDIDGYYTENPRTSTNATIRSVVHELSPDDLVAEATPNNRFATGGIVTKLQAAQFLLERGGKMYLSSGFHLEKARQFLLGGSHEIGTLFYSRVSS

Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. May be important for growth and survival.

A0A0S2UWC9

CAMT1_PETHY

Caffeoyl-CoA O-methyltransferase 1 (PhCCoAOMT1) (EC 2.1.1.104) (5-hydroxyferuloyl-CoA O-methyltransferase 1) (EC 2.1.1.-)

MAENGAAVQENQNVIRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALAIPHDGKILAMDINRENYEIGLPVIEKAGVAHKIDFREGPALPVLDQLVEDKNNHGTYDFIFVDADKDNYINYHKRIIDLVKVGGLIGYDNTLWNGSLVAPADTPMRKYVRYYRDFILELNKALAADPRIEICMLPVGDGITLGRRIS

Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation. Methylates caffeoyl-CoA to feruloyl-CoA, also able to methylate 5-hydroxyferuloyl-CoA.

A0A0S4FKT4

VSP1_CRODO

Thrombin-like enzyme collinein-1 (SVTLE collinein-1) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)

VIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRKHILIYVGVHDRSVQFDKEQRRFPKEKYFFNCRNNFTKWDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRVMGWGTIKSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATIRILCAGVLEGGIDTCHRDSGGPLICNGEFQGIVSWGDGSCAQPDKPALYSKVFDHLDWIQNIIAGSETVNCPS

Thrombin-like snake venom serine protease. Releases fibrinopeptide A and B in the conversion of fibrinogen to fibrin, with preferential activity on the alpha chain of fibrinogen. Also hydrolyzes N-p-toluensulfonyl arginine ester (TAME) and chromogenic artificial substrates of the blood coagulation cascade: S-2222 for factor Xa, S-2302 for kallikrein and S-2238 for thrombin. When tested in vitro, the recombinant protein does not degrade blood clots, suggesting that this toxin lacks fibrinolytic activity. In addition, it moderately inhibits human Kv10.1/KCNH1/EAG1 currents, with a mechanism independent of its enzymatic activity. It selectively blocks Kv10.1/KCNH1/EAG1 in a time and dose-dependent manner (IC(50)=4.2 uM for native protein and IC(50)=2.5 uM for recombinant protein). It may have a preference in interacting with Kv10.1/KCNH1/EAG1 in its closed state, since the inhibitory effect of the toxin is decreased at more depolarized potentials. Corroboratively, it may have possible antitumor applications, since it reduces the viability of human breast cancer cell line MCF-7, which strongly expresses Kv10.1/KCNH1/EAG1, but does not affect the liver carcinoma and the non-tumorigenic epithelial breast cell lines, which weakly express Kv10.1/KCNH1/EAG1. When tested on peripheral blood mononuclear cells (PBMC), the native protein shows mild cytotoxicity, whereas the recombinant protein does not show any cytotoxicity. Native form is not immununogenic, since it does not induce statistically significant antibody production in mice, whereas recombinant form shows an antibody titer slightly higher than the native form. In vivo, subplantar injection in mice paw induces a discreet paw edema. In addition, intraperitoneal injection of the recombinant protein into mice led to fibrinogen depletion, resulting in the blood incoagulability.

A0A0U1QT59

TMC_DROME

Transmembrane channel-like protein

MQNDEEPAAAAGTSGLSNGESLRSPPAPAPRRPKPGILRLDIGKPRRSSGGSVDFRCVGSSSSNGNTSNVATGANSENNSGVTSPHQLSVTWAPPCDLDRGGWQMQSSADAKREFYKGQRGRRAASQEDHRSYELNDFPLQNQSSDAESCHQEPHFAHQRSPGIGFDEDGGGGDIDDEESYTISVSAIMQRRASVRGYRGKRGSRSSRRASSPMDHVLDSVERRRSSVYTTSSEEGTNQESTQEQIFENIRLHKEVIQSVKLQPWPIRKKLKLVRQAKTYVARHEGALQERFAMSRSTRDLWARFKILMAARWRHWKRETASFLTVLIPWELRIKEIESHFGSGVASYFTFLRWLMWVNIMIAIPLVAFVIGPEYFATKHGETDPRKRMSDPEARVAGNLFTFWEFEGYLKYSPMFYGYYSSTSGISTSGYKLPLAYFLTAVLVYIYSFVATLRKMAENSRNSKLSSKDDECVFSWKLFTGWDFMIGHAETAHNRIASVVVGFKEALLEEAEKKKDNRNWRVILQRILVNILVMGLLGLSGATVVLLVNHSEDLAKHDNWLSRNAVNVTMTLLSFFLPMIFEALGLFENWHPRQQLRLQLARIMILNMLNLYSLMFSFIYKINSKEKPLQMLKLENETNTMELKNLLSSIEALRAMTPTTSLYGESTSDGLFDDSTSTATWGEDGGGLFSTTAAAALISTTVQRLKCYNMTVKCSKLRRNIISGKHLATTLMVLNLTTPAMVPPTLPTTLPTTFPTTLPTTLPTTLPTALPTTLPTTLPTTLPSTLATTTATTSSIWSTTEETSPTTTTTSPWTTLPPSTTTTEATTTTERATTTTEATSTTTLKITTAEINSTLSDTTKPLGKSIDTEIPNSTTNSATLSTIPATLNTTNLPLNSTTKLTTTTSTEKPQGEDNFIYTTGEDEGSYDYGSDSTSDAPDNNSYSDITDYSSEPSEIEDFDEQESTDQADDPLAKVLEQLDENETKGRRKRALAESPFFTSKYSRRHRNESAVSAGQPRETTESVNATPSRWPFNWASFRQTTPRTTTTRRVPSGILTKEEWERLRRLRGRITTTTSTSTTSTTTRRPRWRYRTTTTELTSTTEEESSTTESSTDSSSPGSTTNAFDSSSSTTEEDEYTTTEGSENRPYYVGYVDISEMGSTIYYDGDSEFLEECVITICPKGDDFFGSTTESPDSTTQSSDSKQLTTVKLTPLERKQKRLKEVQLAIKQIQTNLTTMCWETSLGQELSKVIVFDGLMSIVAPLCIDFLRALFVRYVNQNWCWDMEKTFPQYGDFKIAENILTLINNQGQVWMGIFFSPGLVLINLVKLMIMMYFRSWIVLTCNVPHEVVFKASKSNNFYLSLLLTMLFLCVLPVGYAIVWLRPSWHCGPFSEYNRIAEFITNTTRNALPKQLHEPLDYLTSSSTVIPLLLLLILIIYYLVSLTGALREANQDLRTQLQKEREEERKKIFKVPEVKQAEPTATTLTNRWRKVLEASSPVTPTQPPDFDTEEYKNQARKELISRIMKKALRKGSATSDEDSFVRRDDDDTDTEHQDSLPHDEEAKDKRFGLSRLQQIRRTRKPSLVDIVQIAKQERARAGSIVAGTSSSGTGNFPIKETHPKSRFKVEKHERKDRGSMKDKKDTRHRQSPQQQQQPPPYESPKDNEHDPDTNSRIVSASLLRRHKEQAEGEEPPTTPDAPQTPNSPVEPVEQALEESTPETPTLAKSKFHIVDEKKPPPHEVEDKPLPTPKESGSGGGSLGKFKFRKHKFKSNNVAAVKPEPEVFKFDERSVERSSDVPATHAAEYLNNEPSGTEEQDRSLPSPTPSQGQGHHQRQLSVLSRQGRKKIGNLLALVREAVNLKKDDVEQAGSDESPGPTTPTYLAYTPPPPPSVLSSVSSSTALEMPPTPEPESPTPSAPLHFGSSTSSRAPSKPPKPPMVPASATAPTATMDDLEELDTAGPITFPRRSDSHRRRTMRQDSQSSIWSDNIPTITISTTGSDECIVDAAAPQNGLPDPRSASPEPTVNIIRIDIENEHEK

Probable ion channel. Component of mechanosensitive neurons that participates in proprioception, sensing food texture, and directing egg-laying site selection (oviposition). Component of multi-dendritic neurons of the labellum (md-L) where it is required for sensing the hardness and viscosity of their food, enabling them to behaviorally discriminate their preferred softness and smoothness from harder and stickier food options. Required as part of oviposition site selection process to relay mechanosensory and chemosensory information on the hardness and sweetness of potential egg-laying substrates, thus ensuring females select the most optimal site for their eggs survival. Females determine the softest substrate for their eggs first by making a coarse evaluation of substrate hardness using mechanosensitive channels nan and Piezo in the leg tarsal bristles, followed by a much finer assessment using nan, iav and Tmc mechanosensitive channels on the labellum. This protein is required to sense subtle differences in substrate stiffness (between 0.25% and 0.3% agarose), likely acting in the md-L neurons. Also required in neurons on the labellum, including the md-Ls, and possibly in the brain, to inhibit discrimination of egg-laying substrates of different hardness if the substrate contains sucrose. During oviposition evaluation, activation of sweet neurons by sucrose enhances the activity of the Tmc neurons resulting in females losing their softness preference in favor of egg-laying sites that contain sucrose. Acts in the larvae peripheral sensory neurons, to contribute to proprioception and sensory feedback for normal forward crawling behavior. Required for the normal activity of the proprioceptive sensory dendrites, ddaE which show preferential responses to forward locomotion, and ddaD which show preferential responses to backward locomotion.

A0A0U1RPR8

GUC2D_MOUSE

Guanylate cyclase D (EC 4.6.1.2)

MAGLQQGCHFEGQNWTAPHWKTCLPCQGPWRLTVSHLKTVSSISVLSVVFWSVLLWADSLSLLAWARETFTLGVLGPWDCDPIFAQALPSIATQLAVDQVNQDASLLPGSQLDFKVLPTGCDTPHALATFVAHKNIVAAFVGPVNPGFCSAAALLAQGWGKSLFSWACEAPEGGGDLVPTLPSAADVLLSVMRHFGWARWAIVSSHQDIWVTTAQQLATAFRTHGLPIGLVTSLGPGEKGATEVCKQLHSVHGLKIVVLCMHSALLGGLEQTTLLHCAWEEGLTDGRLVFLPYDTLLFALPYGNRSYLVLDDHGPLQEAYDAVLTVSLESSPESHAFTATEMSGGATANLEPEQVSPLFGTIYDAVILLAHALNRSETHGAGLSGAHLGDHVRALDVAGFSQRIRTDGKGRRLAQYVILDTDGEGSQLVPTHILDTSTWQVQPLGKPIHFPGGSPPAHDASCWFDPNTLCIRGVQPLGSLLTLTIACVLALVGGFLAYFIRLGLQQLRLLRGPHRILLTSQELTFLQRTPSRRRPHVDSGSESRSVVDGGSPRSVTQGSARSLPAFLEHTNVALYQGEWVWLKKFEAGVAPDLRPSSLSFLRKLREMRHENVTAFLGLFVGPGVSAMVLEHCARGSLEDLLQNENLRLDWTFKASLLLDLIRGLRYLHHRRFPHGRLKSRNCVVDTRFVLKITDHGYAEFLESHCSSRPQPAPEELLWTAPELLRGPGKATFKGDVFSLAIILQEVLTRDPPYCSWGLSAEEIIRKVASPPPLCRPLVSPDQGPLECIQLMQLCWEEAPDDRPSLDQIYTQFKSINQGKKTSVVDSMLRMLEKYSESLEDLVQERTEELELERRKTERLLSQMLPPSVAHALKMGTTVEPEYFDQVTIYFSDIVGFTTISALSEPIEVVGFLNDLYTLFDAVLDSHDVYKVETIGDAYMVASGLPRRNGNRHAAEIANLALDILSYAGNFRMRHAPDVPIRVRAGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVSQSTVQALLSLDEGYKIDVRGQTELKGKGLEETYWLTGKVGFCRPLPTPLSIKPGDPWQDRINQEIRTGFAKARQGLAEPRKSGEAGPGP

Functions as an olfactory receptor activated by urine odorants, uroguanylin and guanylin and as well by the volatile semiochemicals carbon disulfide (CS2) and carbon dioxide (CO2). Has guanylate cyclase activity upon binding of the ligand (By similarity). Activation of GUCY2D neurons leads to the cGMP-dependent activation of the CNGA3 channels, membrane depolarization and an increase in action potential frequency. Signaling pathways activated by GUCY2D may trigger social behaviors such as acquisition of food preference.

A0A0U1RRE5

NBDY_HUMAN

Negative regulator of P-body association (P-body dissociating protein) (Protein NoBody)

MGDQPCASGRSTLPPGNAREAKPPKKRCLLAPRWDYPEGTPNGGSTTLPSAPPPASAGLKSHPPPPEK

Promotes dispersal of P-body components and is likely to play a role in the mRNA decapping process.

A0A0U3BRC5

GFDPS_LEUCN

Geranylfarnesyl diphosphate synthase, chloroplastic (LcGFDPS) (EC 2.5.1.81)

MSHCTIFLYKYFPGKPRYQHCSFLHPLNHKLKSLFLPITGSRFLSNSTFSVSDSAHSHQAKPHVRNAQFDFKAYMLEKITAVNQALDAALPVREPVKIHEAMRYSLLLGGKRICPIVCLAACHLVGGDESTAMPSAAALEMIHAMSLMHDDLPCMDNDDLRRGRPSNHVVFGEGATVLAGYALIARAFEHIATATQGVGPGKILRVIGELAQLIGAEGVVGGQVVDLRCGGEGQMAIGLEQLEYIHLHKTAASVEASAVAGAVLGGASEEEIERLRKYSRSAGLLFQVVDDILDVTKSSEELGKTAGKDLAAGKTTYPKLLGMEKSREMAEKLKREAQEQLLGFDPIKAAPLIALVDFIAYRDK

Involved in the biosynthesis of leucosceptrane sesterterpenoids natural products, which are playing defensive roles toward herbivorus insects (e.g. Spodoptera exigua). Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFDP), the C(25) prenyl diphosphate precursor to all sesterterpenoids. Geranylgeranyl diphosphate (GGPP) is the preferred substrate, however dimethylallyl diphosphate (DMADP), farnesyl diphosphate (FDP) and geranyl diphosphate (GDP) can also be used as allylic substrate.

A0A125QXJ1

ABCB6_MESAU

ATP-binding cassette sub-family B member 6 (ABC-type heme transporter ABCB6) (EC 7.6.2.5) (Mitochondrial ABC transporter 3) (Mt-ABC transporter 3) (P-glycoprotein-related protein) (Ubiquitously-expressed mammalian ABC half transporter)

MVTVGNYCEAEGPLGPAWAQNGLSPCFFFTLVPSTLMALGALALVLVLPCRRRDVPSGTEELFWAADSRVAPYALQLFLATLQVALPLAGLAGRVGTARGVRLPGYLLLASMLGSLASACGLWLLVAERRQARQSLAMGVWMKFRHSSGLLLLWTVAFAAENLALVSWNSPQWWWARADLGQQVQFGLWVLRYVISGGLFILGLWAPGLRPQSYTLRVHEADQDVERNQAQSTDRTSTWRDLGRKLRLLSSYLWPRGSPALQFIVLICLGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRVVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLFLTIVVTEWRAKFRRAMNTQENITRARAVDSLLNFETVKYYNAEGYEVERYREAIIKYQGLEWKSSASLVVLNQTQNLVIGLGLLAGSLLCAYFVSEQKLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGQIEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRIAAGDSEVEAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVSADQILVIKDGCIIERGRHEALLSQGGVYAEMWQLQQKGQETVSEDSKPQDIA

ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen. May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may participate in the de novo heme biosynthesis regulation and in the coordination of heme and iron homeostasis during phenylhydrazine stress. May also play a key role in the early steps of melanogenesis producing PMEL amyloid fibrils. In vitro, it confers to cells a resistance to toxic metal such as arsenic and cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-38 and vincristin (By similarity). In addition may play a role in the transition metal homeostasis (By similarity).

A0A126GUP6

MP1_DROME

Melanization protease 1 (EC 3.4.21.-)

MEPHFFFTVLWMLLMGTSSTYAQEIFGYCRTPDENSGTCINLRECGYLFELLQSEEVTEQDRRFLQASQCGYRNGQVLEKHFCFTNVQICCANSRMRNQQPQWGNHPQPTQTTKPTKRSGTKLLPMAPNCGENFGDRVVGGNETTKREFPWMALIEYTKPGNVKGHHCGGSLINHRYVLTAAHCVSAIPSDWELTGVRLGEWDASTNPDCTVGKNGRRDCNEPYVDYPVEERIPHPQYPGNSRDQLNDIALLRLRDEVQYSDFILPVCLPTLASQHNNIFLGRKVVVAGWGRTETNFTSNIKLKAELDTVPTSECNQRYATQRRTVTTKQMCAGGVEGVDSCRGDSGGPLLLEDYSNGNSNYYIAGVVSYGPTPCGLKGWPGVYTRVEAYLNWIENNVRA

Serine protease which plays an essential role in the melanization immune response by acting downstream of sp7 to activate prophenoloxidase (PPO1). May function in diverse Hayan-dependent PPO1-activating cascades that are negatively controlled by different serpin proteins Spn27A in the hemolymph and Spn77BA in the trachea. Regulation of melanization and PPO1 activation appears to be largely independent of the Toll signaling pathway.

A0A131MCZ8

CNNM3_CAEEL

Metal transporter cnnm-3 (CNNM family homolog 3)

MSKTPWALGLLIFLLTFTSPLSSSPVRSTDNSTSSKGLLNVNSSVILEPSILPSSASKPESLHLSKVRVSGLRLEAHASSTENIVLGHNKKHNVVVVPNKNVRVVLFGQNFQDIGALTFTADGSCKDLAHFFEADFSSMTPIRVVVEMSFPKTTESKDSFKLCVSEKFYANPQFVIVEDPFTMVTTEIPPVDEYMPKWLSWICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGTEQEKRDAGRILPIRKKGNQLLCTLLIGNVVVNVGVSLLMDQLVGSGFAVLVAATSCIVVFGEIIPQALCVKLGLPIGARTIPITQVLLFLMYPLTWPISKVLDIFLKEELTRSLERNKLVEMLKLSEKSIIGGQSDEFKMVLGALELYDKTVAHAMTRYEDIFMLPHTLTLGAGMVTQILDMGYTRIPIYENDRKNIVALLFVKDLALLDPDDNHNVMKIASIYNHEVRRVLVDMPLRNMLEEFKRGEYHMALVERLVEQEDKDPIYELCGLITLEDIIEEIIQCEIIDETDAVCDNVHRKKRQRKRNHDMSQIVNTAHAKCAINIQMLAVTIQVMSTCHKIFSSNYILPTILEKLIRKNCKKVETTQFSCLKEVGVVQPKPAVLFTKGEFSNKFIMILSGRAVVTIGKEEMRLEAGAWHSFGTEVLDAMAEAIERSLNQSTSRSTVSLNTEITNNSIGFIPDFDTVILYECVFCEITAADLLLAYNSSQIMQNNTKMQVVRSNSRISLIEEIPKDAVSTPIRNGSVKLRTVSEGETVHLLPKNMECHFNKQEKYEEEEE

Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis. Promotes postembryonic gonad development by regulating Mg(2+) levels, probably via AMPK signaling.

A0A139GI49

KAWA_MICA8

Kawaguchipeptin peptide (Cyclic cyanobactin) [Cleaved into: Kawaguchipeptin A (Non-posttranslationnaly modified kawaguchipeptin B)]

MKNPTLLPKLTAPVERPAVTSSDLKQASSVDAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAGVNAAWLNGDNNWSTPFAADGAE

Both kawaguchipeptin A and B, which only differ by post-translational modifications, have antibacterial activities, since they inhibit the growth of the Gram-positive bacterium S.aureus at a concentration of 1 ug/mL.

A0A140H546

MAFB1_TOXGO

Mitochondrial association factor 1 form b1 (MAF1RHb1 allele) (MAF1b)

MWRIWRCRLSFLFATGCLLGALTAGLGSQMSDSVGRNVQAPAGVADASQEAGDVVEERTERTEEQAFALGPPRRHSSESLFPRNASVTARRRRNRRIALIATAVGVAVILAAVYVLRRRRAQRPQDPEPPAPRSVEDPEVLPEEDEASSSLPPPPPPSPPPPPPVEDPLSPESQTVDLSCLSGTTVRFFGPSHHFGGFTPLYDPAPDKRVATVDAGANALFIGGGGLNGQFAKTLLEEAEKHGIRLTPEELSQHSQRIQQSLLRRAVKSPGKLVELDTGVASPVFARSFGFVPVVPGLMWEESEVGPNVGVTFVHILKPEVTPYGNLNNNVMMYTVAPSGAAPDKTYSLAYKTTIAGVIGAAAAYNDTPAGQQYPVQGLRLPLLGGGIFRRNRSLESIGRANAEGTSLAITRYGPNFELQYMYDPSNAALHGLQEAESTYLASMLD

During host cell infection by tachyzoites, required for tethering the parasitophorous vacuole to the host mitochondria. This process, known as host mitochondrial association (HMA), induces the formation of SPOTs (structures positive for outer mitochondrial membrane (OMM)), a cellular response to OMM stress, which leads to the constitutive shedding of OMM vesicles containing proteins such as mitofusins MFN1 and MFN2, which normally restrict parasite growth. Specifically, binds to the host OMM import receptor TOMM70 to interact with SAMM50, a component of host mitochondrial intermembrane space bridging (MIB) complex. By targeting SAMM50, induces the disassembly of the MIB complex, thereby promoting the formation of SPOTs. Inhibits host TOMM70 import activity. Plays a role in the modulation of the host innate immune response to parasite infection.

A0A140JWS2

PTMG_PENSI

Geranylgeranyl pyrophosphate synthase penG (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Penitrem biosynthesis cluster 1 protein G)

MLFLAPGYIFPHVATPVTVAIDFAQAVKEGAYSFLDLKASPVPNPELFQPPSRVSIGMTGGREERNEEIIRGPLNYLLSLPGKDIRGKLIDALNEWFRVPEDKLSTIKEIIVILHTASLLIDDIQDSSQLRRGNPVAHRIFGVAQTINSANYAYFLAQAKLADLNDSRAFDIFTKGLLKLHRGQGMELYWRDNLICPTEEEYVEMVSCKTGGLFYLAVQLMQLNSEVTVNFSSFINLLGIIFQIRDDYMNLQSGTMTKTKGFSEDLTEGKFGYPIIHSIHAAPNDQQLIQILKLKTNDEVIKQYAVRYIESTGSFIYCREKLDLYLQEANETFQGLELLLGPSKGIRAILNFLRTR

Geranylgeranyl pyrophosphate synthase part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline. Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD. A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine. The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE. Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A.

A0A140LI88

ANR31_MOUSE

Ankyrin repeat domain-containing protein 31

MENGAEASDCDSDETVIEGSVTENEPEDEELPWRRLLLNQDTTCRSEFCFHSGVDGMQKGIHSPEIQLGLKLRKDSQEQNNKNKLLLALSEDLVLQDPQDKTAQNQVLLQTTKEFPVFTVSFPHPEVSWSHQNTGGHEAENCENLPHSKKELRENSDSPEVSLLSGTSPVAPDLVALKERLTEPVKTLAVPNTLSEPGEEVTQTMTSKETKDEESSLETFVSTLEKLLESSECTQEERLLEVMDDFNPQELFSTLSNSLGSVSVPLNAWAAQGRDELENKADAALPAKLLAAVNTGADVGPSCQGQEKSSSVSGGNGCLAVQPIMSQVDEDCTQIAQNIEDPKPFRLQTLTHENAISYEQINKKKNSDPIKNTSTQETPRVLRRSSRLEKLKASRDVVHTEAVLKKPERILSNTLSFKDQINSIFTTDSFSKRKNMHSSGFKNEQIRKSEQLRKKNGTGEMKKMCLCTINRRNVFGENLLYKAALHNDVDLVRCCIKNGENVNQPSYDGWTALHEASIGGYYQAVSELLKGGADVNVKGKYQITPLHDAVMNRHYKVAELLLMSGADPLFRSDHGTCALDEAKDSSMETLLMKYIPQQKKCHLSAQRNSTDPAHVEDMFQNKKPKLSSNNYTEFICDENFDRQEPGHLEINKGSNNLLMSKEYVCEHCQKDSNTTKFGKSNLNSVKNSRTNVSKRKGQKNRQQKKTQVDDRDCNLSQKIGTSSFRRTNKLLTQQQHAVQTLSDLPEESFELSTTTLSSLENGIGYNEACLVSKKSDTHVLDSSDGQELESVDQTEAASVSELSSYKEIKLLPVTTHQQPHTNQEQYSSPYKSLGNNSSNEKGKATNKWEDSFFSFIKGRSADSDSDCHTLDKSIASPKEGMSHDHHEEIMTGQEVDSQQRLSSENYFSQENDLKVHPLTTHPQEEAVNFCDSNLISVQHTPDYKNCLHEISFGNSYAKTEQSSTSCTRPPSTQKVSPLTVEVELLKGLQDSLAHRDSSPLVNQAGIHSLERKQDTDKNYTKKGPNTSSSSRPLPTVVHSQVIEITKAEKRREDLPGNEPINNTDFYSTDINKELANSSQLNQRKEKENVRKSDAELTHNDSEAERTLKSCEEKKKNMDSETHSPCDIQEHRKDQNFRKRKCSLKAPCSQGVNTTGIGKRNKKGESQLHVAARGGNLSRVKVLIEARADVNLRDNAGWTPLHKAASGGFDDVIIELLQAGANVNCENIDGIVPLHGASAGNHLKAAEILLEHGANPNQKDQKQRTALDEADDEKMKELLKSYGAIESTNGEKRNSTDLVKIPTVQPKRYKQFICDNDKAIGSPVPSHKAKKSESLPVHQTISAILQDIEEKQENLLKLEIRNSEDEEQYIGKMLEIKEVMDNILAQQKTERDDLAKKYRVSMESFKHGALREQLANLATRQKSLLVVAKKQKKIRLKIQNYKNATAVSGVGLRKLPCNSDISSDKKSQEPPTMGDSAHAQPGLLAPVSLAYGSMQEIPLSPEIESESQKINICLNAEAIRREEFSGNDINSKQNVQDCTLGGLLRSKPTDDAEKIASSSQPAALTPHAENSQAEATVKGCGFDSSALTGTINISEDKSIFSPNGACLAADPHSQKLSRCNPKRRNKKTASQQPSAGAAEPLPQAPAVLDTYTVHQTLPCLRDSAAAASHTDSTQSSLSSASAHQHPTKTVPHRNTTPRKKAVQLKDLILRGRINPGNNILEFKTQETTHRASVLPSGKLKGENGQIYQNPVTWLKELLGGGSYVTWNYAWNTVTYLGRELVKCVSEEAPMSAELNPPQLHQPHLSAGTSRESMQTIPHYLQIKEILQISKQELLPCHVMEQHWKFYVGRSHSEALLSW

Required for DNA double-strand breaks (DSBs) formation during meiotic recombination. Regulates the spatial and temporal patterns of pre-DSB recombinosome assembly and recombination activity by acting as a scaffold that anchors REC114 and other factors to specific genomic locations, thereby regulating DSB formation. Plays a key role in recombination in the pseudoautosomal regions of sex chromosomes.

A0A140LIF8

IRGM2_MOUSE

Immunity-related GTPase family M protein 2 (EC 3.6.5.-) (Interferon-inducible GTPase 2)

MEEAVESPEVKEFEYFSDAVFIPKDGNTLSVGVIKRIETAVKEGEVVKVVSIVKEIIQNVSRNKIKIAVTGDSGNGMSSFINALRLIGHEEKDSAPTGVVRTTQKPTCYFSSHFPYVELWDLPGLGATAQSVESYLEEMQISIYDLIIIVASEQFSLNHVKLAITMQRMRKRFYVVWTKLDRDLSTSTFPEPQLLQSIQRNIRDSLQKEKVKEHPMFLVSVFKPESHDFPKLRETLQKDLPVIKYHGLVETLYQVCEKTVNERVESIKKSIDEDNLHTEFGISDPGNAIEIRKAFQKTFGLDDISLHLVALEMKNKHFNTSMESQETQRYQQDDWVLARLYRTGTRVGSIGFDYMKCCFTSHHSRCKQQKDILDETAAKAKEVLLKILRLSIPHP

Immunity-related GTPase that plays important roles in innate immunity and inflammatory response. Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Required for clearance of acute protozoan and bacterial infections. Acts by participating to Tgtp1/Irgb6 and Gbp1-mediated parasite killing by promoting their accumulation on the T.gondii parasitophorous vacuole membranes. Also required for prolonged loading of ubiquitin and p62/Sqstm1 to parasitophorous vacuole membranes. Also acts as a key negative regulator of the inflammatory response by inhibiting the non-canonical inflammasome, thereby protecting against Casp11-driven septic shock during endotoxemia.

A0A140N5J7

KDSC_ECOBD

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (EC 3.1.3.45) (KDO 8-P phosphatase)

MSKAGASLATCYGPVSADVMAKAENIRLLILDVDGVLSDGLIYMGNNGEELKAFNVRDGYGIRCALTSDIEVAIITGRKAKLVEDRCATLGITHLYQGQSNKLIAFSDLLEKLAIAPENVAYVGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCDLLLLAQGKLDEAKGQSI

Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.

A0A142I5B9

POLG_ZIKVK

Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (NS5)]

MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGTDTSVGIVGLLLTTAMAVEVTRRGNAYYMYLDRSDAGEAISFPTTMGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLVWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAAKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVPINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMAICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRYGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMMRRIIGDEEKYVDYLSTQVRYLGEEGSTPGVL

[Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Inhibits the integrated stress response (ISR) in the infected cell (By similarity). [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner. In addition, host NCAM1 can also be used as entry receptor. Interaction with host HSPA5 plays an important role in the early stages of infection as well. Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis. Antagonizes also the host alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). Disrupts host centrosome organization in a CEP63-dependent manner to degrade host TBK1 and inhibits innate immune response (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (By similarity). [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (By similarity). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Leads to translation arrest when expressed ex vivo (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (By similarity). [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (By similarity). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (By similarity). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (By similarity).

A0A144A134

ISN1_PLAF7

IMP-specific 5'-nucleotidase 1 (PfISN1) (EC 3.1.3.99)

MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLNIKNEQKNYMIKYEVLEEAVIRIKKEIIKNKITAPYCAFNGGQDLWVDVGNKAEGLLILQKLLKIQKKKCCHIGDQFLHSGNDFPTRFCSLTLWVSNPQETKACLKSIMHLNIKSFIPEVLYENQ

Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine. By dephosphorylating IMP, plays a role in the purine salvage pathway. Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor.

A0A144A2H0

AMPP_PLAF7

Aminopeptidase P (PfAPP) (EC 3.4.11.9) (Xaa-Pro aminopeptidase)

MQLNFLLFVFIFLMVFHLNIFNKGKRQNLVSAYLNHFKKSYFSGVTSGSDCVNKSEVSSDNNNNNNNNNNKIAHNFFSKKYQRNFENNNLSENQENNKNIIYSGSNIFKNIYNTEMMSNNNTVDVNMMDNNPAARLEELRTIMKKNKIDVYILINSDEHNSEIINEKDKKIVKITNYSGADGILIVTKDKPILYVNALYELQAMNELDQNLFTLRISRIDNRDEIFETISSLEFNTIAFDGKNTSVVFYEKLRKALLNAYPKKKIVEKIIYNNNFDDVNKKDDENVLNFLVLEKSLVEIKDYPVNNKTLYIHDRKYNGACAGEKIDKLKQSLMYDIKNVDNLLLSELDEIAYLLNLRGYDYQYSPLFYSYLLFQFDREEQDFSKIVFFTTVKNLPADVKNLLEINKVIVKEYEEIVPYLRDVVIPSIPKHNDDNPDFKKYDISLSPYINLMIYKLFDRKNVLLQNSPVVKMKAVKNDVEIDNMKQAHILDGLALLQFFHWCEQKRKTKELFNETEMSLRHKVDYFRSTKKNFIFPSFSTISASGPNAAVIHYECTDKTNATIKPAIYLLDSGGQYLHGTTDVTRTTHFGEPTAEEKRIYTLVLKGHLRLRKVIFASYTNSSALDFIARENLFNNFMDYNHGTGHGVGLTLNVHEGGCSIGPVGGAPLKKNMVLSNEPGYYMKDKFGVRIENMQYVISKEITDTTEYLSFDDLTMYPYEKKLLDFSLLTNQEIKELNEYHTTIRNTLLPLVKQSPQEYGESVEKYLIEITEPIAIHNN

Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. In the food vacuole, involved in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides. In the cytoplasm, may be involved in the last steps of the turnover of ubiquitinated proteins (Probable).

A0A144LUY5

CTCN1_ECHES

Centrocin 1 (EeCentrocin 1) [Cleaved into: Centrocin 1, heavy chain; Centrocin 1, light chain]

MMIKIAVVLCAVMATTMVRAKYVEEQELADLLDLLISEEVSSPDDAVALQGWWRRTVDKVRNAGRKVAGFASKACGALGHSPQEARAKVLEAFPEMKEADLDEEDIGKYCGYAHALNGR

[Centrocin 1, heavy chain]: Has antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and against fungi with minimum inhibitory concentration (MIC) between 0.78 uM and 50 uM. Shows little hemolytic activity even at a concentration of 100 uM. [Centrocin 1, light chain]: Has no antimicrobial activity. Shows no hemolytic activity.

A0A144LVL3

CTCN2_ECHES

Centrocin 2 (EeCentrocin 2) [Cleaved into: Centrocin 2, heavy chain; Centrocin 2, light chain]

MMIKIAVVLCAVMATSMVFANDVKEQELADLLDLLISEEVSSPDDAVAESWGHKLRSSWNKVKHAVKKGAGYASGACRVLGHSPQEARAKVLEAFPEMKESDLDEEQVGKYCAVAHAIHGR

[Centrocin 2, heavy chain]: Has antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and against fungi with minimum inhibitory concentration (MIC) between 0.78 uM and 50 uM. Shows little hemolytic activity at concentrations up to 12.5 uM but >50% lysis at 100 uM.

A0A145P7T2

RAM1_LOTJA

GRAS family protein RAM1 (Protein REDUCED AND DEGENERATE ARBUSCULES) (Protein REQUIRED FOR ARBUSCULAR MYCORRHIZATION 1) (LjRAM1)

MINSMCGSSVSLKSENSRNKPQPTSPNESVLQSKKNATQSSADLEQTSLNLTPPSLNLPALKFDLDGDVEVQSPDSSMWESFFSDHLLDGDFMISSPVRNNVPSPQASTFNSNYNYAHQGIQSQSLSGCSPPRFSSPLGAFNSNKGKGLSPLHRVFNSPNNQYMQHVENLALPAIEEFLEEYQGDHGLGGGGGYSNSSNKVSSDIGSSSECFDMQNHIPSMLDSLTMQNSSRYCGSVSEDSSVHGGSSQLSQDSDFYHQMGSMASASLSQALQQERYQEKQQKQHQTQQQQQPQQQQQNLTVPIPIGMDQEQDSGLQLVHLLLACAEAVAKEEYMLARRYLHHLNRVVTPLGDSMQRVAACFTESLSARLAATLTTKPQSISNGTSMPRSSSSSCLSPFPSNSIEVLKIYQIVYQACPYVKFAHFTANQAIFEAFEAEERVHVIDLDILQGYQWPTFMQALAARPGGAPFLRITGVGPCIDSVRETGRCLTELAHSLRIPFEFHPVGEQLEDLKPHMFNRRVGEALAVNTVNRLHRVPGSHLGNLLSMIRDQAPNIVTLVEQEASHNGPYFLGRFLEALHYYSAIFDSLDATFPPESAQRAKVEQYIFAPEIRNIVACEGAERIERHERLEKWRKIMEGKGFRGVALSPNAVTQSRILLGLYSCDGYRLTEDKGCLLLGWQDRAIIAASAWRC

Transcription factor acting as a central regulator of arbuscular mycorrhiza (AM)-related genes (e.g. PT4) required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis). Also involved in restricting mycorrhizal colonization of the root meristem (By similarity).

A0A151V4J3

AA13_MAGO7

Lytic polysaccharide monooxygenase 13A (LPMO 13A) (EC 1.14.99.55)

MKWSVIQALALASGVQAHGYLTFPMSRTGLNAQAGPDTCPECTILEPVTAWPDLDSAQVGRSGPCGYNARVSVDYNQPGPRWGSAPVVTYKGGDVADVQWCVDNNGDHGGMFTYRICQDQALVDKLLTPGYLPSEAEKQAAENCFRAGTLPCTDVNGQSCGYSPDCSPGQACWRNDWFTCKGFQDTKCRGVDNAPLNSCYTSIAGGYTVSSRIKIPNYVSNHTLLSFKWNSFQTPQIYLTCADIKITAPDSQSPPTTTTTSTPASPPPTSCATPAASVAVTFRSKTTTSVGQTVKIAGSIAQLGGWDASKAPALSASQYTSSNPLWTTTISLPAGATFEYKFIRVESSGAVTYESGANRVYTVPRDCAGTATVDTAWK

Starch-active lytic polysaccharide monooxygenase that oxidizes the C1 position of starch substrates.

A0A163UT06

SET17_CAEEL

Histone-lysine N-methyltransferase set-17 (EC 2.1.1.-) (EC 2.1.1.364) (SET domain-containing protein 17)

MNIKHNYISYFQMNGIQIPGISNPEAIIPITGEKKSYKLVLDFNDGAISIIEARYLDSKLHREIQDLSDNDVTILGTEISDGAYDENLDIHCDKCNKFYRPYCRLHPLFKIPDRVLKRDESSNLSFSQQTLPILFRIEESKLPNAGLGVIAEVFIPVGMVFGPYKGRRCQKKTDFYKDGYAWLIKSGDKRFYIDGSDAERSNWLRYINSPRFEDEQNMLAFQTNGKIFYRVIKPIRINQELLVWYGSSYGNEFVESENGNKYKKPAKNPFICVGAQR

Histone methyltransferase that specifically mono- and di-methylates 'Lys-4' of histone H3 in vitro. Does not tri-methylate 'Lys-4' of histone H3 in vitro. Promotes spermatid development and fertility by positively regulating the transcription of spermatocyte-specific genes in primary spermatocytes. Together with spr-5, required for transgenerational fertility.

A0A166U5H3

BMT_KITPR

Bergaptol O-methyltransferase (PpBMT) (EC 2.1.1.69)

MAGMKTSPSQDEEACVLAIQLATSTVLPMILKSAIELDILNTISKAGPGNYLSPSDLASKLLMSNPHAPIMLERILRVLATYKVLGCKPSELSDGEVEWLYCWTPVCKFLSNNEDGASIAPLLLVHQDQVPMKSWYHLTDAILDGGTAFNKAYGMNIFDYASQDPQFNKVFNRSMAGHSTITMKKILETYNGFEGLKSIVDVGGGSGATLNMIISKYPTIKGINFDLPHVVGDSPIHPGVEHVGGDMFASVPKGDAIFLKWIFHSWSDEDCLRILKNCYEALADNKKVIVAEFIIPEVPGGSDDATKSVVHLDAVMLAYVPGGKERTEKEFEALATSAGFKSFRKVCCAFNTWIMEFSK

O-methyltransferase involved in the biosynthesis of furocoumarins natural products such as bergapten, a photosensitizer used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses. Catalyzes specifically the methylation of bergaptol. Not active on xanthotol, isoscopoletin, scopoletin and esculetin.

A0A172J1V3

PHZM_LYSAN

Phenazine O-methyltransferase PhzM (EC 2.1.1.-) (SAM-dependent O-methyltransferase)

MTENNRAGAVPLSSILLQMITGYWVTQSLYVAAKLGIADLVADAPKPIEELAAKTGAKAPLLKRVLRTIASIGVFTETEPGIFGITPLAALLRSGTPDSMRPQAIMHGEEQYRAWADVLHNVQTGETAFEKEFGTSYFGYLAKHPEADRVFNEAQAGYTKQVAHAVVDAYDFSPFKTVIDIGAGYGPLLSAILRSQPEARGILFDQPHVAQAAGKRLAEAGVGDRCGTVGGDFFVEVPADGDVYILSLLLHDWDDQRSIEILRNCRRAMPAHGKLLIVELVLPEGEEPFFGKWLDLHMLVLLGAQERTADEFKTLFAASGFALERVLPTASGLSIVEARPI

Involved in the biosynthesis of phenazine natural products including myxin, an N(5),N(10)-dioxide phenazine antiobiotic, which has antimicrobial activity. O-methyltransferase, which converts iodinin (1,6-dihydroxyphenazine N(5),N(10)-dioxide) to myxin (1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide). Catalyzes both monomethoxy and dimethoxy formation of phenazine natural compounds. Acts on a wide variety of substrates, catalyzing O-methylation of phenazines with non-, mono- or di-N-oxide. Highest activity with 1,6-dihydroxyphenazine (DHP) as substrate. Less active with monohydroxy-containing and monohydroxy-monomethoxy-containing phenazines. Least active with non-phenazine substrates, such as 8-hydroxyquinoline and 6-hydroxyquinoline. Is not able to convert 1-hydroxyphenazine to 1-hydroxy-N5-methylphenazine (pyocyanine), hence does not function as an N-methyltransferase.

A0A172U6X0

LR3E_METSD

L-ribulose 3-epimerase (LRE) (EC 5.1.3.31) (MetLRE)

MAFPKRLEYGGHALVWSGDWSAAGARKAIAGAARAGYDYIEIALLDPWQIDVALTKDLLQEYNLRAHASLGLSAATDVTSTDPAIVAKGDELLRKATDVLYALGGSELCGVIYCALGKYPGPASRENRANSVAAMQRLADYAADKGINIDLEVVNRYETNIMNTGLEGLAFLDEVNRPNAFLHLDTYHMNIEENGMAKSVLAAGDRLGYVHIGESHRGYLGTGNVDFASFFAALKQIDYRGPITFESFSSEIVDPKLSNTLCVWRNLWHDSDDLAGKALEFIKQRY

Catalyzes the epimerization of various ketoses at the C(3) position. Exhibits the highest enzymatic activity toward L-ribulose, followed by D-ribulose, D-allulose and D-fructose. Shows lower activity with L-xylulose, L-tagatose, D-xylulose, D-tagatose, L-sorbose, D-sorbose, and weak activity with L-allulose and L-fructose.

A0A178VEK7

DUO1_ARATH

Transcription factor DUO1 (Myb-related protein 125) (AtMYB125) (Protein DUO POLLEN 1)

MRKMEAKKEEIKKGPWKAEEDEVLINHVKRYGPRDWSSIRSKGLLQRTGKSCRLRWVNKLRPNLKNGCKFSADEERTVIELQSEFGNKWARIATYLPGRTDNDVKNFWSSRQKRLARILHNSSDASSSSFNPKSSSSHRLKGKNVKPIRQSSQGFGLVEEEVTVSSSCSQMVPYSSDQVGDEVLRLPDLGVKLEHQPFAFGTDLVLAEYSDSQNDANQQAISPFSPESRELLARLDDPFYYDILGPADSSEPLFALPQPFFEPSPVPRRCRHVSKDEEADVFLDDFPADMFDQVDPIPSP

Transcription activator that acts as a positive regulator of male germline development by promoting both gametic cell specification and cell cycle progression. Binds to canonical MYB sites 5'-AACCGTC-3', 5'-AAACCGC-3' and 5'-AACCGT-3' in promoters to trigger the expression of male germline-specific or enriched genes (e.g. MGH3, GEX2 and GCS1), including those required for fertilization. Required for sperm cell specification leading to pollen maturation by activating a germline-specific regulon. Involved in pollen mitosis entry at G2-M transition via the regulation of CYCB1-1, DAZ1 and DAZ2 expression.

A0A178WF56

CSTM3_ARATH

Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 3 (AthCYSTM3)

MAQYHQQHEMKQTMAETQYVTAPPPMGYPVMMKDSPQTVQPPHEGQSKGSGGFLRGCLAAMCCCCVLDCVF

Regulates negatively salt stress responses and Na(+) homeostasis. Prevents Na(+) efflux, disturbs reactive oxygen species (ROS) homeostasis, and represses the expression of nuclear salt stress-responsive genes. Involved in resistance to abiotic stress.

A0A193AU77

GGT24_PUNGR

Gallate 1-beta-glucosyltransferase 84A24 (EC 2.4.1.136) (UDP-glucose:gallate glucosyltransferase) (UDP-glycosyltransferase 84A24) (EC 2.4.1.120, EC 2.4.1.170, EC 2.4.1.177, EC 2.4.1.194, EC 2.4.1.81)

MGSESLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNIGEEPSPIGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKEVIPRMIKKNEEQNRPVSCLINNPFIPWVSDVAESLGLPSAMLWVQSCACFAAYYHYYHGLVPFPSESAMEIDVQLPCMPLLKHDEVPSFLYPTTPYPFLRRAIMGQYKNLDKPFCVLMDTFQELEHEIIEYMSKICPIKTVGPLFKNPKAPNANVRGDFMKADDCISWLDSKPPASVVYVSFGSVVYLKQDQWDEIAFGLLNSGLNFLWVMKPPHKDSGYQLLTLPEGFLEKAGDKGKVVQWSPQEQVLAHPSVACFVTHCGWNSSMEALSSGMPVVAFPQWGDQVTDAKYLVDVFKVGVRMCRGEAENKLIMRDVVEKCLLEATVGPKAAEVKENALKWKAAAEAAVAEGGSSDRNIQAFVDEVKRRSIAIQSNKSEPKPVVQNAAVADHFGAKATTNGVAADLAGSNADGKVELVA

Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins).

A0A193AUF6

GGT23_PUNGR

Gallate 1-beta-glucosyltransferase 84A23 (EC 2.4.1.136) (UDP-glucose:gallate glucosyltransferase) (UDP-glycosyltransferase 84A23) (EC 2.4.1.120, EC 2.4.1.170, EC 2.4.1.177, EC 2.4.1.194, EC 2.4.1.81)

MGSESSLVHVFLVSFPGQGHVNPLLRLGKRLASKGLLVTFTTPESIGKQMRKASNISDQPAPVGDGFIRFEFFEDGWDEDEPRRQDLDQYLPQLEKVGKVLIPQMIQKNAEQGRPVSCLINNPFIPWVSDVAETLGLPSAMLWVQSCACFLAYYHYYHGLVPFPSENAMEIDVQLPSMPLLKHDEVPSFLYPTTPYPFLRRAILGQYKNLEKPFCILMDTFQELEHEIIEYTSKICPIKTVGPLFKNPKAPNTTVKGDFMKADDCIGWLDSKPASSVVYVSFGSVVYLKQDQWDEIAYGLLNSGVNFLWVMKPPHKDSGYTVLTLPEGFLEKAGDRGKVVQWSPQEQVLAHPATACFVTHCGWNSSMEALTSGMPVVAFPQWGDQVTDAKYLVDEFKVGVRMCRGEAEDKLITRDVVEQCLREATQGPKAAEMKKNALKWKAAAEASFVEGGSSDRNLQAFVDEVKRRSIEITASKPAVKAAPNGVVAAAESVVETKANGKVELAA

Glucosyltransferase that catalyzes the formation of 1-O-beta-D-glucose esters with hydroxybenzoic acids and cinnamic acid including its derivatives as preferred glucosyl acceptors. Has significant activity with gallic acid (3,4,5-trihydroxybenzoic acid), 3,4-dihydroxybenzoic acid, 4-hydroxybenzoic acid, cinnamic acid, sinapic acid, coumaric acid, caffeic acid and ferulic acid in vitro. Gallic acid is the predicted native substrate of the enzyme, which thus catalyzes the formation of 1-O-galloyl-beta-D-glucose, the first committed step of hydrolyzable tannins (HTs) biosynthesis, with punicalagin isomers being the major HTs of pomegranate. Catalyzes the formation of flavonoid glucosides with genistein, apigenin and luteolin in vitro. Has low activity with benzoic acid, 2-hydroxybenzoic acid, 3-hydroxybenzoic acid, 2,4-dihydroxybenzoic acid, naringenin and quercetin. No activity with catechol, resveratrol, chlorogenic acid, catechin and epicatechin (building blocks of proanthocyanidins) or cyanidin, delphinidin and pelargonidin (the three anthocyanidins).

A0A193KX02

TOMT_DANRE

Transmembrane O-methyltransferase homolog (EC 2.1.1.6) (Protein mercury)

MVSPAIALAFLPLLLTLIIRYRYYFVLLYRAVLTRWVRDCLSGISREERAFQYILTHATPGDSQSILDTFDTWCSKVEFISNIGPKKGKILDRLLQENCPITVLELGTHCGYSTVRMARSLPIGARIYSVEMDQRNAQVAEKIIRLAGFDDDMVELIQRPSDEVIPRLREDLGVERLDLVLMDHWKRCYLPDLHLLEDSGLIGQGSIILADNVIFPGAPNFLRYARRCGLYEVRVHRATLEYMRGIPDGMAELTYIGIK

Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function. Component of the hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity.

A0A1B0GTW7

CIROP_HUMAN

Ciliated left-right organizer metallopeptidase (EC 3.4.24.-) (Leishmanolysin-like peptidase 2)

MLLLLLLLLLLPPLVLRVAASRCLHDETQKSVSLLRPPFSQLPSKSRSSSLTLPSSRDPQPLRIQSCYLGDHISDGAWDPEGEGMRGGSRALAAVREATQRIQAVLAVQGPLLLSRDPAQYCHAVWGDPDSPNYHRCSLLNPGYKGESCLGAKIPDTHLRGYALWPEQGPPQLVQPDGPGVQNTDFLLYVRVAHTSKCHQETVSLCCPGWSTAAQSQLTAALTSWAQRRGFVMLPRLCLKLLGSSNLPTLASQSIRITGPSVIAYAACCQLDSEDRPLAGTIVYCAQHLTSPSLSHSDIVMATLHELLHALGFSGQLFKKWRDCPSGFSVRENCSTRQLVTRQDEWGQLLLTTPAVSLSLAKHLGVSGASLGVPLEEEEGLLSSHWEARLLQGSLMTATFDGAQRTRLDPITLAAFKDSGWYQVNHSAAEELLWGQGSGPEFGLVTTCGTGSSDFFCTGSGLGCHYLHLDKGSCSSDPMLEGCRMYKPLANGSECWKKENGFPAGVDNPHGEIYHPQSRCFFANLTSQLLPGDKPRHPSLTPHLKEAELMGRCYLHQCTGRGAYKVQVEGSPWVPCLPGKVIQIPGYYGLLFCPRGRLCQTNEDINAVTSPPVSLSTPDPLFQLSLELAGPPGHSLGKEQQEGLAEAVLEALASKGGTGRCYFHGPSITTSLVFTVHMWKSPGCQGPSVATLHKALTLTLQKKPLEVYHGGANFTTQPSKLLVTSDHNPSMTHLRLSMGLCLMLLILVGVMGTTAYQKRATLPVRPSASYHSPELHSTRVPVRGIREV

Putative metalloproteinase that plays a role in left-right patterning process.

A0A1B1J8Z2

CHIT5_LOTJA

Class V chitinase CHIT5 (LjCHIT5) (EC 3.2.1.14)

MIIKLLVALIHYLHETMAVQSIITTPLLVILMSLRSYAFTEPSLHRQQPPSKGGVRAAYWPAWSDFSTSSIDTNYFTHIYYAFVQPAPESFNLEITESYKKWAPKYDGIHNIRPRVTTLLSIGGGGNNATLFSEMASSKQNRASFINSTIHVARKHEFNGLDLDWEWPGDEKDMSNLALLLKEWYKALVVEANTSRKSRLLLTSAVYFNSTISLIGNGPRSYPVRAIRKYLDWASPMCFDYNGAWANETGFNAALYDPNSNISTKYGIGSWIGSGVPAEKLVMGLPLYGRAWELKDPNDHGVGAKAVGPAVDTDGSMDYDEILVFNKDTGAKVVYDEVAVSFYSYSGTTWIGYDDGPSITKKVQFARSMGLKGYFFWAIGKDKDWTISKQASNAWGY

Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5. Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules. Has the capacity to inhibit hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay. Involved in symbiotic signaling. Required for root hair infection threads (ITs) elongation and nodule development. Possesses Nod factor (NF) hydrolase activity. NFs are lipo-chitooligosaccharide signaling molecules produced by nitrogen-fixing rhizobia to initiate nodulation (symbiosis) on the roots of legumes. Modulates NF levels and signaling to complete transition of infected nodules to functional nitrogen-fixing organs.

A0A1B1WAJ0

RAD1_LOTJA

GRAS family protein RAD1 (Protein REQUIRED FOR ARBUSCULE DEVELOPMENT 1) (LjRAD1)

MSPPLYSVLLEDENSVFLLDLDLSSPMGFHAYPHLPILDSSIANWSLPFSISDETFRESKKLKRTMIPISSADFSISSSSSLSVSVNSIPRLNFRDHIRTYKRYLAAEELPEDTNSSESVVGAEEDGCADGMRLVQLLIACAEAVACRDKAHASMLLSELKSNALVFGSSFQRVASCFVQGLAERLTLIQPIGSGAGVSQSMMNIMDAASEEMEEAYRLVYETCPHIQFGHFVANSTILEAFEGESFVHVVDLGMSLGLPHGHQWRGLIHSLANRASGHGRVRRLRITAIGLCIARLQAIGDELSDYANNLGINLEFSVVQKNLENLQPEDIKVNDDEALVVNSILQLHCVVKESRGALNSVLQMIHGLSPKVLVMVEQDSSHNGPFFLGRFMESLHYYSAIFDSLDAMLPKYDTKRAKMEQFYFAEEIKNIVSCEGPLRMERHERVDQWRRRMSRAGFQAAPIKMVAQAKQWLLKNKICDGYTVVEEKGCLVLGWKSKPIVAASCWKC

Transcription factor acting as a regulator of arbuscular mycorrhiza (AM)-related genes (e.g. PT4, STR and RAM2). Required for the morphogenesis of arbuscules upon symbiosis with AM fungi (e.g. Rhizophagus irregularis). Also involved in restricting mycorrhizal colonization of the root meristem.

A0A1B4XBK0

SDNC_SORAA

Geranylgeranyl diphosphate synthase sdnC (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl pyrophosphate synthase) (GGPP synthase) (GGPPSase) (Geranyltranstransferase) (EC 2.5.1.10) (Sordarin/hypoxysordarin biosynthesis cluster protein C)

MSFDQFAPFMTLGRPDAVCDECSRPVAPNSISDDDAAVNTTETDTQHANIPEEQDVINIKLDSTFNAESSAETIDLKVEGVKLAIVSQQPTYEAITAETTSSVATSEEASSDTATSLTNLTSREPSPSSSSASSVAEECPSEEPASDDTVPAASEKNHPDGTLNPNYHDARADEVHPQHEVVQVQAPHLPPPQGVQPAATENPDHDSLFSVFTQDHNPLLSGTIVGAPADYVASTPGKKIRDKAASALNIWLQVSPDDLNQIRTVIDMLHNASLILDDVEDGSVSRRGRPATHMIFGMPQAINSAGYQINRAMMEVLKLGSQDCLEIFIEELDRLYIGQGYDLFWTFNIKRPSVEKYISMVDYKTGSLFNMLVRFMAAKTGAKGGVETDNNKAPIAPPDLTRLVVLLGRYFQIRDDYMNLTSDEYTLQKGFCDDLDEGKFSLTLVHALENSPEAEKSILRHLLTQRLSSNGQGMSLAQKHLVIDIVKGAGSLEYTVTALRKIGMEIVNELDQIEGVTGIENKELRRLVEVLRV

Geranylgeranyl diphosphate synthase part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure. First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate. The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene. Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF and sdnH to give a hydroxylated cycloaraneosene derivative such as cycloaraneosene-8,9,13,19-tetraol. Although the order of the hydroxylations is unclear, at least C8, C9 and C13 of the cycloaraneosene skeleton are hydroxylated before the sordaricin formation. Dehydration of the 13-hydroxy group of the hydroxylated cycloaraneosene derivative might be catalyzed by an unassigned hypothetical protein such as sdnG and sdnP to construct the cyclopentadiene moiety. The FAD-dependent oxidoreductase sdnN is proposed to catalyze the oxidation at C9 of the hydroxylated cycloaraneosene derivative and also catalyze the Baeyer-Villiger oxidation to give the lactone intermediate. The presumed lactone intermediate would be hydrolyzed to give an acrolein moiety and a carboxylate moiety. Then, [4+2]cycloaddition would occur between the acrolein moiety and the cyclopentadiene moiety to give sordaricin. SdnN might also be involved in the [4+2]cycloaddition after the hypothesized oxidation to accommodate the oxidized product and prompt the [4+2]cycloaddition. GDP-6-deoxy-D-altrose may be biosynthesized from GDP-D-mannose by the putative GDP-mannose-4,6-dehydratase sdnI and the short-chain dehydrogenase sdnK. The glycosyltransferase sdnJ catalyzes the attachment of 6-deoxy-D-altrose onto the 19-hydroxy group of sordaricin to give 4'-O-demethylsordarin. The methyltransferase sdnD would complete the biosynthesis of sordarin. Sordarin can be further modified into hypoxysordarin. The unique acyl chain at the 3'-hydroxy group of hypoxysordarin would be constructed by an iterative type I PKS sdnO and the trans-acting polyketide methyltransferase sdnL. SdnL would be responsible for the introduction of an alpha-methyl group of the polyketide chain. Alternatively, the beta-lactamase-like protein sdnR might be responsible for the cleavage and transfer of the polyketide chain from the PKS sdnO to sordarin. Two putative cytochrome P450 monooxygenases, sdnQ and sdnT, might catalyze the epoxidations of the polyketide chain to complete the biosynthesis of hypoxysordarin. Transcriptional regulators sdnM and sdnS are presumably encoded for the transcriptional regulation of the expression of the sdn gene cluster.

A0A1C3NSL9

AJM1_CAEEL

Apical junction molecule

MSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAESEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHKLADADRDQEEELVFNEERRKTVTMDDNASLRSASITFDANRDEQDLLNESFASNPTDETVLMQKTKDEMDATSERPRSPLDLPPPPASVVLHPSAPPPPPPPLSSTEVVGNTTTTTTTHYAPKTWNDPSITTAPKIPVSLLSGAQPLPSVLTQRTTTSSYSAPNYSASSMSGVPSDVAPPPPLPIPNQSSSSAASYQHHHASSISKSISSSREDLLSEHATSRSTVREIPVHRAPSTAPSHSSVFEYHMMPTTTSTYHHVETPSDEYYRREVMTRTIITRSTEALSQTPLGRPASPLDRYLPYPTTTTTTSGDGRTREEKTVDYKVTYHRDIEEQERRIREDQARRQQEEQDRRDREDNARRILAQREHQEMERLREQQNLSERALAERERADKERLQQERLLRQQREKKRREEWDRLESIRLAEEEAELARRRALEKERIDREKAEEERKTMERLERERARLERERLEEERRQKEKAETERIERERREHERIEIERIERIKRERIERERREREEKKAEEDRLLRERLELERIERERRELEARERQELELQRREAEDRERQRLEDEAREMRRREEERREAELVADVHRQAEERERLRKRQEREEAERLERIRLEQQKIDMERIDAERRERERKEEERREFELIEAARRKKEARDRDRLDEMERERVREEEERREKERREQERRIAAEKERKRRQEEEEEIARLNELQRAAAARQAQRNAELDRQRQRDELDRKAQELSEREMREKERRDRERANEEAQLADLLERERHNQLIRENERREAVERANNRRLEDRRSRDKLDHIVRERSEKEQFELEKRRLLAEKEAMNRKKNHLLSSETLAKLTQPMYYTTREPEVTTKVERQVIERIDRNVWVEDVPYAPSQSAMGYLDNDENNRDRLYNPNDLNRNGSSRSRYQRAKNEKARRDFYHSSQDSADPVTERFRKSTDDLTTRSRPEYRGPLLQKFHDSEFRTTALNETDGLPYRRMGPSPYEQPFAKLLEETERRYAHYNSRASNPSIYQSSRYYYPERHGQPQHTDNTRAESVVAYERESRRESPADQAHIRSRSADYLMDRRIREETEVPENQLQKTRVEPHDQSPRESRISEYEMRFRKSTEKLTVPDWYRENRPQGQTAQTSTYRYGNGVEPMSTTTTTTTVINGTSSHQQAPPPVPPQPIGNIGLPRGMFDRYKDDIEELRRSRSSLHQTGQQETSNRQGSTLSVGGIVDQGHALPGYTVSEVPNAWNLHTSRTSRVVEVADTFVGTSSHEYGNFTNRYGGRVTIEEVLDSIFQKVTPTNQRLNFDRSYPQADELFQGNVDGPGIYTNNYSVMRQVLKSPERAEHILQNEELFVRCTECHRTRELSAARLFFVSCKHCYTYYCSRECRHNNWPNHSGRCSFARINTLCKDVIMKVREDEQAQAFMSKVARDGFSVSGRGSVNIRLSSPQLAQAYVSNGWRALSAYPNDQLLYYYTVKALIAERKEPSLIALCNRYEPREKFILSVSIIADIEHCPETPPPETRELSAVQFSSPRSRYEAIQNQNAPYFSEFAHNV

Controls adherens junction integrity. Required for the correct rate and completion of elongation of the embryos.

A0A1C7D1B7

ELP3_DEHMC

tRNA uridine(34) acetyltransferase (EC 2.3.1.-) (Elongator complex protein 3 homolog) (DmcElp3)

MKKLSRTISGVTPVAVMTKPLPCPGKCIYCPTFAATPQSYTPESPAVLRAKSCEYQAYKQVALRLRIIQDMGHPTDKVELIIMGGTFLSADITYQYGFIKDCYDALNGVVAGSLEEAKTINETAQHRCVGLCIETRPDICGKAEIQRMIDFGTTRVELGVQMLDDDIYKLVERGHRVSDVAEATCLLREYGLKVHYHWMPGLPGSSPEKDLALSRMVFEDPRFCPDGLKLYPTMVVEGTILEQWWKEGRYTPYPNGTMTGLIADIKALVPPYVRISRVLRDIPAVFISAGLKDSLRDGVRQILESRHQKCRCIRCREYGHRQRKGQTSGEPTLRRLDYPASGGKEIFLSFEDASDTLYGLLRLRIPCASLPVLGQKYGAKTGLVRELHVYGTELSLGEQGDQSAQHRGLGRKLLAEAECLARDEFGLDSLAILSGVGAREYYRSLGYELVAGYMCKHLD

tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not show protein lysine acetyltransferase activity (By similarity).

A0A1D5NS60

ZN16L_DANRE

Zinc finger protein 16-like (Zinc finger protein 697-like)

MSRKRNHCYMETGASSESQGAFVDSAGPFSRDEEDFSELEPDEQLVCSVTEITEHLGRNITVVLESALSEIRKLVGVRIRVLKMELREKSDEIELLKAKLESAEKDGRVSNFSSLDFRKSEHQKYGAEPKKAKTGTPVVKKENINAICDYLMKDKNQRGAAEVESDHSNQAFGSERDVRTEAQPHGSLSLWPDSGPADTDAETDIFSMLPSASKRMYDYEWMTGVELNSAEFKGDSETKCEDVPPMDEEDENEDSEEGRGSLRSVSDHFPLDTQGSPGEDRSSPAEDSMDRMEPGQQFTSHTFICPFCGTLCPDSSFLEEHIKLMHHGESLLQSTSAGSSSQAEGDSGEAGPASRGAREKKVEGGYECGDCGRHFNYLGNLRQHQRIHTGEKPFVCPECGERFRHTARLKSHRLSHSGAQSPFPCPQCGKGFPVLSGLKRHQRVHTGESPYACPQCGRRFKELGNLYTHMRIHSGATPYTCYQCGRSFRHLGTYKSHRCMPATQMPSEHSPPWAQEDKVQTGRLQGYV

Probable transcription factor (Probable). Important for development and migration of oligodendrocyte precursor cells, and normal myelination of axons in the central nervous system (CNS). Functions autonomously in oligodendrocytes to promote CNS myelination. Seems to act in parallel with notch3 during oligodendrocyte development.

A0A1D5NSK0

CIROP_DANRE

Ciliated left-right organizer metallopeptidase (EC 3.4.24.-) (Leishmanolysin-like peptidase 2)

MSFLLCIGILLLPWFPCVCGKCIFDQIQRSVNVVSPPTAQYASAYRFKTQRSKRHIMPMDNLQPIRIKIWIPSESPALSDWEREKLMSAVGEAVSEVSSLLSVKRVKDRLLLNRDVNKYCKFIWRNSSTLNHMKCGRAHENYRFESCLGVIIPDEHLDGCSVYPNPEHPVPTVLRPRGPGVPDADFLLYVFTHNTEKCRAESSVLAYTAHCQTGSDGRPLAGTMVICRETLKKERYTYQHFVKVTTVIHELFHVLGFSKELLSNWKDFGVDCWSHGQVTSTDQTGQVRLYSPTVIRAMQKHFNSTHTDLGAPLENKDAALDGLSSHWEARVLQGSIMAASLVEASLVRIDAITLAALQDTGWYSVNHSRAQSLVWGEGEGSDFGSVSACHNSSAFFCTGSGLGCHFLHLNKGECVTDQYLDGCHIFKPLANASECWIEDNARSGMNEGGGEIFGSDSRCFISNITRLNNVTAYTPVSGHCYRHRCTGINKYHIQVKDSDWMDCPAGTSIEVSGYQGFIFCPENRLCKYSDLAPPTSTQRTESLFSDTTAQSDLGMMEKDAAVQPSFTSLFLVSEAKISLAAVLSLMAVFALLSAAVLLYRKNLSVRVHAASYRTPLPHILYRN

Plays an essential role for patterning the left-right axis. Requires solely on the left side, downstream of the leftward flow, but upstream of dand5, a nodal inhibitor involved in left-right patterning.

A0A1D5NY17

TM182_CHICK

Transmembrane protein 182

MKLSVGIFFGGLFAALGVLLFLVAFGTDYWLLATEIGRCSKAPEDAGTEKATFHHEGFFWRCWFSGNVREHNTSMWKFWYTNQSPSKNCTHAYLSPFPHIRDEHNSTSYDSAVIYRGFWTVLMLLGVITIVMASFLIICAAPFASHILYKAGGGFYILAGVLFSLVVVMYVIWVQAMADLENYTNMKKMDCPDFAVYVRYGWSFMLAPIGVFFALLAGMLFLLVGRAIYLNSD

Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1. Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis.

A0A1D5PPP7

CASP6_CHICK

Caspase-6 (CASP-6) (EC 3.4.22.59) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]

MSGAERRPAAGRVQLDSKPTPTTTADGNQNITEVDAFDKRQTFDPAVQYKMNHQRRGVALIFNHEHFFWHLRLPDRRGTLADRNNLKRSLTDLGFEVRIFDDLKAEDVLKKVFEASRDDYSNADCFVCVFLSHGENDHVYAYDAQIKIETITNMFRGDKCQSLVGKPKIFIIQACRGDKHDDPVLVQDSVDSKDETTVNQTEVDAAGVYTLPAGADFIMCYSVAQGYFSHRETVNGSWYIQDLCEALGKHGSSLEFTELLTVVNRKVSHRKVDICRDINAIGKKQIPCFASMLTKKLYFHPKSK

Cysteine protease that plays essential roles in programmed cell death, development and innate immunity. Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein lamin-A/LMNA thereby inducing nuclear shrinkage and fragmentation. Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution. Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity. PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis (By similarity).

A0A1D5PRR9

FANCM_CHICK

Fanconi anemia group M protein (Protein FACM) (EC 3.6.4.13) (ATP-dependent RNA helicase FANCM) (Fanconi anemia-associated polypeptide of 250 kDa) (FAAP250) (Protein Hef ortholog)

MSGGRQRTLPEAWRRAAGPALQAGRDADGNDDDDDELLAAAAAELDPDPNPNVDPNPGPGPEAAAGGFCAAAGALWIYPTNRPERPYQLRMARAALFANTLLCLPTGLGKTFVAAVVMYNFYRWFPSGKVLFLAPTKALVAQQMEACAQLMGIPGRDMAEMTGGTQALSRRELWASRRVFFLTPQIMVNDLSRGTCPAVEVKCLVVDEAHKALGNHAYCQVVKELSRYTTQFRVLALTATPGSDTKAVQQVVSNLLIAQIELCSEDSPEIQPYSHERQVEKIVVPLGEELGGIQRAYIHVLETFAGRLIKLGVLARRDVPSLTKYQIILARDQYRKNPSPQNVGMQPGIIEGDFALCISLYHGYELLQQMGVRSLFIYLCGIMDGSKGLTRTKNELGRNEDFMRLYQQLTDMFSDTCQTSANGNLHKSRTVSENKKEFIYSHPKLKKLEEIVIEHFKSRKMGCSDQTTSGGTCVDTRVMIFSSFRDSVQEIAEMLSRFSPVVRVMTFVGHSTGKSTKGFTQKEQLEVVKRFREGGYNTLVSTCVGEEGLDIGEVDLIICFDAQKSPIRLVQRMGRTGRQRQGRVVVILAEGREERTYNQSQSNRRSIQKAISGNKMLHFYQHSPRMIPEGINPELHRMFITAEKYKPNDSGRLPKGRPSSLHHKSALFSCVTDPKEMHCHENWSLSPEEFEIWDRLYRLKENDGVKEPILPHTRFETLENLDKTSKPEEEAAHKLSLSEWSIWQSRPFPTSMVDHSDRCYHFISVMELIEVMRQEQGDCSYELELQPHLRIEDIHVRRNKGHLSTTSSAFAQKTHSSKRDMARTKRPFVPDVNDNEREFFSIFKTTNTKTPRTAPGLDLEEPELPTDTNGSEPCSARRLTLVASTDQGSPKEEEIEKVTFDLNEFNDLCDDGESTVAHESAAVKDLRLLDKHCSSVGLNHTDLGYSSFTAEKSPASSDLFYLPESHVDSFVLVSSSAELAGLEGAFSCVKGLLAHSPPPVSKLEGIEELLRHEETLCPLPKVSCRSYSGQLPHGDFPSSLAVDQSLLPAESPELEVTIGLSAAVNTCVSKPASTPTAAGGAEERPPGGGSFHSLLGKEGFTANHTDNPPNKHFVQGDEEDSEMKRDVTIDGEKSIHLFEDEHTYKVNDEMPSVDVEPLLRLGSGGHTARPSAGPASQQPPSGDSPRGDTACGEGAARGEMAPGGAWGRGSAAEQALHNSELCDYSQELFSVNFDLGFSIEECEEEIFEGDTDAMNTPKLNSASRSRADVQLTANRKSLNDGCRVQTPPKWDCKGLKGRNISTPLPLQSGHVRDTAVPGGTAGGRTGRGSPGASPPSPATPTGRRVSSAEATRRIRKKVFSTVREETPEVCPTDKVNPNSQRNSFGSSASDALHTTGGRTENLEGTNLHTSRVFPAEGTSSESEEEIVFQRKNRRNNVLRSPDVGSDSDFGSPVCAVRKRRHPLTVSDVSSDDGVDFHKNPNRGTRGCSAAGSKAQLRGVKRQKVRSKVTCKNAARQFLDEEAELSQQDESCVSSDETEDTDKELSSSLAQFLNDDAEVTQVLNDSEMRGVYLKSVRSPALGSRYRMVHREFNSTEIFSQIPEQDEAYAEDSFCVAEGDEETCNKSESSEEEEVCVNFDLLNNESFGGGGGRYLTRRRKKLHGANMEQNCSAPVQKKPSRIIVLSDSSGEETNVSNEKGTAAHCSRAGRENAELLTSMPSVSSVPHKKSAGDVSAHQSAESKSGMLLGLKASVSEVLDFHPGPRSGSGKEALQAAAQHLQLESSVKNSAGNAPGATKASPALLDGDTALCVLVDSREISSGADVISSLKAVHGLKVQVCSLGSGDYVVSNRMAVERKFQSELLSSVNRTKVTQRLQRLQGMFERVCVIVEKDRTRPGETSRFSQRTQHYDATLAALLQAGIRVLFSSCQEETAVLLKELALLEQRKNAAICVPTEVEGHKQEMLNFYLSLPNISYLAALNMCHHFSSVRTMVNSSPSDIAAGARVSLQRAEETYRYLRYGFDTQMLPESLCAKGKSNTATRS

DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (By similarity). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates (By similarity). Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork (By similarity). This activity is strongly stimulated in the presence of CENPS and CENPX (By similarity). In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates (By similarity). In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA (By similarity).

A0A1D5PUP4

RECK_CHICK

Reversion-inducing cysteine-rich protein with Kazal motifs

MAAAVAAWPWALFCLAAVPPLLSPGAAGLSCCYHAKDNLMCRDVCEQILSSKSDSRLKHLLQRAPEYCPESMGEVWGCINSSLPGVLKKSDGWVGLGCCELAIAVECRQACKQASSKNDILKVCRKEYENALFSCINRNEMGSICCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDYACQTACKRILMSMKTELEIVDGLIEGCKTMPLPQDPLWQCFLESSRSVHPGVTVHPPPSTGLDGAKLHCCSKANSSTCRELCTKLYSTSWGSSQSWQEFDRFCEYNAVEVSMLTCLADVREPCQLGCRNLSYCTNFNNRPTELFRSCNSQSDQGAMNDMKLWEKGSIKMPFINIPVLDINKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDHNKFPEGHTAESICELLSPTDDLENCIPLDTYLSPSSLGNIVEDVTHPCNPNPCAANQLCEVNRKGCQSGELCLPYLCVPGCKLGEASDFIVRQGTLIQVPSSAGDVGCYKICTCGHTGLLENCVEMHCVDLQKSCIVGGQKKSHGTSFNIDCNVCSCFAGNLICSTRQCLTEHSSEDERQKFTGLPCNCVDQFVPVCGQNGRTYPSACIARCVGLQDNQFEFGSCISKDPCNPNPCSKNQRCIPKKQVCLTSFGKFECSQHECVPRQLNCDQTQDPVCDTDSVEYSNVCTLYQKGKNLAYRGPCQPFCKSVEPVCGHNGETYSSVCAAYSDRVAVDYYGHCQAVGVLSDYGFHTECAFVKCPQLSATGCKPVIAPGACCPLCAGMLRILYDKDKLDNFARVTNKKPITVLDILEKLRLHVSVPQCDVFGYLSIESEIVILIIPVDQKPKPLQIEACNKEAEKIESLINSDSPTLASHVPLSALIASQVQVSFSISSPSVKVGPVLHCLFISFSFTLLKLMDYI

Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (By similarity). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor (By similarity).

A0A1D5PXA5

TRPV4_CHICK

Transient receptor potential cation channel subfamily V member 4 (TrpV4) (Vanilloid receptor-related osmotically activated channel) (VR-OAC)

MADPEDPRDAGDVLGDDSFPLSSLANLFEVEDTPSPAEPSRGPPGAVDGKQNLRMKFHGAFRKGPPKPMELLESTIYESSVVPAPKKAPMDSLFDYGTYRQHPSENKRWRRRVVEKPVAGTKGPAPNPPPILKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQHIIRREIADEDVRHLSRKFKDWAYGPVYSSLYDLSSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLCAMIIFTLIAYYRPMEGPPPYPYTTTIDYLRLAGEIITLLTGILFFFSNIKDLFMKKCPGVNSFFIDGSFQLLYFIYSVLVIVTAGLYLGGVEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPSSESCSEDHSNCTLPTYPSCRDSQTFSTFLLDLFKLTIGMGDLEMLESAKYPGVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPLFLRRVFRSGEMVTVGKGTDGTPDRRWCFRVDEVNWSHWNQNLGIISEDPGKSDTYQYYGFSHTVGRLRRDRWSTVVPRVVELNKSCPTEDVVVPLGTMGTAEARERRHGQTPSSPL

Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by phorbol esters. Channel activity seems to be regulated by a calmodulin-dependent mechanism (By similarity).

A0A1D6E0S8

WAK17_MAIZE

Wall-associated receptor kinase 17 (ZmWAK17) (EC 2.7.11.1) (Receptor-like protein kinase 12)

MPSRSPACRPRGRNRRSAADAVARPLALALILVSTLPRAAHSQDLALPPVQPRGVRRTMTCDNIPEPFGTRSRGASRLPGFEVTCGPNREAMLSIGGDAYMIDFVSVSGSYVVVFAEPITQVCYDGKGKPTPDTGTGAKSSEGTTTTFTWSLEGTPFTFSKSNKLVNFGCNRTLMANFFIVPGDSSPLYTSCTTTCNTLQISGSCLGEACCEAPMDQVNGAKAFSLSFERTTANGTGEEDGTCSAAFFLDKDETVFTFSGDEVRPLKTALLPPGERRMVLDWAIGSTSCEQTQSYTFEKLCKYGTCVDAPTGAGYLCKCPSGYDGNPYVSDGCQDINECRNYNSNNCTYQNLCNNTLGGYTCSCPENNIGDGYRTGTGCNTTLATPVSPSQQPQGINVCDHPEKNPCTYIKYCIDLEGVVSCACPEGMSGDGRKNGRGCCFSCQKHFPLDTVLGVSLVLMVTTTTAASCYCWAVKKRELGRKRAELFRKNGGLLLQQRFSTITSQGEDQYSSKIFSAEELKAATDNYSESRILGRGGQGTVYKGILPDQTVVAIKKSKVFDESQVEQFVNEIAILSQIDHPNVVKLLGCCLETQVPLLVYEFISNGTLFQHIHNRNATRPLTWEDCLRIAAETADALAYLHSASSIPIIHRDIKSSNILLDGNFVAKIADFGASRSVPFDQTHITTLIQGTIGYLDPEYFQSSQLTEKSDVYSFGVVLAELLTRQKPISAARPEDSCNLAMHLVVLFNKGRLLQEIEPHILAEAGEDQCYAVAELSVRCLNVKGEERPAMVVVASVLQELRRSFTIDQAVGIKDESIQENSEQEEKHLHESRSIPSLQSSEVSTQCSMEAKMSSFC

[Isoform 1]: Kinase that contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection. [Isoform 2]: Secreted protein that contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection. May sense the presence of fungal material and relay the signal to WAK17 isoform 1 (Probable).

A0A1D6EFT8

EDSB_MAIZE

Eudesmanediol synthase (ZmEDS) (EC 4.2.3.197) (Terpene synthase 17) (Terpene synthase 7)

MAPSNIVVQSSSTPPVAGGDEEFAPSVWGDFFVTYATPVSQASEQRMSERAELLKAQVRQAFDAASMDVAGLITYVDTLERLGLDNHFRDLIGAALERIGAEELPEHGGGLHIVALRFRLLRQHGIWVSTDVFDAFREDAGGFCSSLCSDDPRGLLSLYNAAHMAVPGEVVLDDAIAFARGRLLDIISKGEVRSPVSEQITRALDIPLPRFTRRLETMHYIAEYEHEEAHDGLLLELARLNFVLVRALHLRELKDLSLWWRELYNTVKLPYARDRMVEIYFWTCGMLHEEEYSLARMFFAKTFGMVSLMDDTFDVHATLDECHKLKEAMQRWDESEVSILPEYLRLLYIKTLSNFKEFEEILEPNKKYRMAYTKEAYKLCSKNYLKEAIWSNQKYQPSFKEHEELSIMTSGLPMLTILTLMGFGDEATPEAFEWVSSVPEMVRAGSQVTRFLNDLSSYKLGKNKKDMPGSVETYMVENGLTGDEAAAAIAALLENRWRILNQTRMEIDHTLLPAAQVVLNMARANEIIYLHGRDAYTFGADLKDLVTTLFLKQVLPL

Component of the volatile terpenes biosynthesis pathways. Dihydroxylated sesquiterpenoid synthase that generates dually hydroxylated products directly from (E,E)-farnesyl diphosphate, primarily eudesmane-2,11-diol, along with two closely related structural isomers.

A0A1D6HSP4

C92C5_MAIZE

Dimethylnonatriene synthase (EC 1.14.14.59) (Cytochrome P-450 19) (Cytochrome P450 92C5) (Trimethyltridecatetraene synthase) (EC 1.14.14.58)

MELASTMSVAMALAAAIFVVLCSVVASARGRREKALKLPPGPRGWPVLGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHTVVASSADAARLVLRTHDSALADRPDTAAGEITSYGYLGIVHTPRGAYWRMARRLCATELFSARRVESFQDVRAQEMRALARGLFGCAAGRRAVAVREHVAGATMRNILRMAVGEKWSGCYGSPEGEAFRRSLDEAFAATGAVSNVGEWVPWLGWLDVQGFKRKMKRLHDLHDHFYEKILVDHEERRRLAQASGGEFVATDLVDVLLQLSEESTKLESESEARLPRDGVKALIQDIIAGGTESSAVTIEWAMAELLRHPEAMAKATDELDRVVGSGRWVAERDLPELHYIDAVVKETLRLHPVGPLLVPHYARERTVVAGYDVPAGARVLVNAWAIARDPASWPDAPDAFQPERFLGAAAAVDVRGAHFELLPFGSGRRICPAYDLAMKLVAAGVANLVHGFAWRLPDGVAAEDVSMEEHVGLSTRRKVPLFAVAEPRLPVHLYSATE

Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (By similarity). Component of the volatile terpenes biosynthesis pathways. Converts mainly nerolidol to dimethylnonatriene (DMNT) and, to a lower extent, geranyllinalool to trimethyltridecatetraene (TMTT).

A0A1D6IEG9

CRP1_MAIZE

Pentatricopeptide repeat-containing protein CRP1, chloroplastic (Protein CHLOROPLAST RNA PROCESSING 1)

MPASLLPPTFLPHHLRRLAPAGCTTSSVTSSSVSIPASRYDFEPLLAYLSSPSVSASLTSPSPPASVPAPEHRLAASYSAVPSHEWHALLRDLAASDASLPLAFALLPFLHRHRLCFPLDLLLSSLLHSLSVSGRLLPHSLLLSFPPSLSDPPSPLLLNSLLAASAAASRPAVALRLLSLLREHDFLPDLASYSHLLASLLNTRDPPDAALLERLLGDLRESRLEPDAPLFSDLISAFARAALPDAALELLASAQAIGLTPRSNAVTALISALGTAGRVAEAEALFLEFFLAGEIKPRTRAYNALLKGYVRIASLKNAEQVLDEMSQCGVAPDEATYSLLVDAYTRAGRWESARILLKEMEADGVKPSSYVFSRILAGFRDRGDWQKAFAVLREMQASGVRPDRHFYNVMIDTFGKYNCLGHAMDAFNKMREEGIEPDVVTWNTLIDAHCKGGRHDRAAELFEEMRESNCPPGTTTYNIMINLLGEQEHWEGVEAMLSEMKEQGLVPNIITYTTLVDVYGRSGRYKEAIDCIEAMKADGLKPSPTMYHALVNAYAQRGLADHALNVVKAMKADGLEVSILVLNSLINAFGEDRRVVEAFSVLQFMRENGLRPDVITYTTLMKALIRVEQFDKVPVIYEEMITSGCAPDRKARAMLRSGLKYIKHMRVA

Required for the translation of the chloroplast petA and petD mRNAs. Required for the processing of the petD mRNA from a polycistronic precursor. Binds with high affinity to the 5'-UTR of the chloroplastic petA transcript. Activates psaC and petA translation by binding their 5'-UTRs.

A0A1D6K6U5

CPPS2_MAIZE

Ent-copalyl diphosphate synthase 2, chloroplastic (Ent-CPP synthase 2) (Ent-CPS 2) (EC 5.5.1.13) (Protein ANTHER EAR 2) (ZmAN2)

MVLSSSCTTVPHLSSLAVVQLGPWSSRIKKKTDAVAVPAAAGRWRARARAQDTSESAAVAKGSSLTPIVRTDAESRRTRWPTDDDDAEPLVDEIRAMLTSMSDGDISVSAYDTAWVGLVPRLDGGEGPQFPAAVRWIRNNQLPDGSWGDAALFSAYDRLINTLACVVTLTRWSLEPEMRGRGLSFLGRNMWKLATEDEESMPIGFELAFPSLIELAKSLGVHDFPYDHQALQAIYSSREIKVKRIPKEVMHTVPTSILHSLEGMPGLDWARLLKLQSSDGSFLFSPAATAYALMNTGDDRCFSYIDRTVKKFNGGVPNVYPVDLFEHIWAVDRLERLGISRYFQKEIEQCMDYVNRHWTEDGICWARNSDVKEVDDTAMAFRLLRLHGYSVSPDVFKNFEKDGEFFAFVGQSNQAVTGMYNLNRASQISFPGEDVLHRAGPFSYEFLRRKQAEGALRDKWIISKDLPGEVVYTLDFPWYGNLPRVEARDYLEQYGGGDDVWIGKTLYRMPLVNNDVYLELARMDFNHCQALHQLEWQGLKKWYTENRLMDFGVAQEDALRAYFLAAASVYEPCRAAERLAWARAAILANAVSTHLRNSPSFRERLEHSLRCRPSEETDGSWFNSSSGSDAVLVKAVLRLTDSLAREAQPIHGGDPEDIHKLLRSAWAEWVREKADAADSVCNGSSAVEQEGSRMVHDKQTCLLLARMIEISAGRAAGEAASEDGDRRIIQLTGSICDSLKQKMLVSQDPEKNEEMMSHVDDELKLRIREFVQYLLRLGEKKTGSSETRQTFLSIVKSCYYAAHCPPHVVDRHISRVIFEPVSAAK

Involved in gibberellin biosynthesis. Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate (ent-CPP). Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses. In response to fungal infection and in associtation with KSL4, is involved in the production dolabradiene, a type of antifungal phytoalexin.

A0A1D6L709

VP8_MAIZE

Probable glutamate carboxypeptidase VP8 (EC 3.4.17.21) (Protein VIVIPAROUS8) (Protein WIDOW'S PEAK 1)

MPHSVLARLPPGSVRLVAAFGLLLLVSLLVLHRRPGRPHVAAAAASDRLTDPSRSRLFLSQSPGANASIAADLRALTAGPHLAGTPASAGAAAHVLARLRAAGLQTLTREYEPLLSYPGHASLALLRPDGSLLARLSLEEPADEGRRVVPPYHAYAPSGGAVAEAVFVNLGREEDYVVLERLGVGVRGRVAVARRGGGYRGGVVARAADKGAVAVLIAGNADGGVERGVVLLGGPGDPLTPGWAATSGAERLKFDDKAVKQRFPSIPSMPVSAKTAAAIIRSLGGPAIPAEWKDGLGVDTGGLGPGPTLVNFTYQEDRKFYKIRDIFGIIKGQEEPDRYVILGNHRDAWTYGAVDPNSGTAALLDIARRLGIMLQSGWKPRRSIILCSWDGEEFGMIGSTEWVEDNLEDLHSKAVAYLNVDCAVQGVGFFAGSTPQLDKLLVDITRQVRDPDVTGKMVHDTWNEMSGGIKIERLARTDSDFAPFLHHAGIPSVDLYYGEEFPGYHTALDTYNWMEKHGDPFFLRHLAITEIWGLLALRLANDPVLPFDYQAYTSQLQEHIKTLSALTSNGHAVNLMNGCVNDLSGAAMEVLKEMKKLQQMDLYDEHARMRRRLLNDRLLLAERSFLQPEGLQGRGWFKHLLYSPPEDYESKLSFFPGIADAISRSANLSDKEQEVAMQHEVWKVCRAIQRAASVLRGEFSEQKPTNFSSLVTP

Involved in the regulation of meristem development and seed maturation processes. Mediates regulation of embryonic regulatory genes and genes controlling abscisic acid (ABA) biosynthesis and turnover in developing seeds. May be required for the synthesis of small signaling molecules that integrates meristem and embryo formation in seeds.

A0A1D6LAB7

RH3B_MAIZE

DEAD-box ATP-dependent RNA helicase 3B, chloroplastic (ZmRH3B) (EC 3.6.4.13)

MASLTLPALALALSNPGAVRLRAAAFRCWALRRRGWAAAGALASPNSVLSEHAFKRLQLGSDDEDGEGPYGSDADEGFEAGEGDNEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALEGRDLIARAKTGTGKTLAFGIPMIKQLIEQDDGRITRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPAGRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTTTSKRTVLSDLITVYAKGGKTIVFTRTKKDADEVSLALTNSIASEALHGDISQHQRERTLNGFRQGKFTVLVATDVAARGLDIPNVDLIIHYELPNDPETFVHRSGRTGRAGKAGTAILMFTSSQKRTVKSLERDVGCNFEFISPPSIEEVLESSAEHVIATLRGVHPESTKYFLGAAEKLTEELGPHALASALAHLSGFSQPPSSRSLISHEQGWVTLQLTREQGFGRGFFSPRSVTGFLSDVCSAAADEVGKIYLTADENVQGAVFDLPEEIAKDLLTMELPPGNTLTKISKLPALQDDGPATDSYGRFSNDRGSRNNRRSRGGGASRGRGGWDTDGEDRFRRGGRSLRSDNDSWSDDDWSGGGRKSNRSSSFGSRSSSYSSRGSPSFGGRSSSFGGRESNRSFSGACFNCGESGHRATDCPNK

Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of chloroplasts.

A0A1D6LTV0

TPS26_MAIZE

Alpha-terpineol synthase, chloroplastic (EC 4.2.3.111) (4-terpineol synthase) (EC 4.2.3.-) (Alpha-terpinolene synthase) (EC 4.2.3.113) (Beta-myrcene synthase) (EC 4.2.3.15) (Gamma-terpinene synthase) (EC 4.2.3.114) (Limonene synthase) (EC 4.2.3.16) (Terpene synthase 26, chloroplastic)

MAGITGVMNMKLAARPSSGRHSRGCRPAVVPSAGKQMLLVRRHPPGSASWPTRATGGGGGGVPAGATAADSSGQAKEEEEEDRASRNTSSFEPSIWGDFFLTYSSPLATSSAQKARMVHRAEQLKKQVAKLIAASGACSLYHRIHLVDALERLCLDYLFEDEINDMVTQIHNVDVSGCDLQTVAMWFYLLRNHGYRVSSDVVFAKFRDEQGGFAANNPRDLLNLYNAACLRTHGETILDEAASFTSKCLKSLAPYTYMEASLASEIKRALEIPLPRSVRIYGAKSRIAEYGNQTEANELVLELAKLNYNLVQLQHQEELKIITRWWNDLELQTRLSFARDRVVECYFWMVGVYFEPSYSRARVILSKVLAIVSLLDDTYDVYGTSQECELFTKCIESWDPAATGGRLPGNMKFIFAKILDTCQSFEDELAPDEKYRMHYLKTFIIDLVRAYNEEVKWREQGYVPATVEEHLQVSARSGGCHLLSCTSFVGMGDVADQEAFEWVRGVPKIVKALCIILRLSDDLKSYEREKMSSHVASTMESCMKEHQVPLEVARVKIQETIDETWKDFNEEWLNLNTNSHLPRELLERIFNLTRTMVYIYQQDDAYTNCHVIKDTINSLFVEPVSIT

Component of the volatile terpenes biosynthesis pathways. Mediates the synthesis of a blend of monoterpenes. Converts mainly geranyl diphosphate to alpha-terpineol. Triggers also the biosynthesis of minor monoterpenes including limonene, gamma-terpinene, beta-myrcene, terpinolene and 4-terpineol.

A0A1D8EJF9

IF4E1_SOLPI

Eukaryotic translation initiation factor 4E-1 (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)

MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNPTTKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV

Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses.

A0A1D8PCL1

HGT1_CANAL

High-affinity glucose transporter 1

MSSKIERIFSGPALKINTYLDKLPKIYNVFFIASISTIAGMMFGFDISSMSAFIGAEHYMRYFNSPGSDIQGFITSSMALGSFFGSIASSFVSEPFGRRLSLLTCAFFWMVGAAIQSSVQNRAQLIIGRIISGIGVGFGSAVAPVYGAELAPRKIRGLIGGMFQFFVTLGIMIMFYLSFGLGHINGVASFRIAWGLQIVPGLCLFLGCFFIPESPRWLAKQGQWEAAEEIVAKIQAHGDRENPDVLIEISEIKDQLLLEESSKQIGYATLFTKKYIQRTFTAIFAQIWQQLTGMNVMMYYIVYIFQMAGYSGNSNLVASSIQYVINTCVTVPALYFIDKVGRRPLLIGGATMMMAFQFGLAGILGQYSIPWPDSGNDSVNIRIPEDNKSASKGAIACCYLFVASFAFTWGVGIWVYCAEIWGDNRVAQRGNAISTSANWILNFAIAMYTPTGFKNISWKTYIIYGVFCFAMATHVYFGFPETKGKRLEEIGQMWEERVPAWRSRSWQPTVPIASDAELARKMEVEHEEDKLMNEDSNSESRENQA

High-affinity glucose transporter. Acts as a multifunctional complement-evasion molecule that causes down-regulation of complement activation by acquisition of human complement factors FH and C4BP. Functions also as a human immunodeficiency virus (HIV) receptor via binding the viral gp160 protein. Modulates hyphae formation.

A0A1D8PPK1

EBP1_CANAL

Probable NADPH dehydrogenase (EC 1.6.99.1) (Estrogen-binding protein) (EBP)

MTIESTNSFVVPSDTELIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYKIWKGNFIRAGNYTYDAPEFKTLINDLKNDRTIIGFSRFFTSNPDLVEKLKLGKPLNYYNREEFYKYYNYGYNSYDESEKQVIGKPLA

Oxidoreductase that binds mammalian estrogens with high affinity.

A0A1D8PQ86

ALS9_CANAL

Agglutinin-like protein 9 (Adhesin 9)

MLPQFLLLLLYLTVSTAKTITGVFNSFDSLTWTRSVEYVYKGPETPTWTAVLGWSLNSTTADAGDTFTLIMPCVFKFITSQTSVDLTADGVSYATCDFNAGEEFTTFSSLSCTVNSVSVSYDKASGTVKLPITFNVGGTGSSVDLTDSKCFTAGKNTVTFMDGDTKISTTVDFDASPVSPSGYITSSRIIPSLNKASSLFVSPQCENGYTSGIMGFVTSQGATIDCSNINIGISKGLNDWNFPVSSESFTYTKTCSSSGIIVEYENVPAGYRPFVDAYISSENVEQYTLTYANEYTCKNGNTVVDPFTLTWWGYKNSEADSNGDIIVVTTKTVTASTTAVTTLPFNPTVDKTETIEVLQPIPTTTITTSYIGISTSYETFTATIGGTATVIVDTPYHITTTVTTFWTGSVTTTTTYSNPTGSIDTVIVQIPSPDPTTTITEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTITNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIVKEPYNPTVTTTEFWSESFASTTTVTNPPDGTNSVIIKEPYNPTVTTTEFWSESFASTTPSVSSFESKTFYSSEAQSSLEIDSSNTFMTSISVSTASSYDESSTIVSSAFPTLHISSYSLSTSFVPPVTLPRYVNTTISSSPSFESSSMYSSVTSAVTSIDNDREVPTSTTTYLHSKLYSESISTVIQTKSSDWSLSLGNSNKPESASTVSEESLHYLSTPGPSSSEYSISFTSEKEGHVSSYVPRVSYTSSVKVSISSTMSSENGMSATHTFGISTNTIPSSTETSIKSATVTTPVSESTNTGMSIFMSTTTESKTTDITTETSVSGEVNLGSATVKVSSSEFISKGTVTRIMPTELTNSESTFTASPSFVLTSTESSVIETPATIEMSSRSSSYSVPLSKLRSEGETTRVIPTSSTATGSTVIGSPSSVSTSNESIITGSSSFVSTTAETISTRSIVTESIVAGSPSLVLTTTVLDTTETTITETSIVGESSSRSLTFKASSLSKGEITGTVTPEMSVSTSKATTGTTSEVSIKESLTTKVPTFTSTTIKPETSETQHSESRTTQIPYSETKGSQLSTANSQVSQTGSSKSSIFESAISKDESTFVSATVKSITTPAVTQYQTSLPNPAVSVSEESGKKSSIIESQTENSATQHSIYFDSIETSTLSNTLANTLVSGAMKNSETTSELTTSDKAIGFSTTTETSIPGATNSALSPSVDSGKSSMLGWSGGIVSTVSTSTRLEDSTATSSSITAANQDSLNPSTVSKYPHGSETIDNGSNGSSHSSSALASTISASHSIKFSAHQTTLSQSLISSSTKTVIASTYDGSGSVIKLHSWFYGLVTIFFLFI

Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections. Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not.

A0A1D8PQB9

ALS4_CANAL

Agglutinin-like protein 4 (Adhesin 4)

MLLQFLLLSLCVSVATAKVITGIFDSFNSLTWTNAASYSYRGPANPTWTAVIGWSLDGATASAGDTFTLDMPCVFKFITDQTSIDLVADGRTYATCNLNSAEEFTTFSSVSCTVTTTMTADTKAIGTVTLPFSFSVGGSGSDVDLANSQCFTAGINTVTFNDGDTSISTTVDFEKSTVASSDRILLSRILPSLSQAVSLFLPQECANGYTSGTMGFSTAGTGATIDCSTVHVGISNGLNDWNYPISSESFSYTKTCTSTSVLVTYQNVPAGYRPFVDAYVSATRVSSYAMRYTNIYACVGAASVDDSFTHTWSGYSNSQAGSNGITIVVTTRTVTDSTTAVTTLPFNSESDKTKTIEILQPIPTTTITTSYVGVTTSYSTKTAPIGETATVIVDVPYHTTTTVTSEWTGTITTTTTRTNPTDSIDTVVVQVPSPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIKEPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIREPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTLTITAPPGGTNSVIIRVHSSTNDESSESTFSTLSVPSFSGSISIVSTVSRPHYVNSTVTHLPSSSSKPVDIPSSDVVTSTNDNSLTSLTGSENGKTSVAISTTFCDDENGCQTSIPQGSVVRTTATTTATTTTIIGDNNGSGKSKSGELSSTGSVTTNTATPDVPSTKVPSNPGAPGTGVPPPLAPSTETQTTNNVPGSPNIPATGTTDIIRESTTVSHTVTGNGNTGVPMNPNPVLTTSTSLTGATNSATNPSHETSVNTGSGGSTNIVTPPSSATATVVIPGTDNGATTKGQDTAGGGNSNGSTATTNIQGGNNEPGNQPGTNTTGEPVGTTDTQSVESISQPTTLSQQTTSSLISTPLASTFDGSGSIVQHSGWLYVLLTAISIFF

Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections.

A0A1D9BZF0

GCNA_MOUSE

Germ cell nuclear acidic protein (Acidic repeat-containing protein) (Germ cell nuclear antigen)

MDSGSSSSSSSSGSSSGSCSTSGSGSTSGSSTTSSSSSSSSSSSSSSSSSSKEYMPELPKQRKASCVVIDSESDSDNTSDEKNTTVCEISSGDETSDIDRPGGQKLPLIVIDDDDDGSPDLKNTKQKSDEPQMSVLEKEGVECIGSDSTSPHDVCEIWDVCGSSNQTSSELEPEGEPESEAKGEPESEAKGEPESEAKGEPESEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGEPESEAKGEMETEAKGEPESEAKGEMETEAKGESESEAKGEMETEAKGESESEAKGEMETEAKGEPESEAKGEMETEAKGEPESEAKGEPEPEAAKGEMETEAAMGEVETEAAMGEPEQEITAEEAKKKRAAYLLAQQRKRKRKNRFICMSSSKPRRKRRRADPQDGADPQDGADPQDRADPQDLADPQDRGDSQDMPSLPGTSDEPIPSGQPVCPRKGMASSRGRGRGRGRGRGRGRGRGRGRGRGAKAGK

May play a role in DNA-protein cross-links (DPCs) clearance through a SUMO-dependent recruitment to sites of DPCs, ensuring the genomic stability by protecting germ cells and early embryos from various sources of damage. Can resolve the topoisomerase II (TOP2A) DPCs.

A0A1E1FFL0

PRHA_PENBI

Multifunctional dioxygenase prhA (EC 1.14.11.-) (Paraherquonin biosynthesis cluster protein A)

MAPMIPPRLQRFPATASADEIFAAFQEDGCVVIEGFISPEQVARFSQEVDPAMEKIPVEVTNNGNSNDRTKRFSKCVIASPTFRNEIIESDLMHELCDRVFSKPGEGMGYHFNDNMVIEVQPGAPAQRLHRDQELYPWWNSMGPAGPECVINFFCAVTPFTEENGATRLVPGSHLWPEFTQINERDCPQFGKIETVPAIMQPGDCYLMSGKVIHGAGHNATTTDRRRALALAIIRRELRPMQAFSLSVPMKLAREMSERSQTMFGFRSSVQHCDVDMVHFWGNDGKDIAHHLGLEAPSVHV

Multifunctional dioxygenase part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B. The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK. Finally, prhA leads to berkeleydione via the berkeleyone B intermediate. PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione. Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable).

A0A1E3P8S6

EAT1_WICAA

Ethanol acetyltransferase 1 (EC 2.3.1.268) (Acetyl-CoA hydrolase) (EC 3.1.2.1) (Acetyl-CoA thioesterase) (Alcohol acetyltransferase) (AAT) (Ethyl acetate esterase) (EC 3.1.1.-)

MFFTKVLNNQVANGLKQLPVHKRVQMAYDLHIPNKTVNPNLNIRSHEPIVFVHGIFGSKKNYRHDCQKIANVTHTPVYTIDLRNHGQSMHALPFDYETLAQDVTDFCEDHGLKKVNLIGYSLGAKICMLTMLQNPDLVRSGVIIDNSPIEQPHIEIFLTQFIKSMLHVLNSTKIRADDKDWKSKANQAMRRYIPNGGIRDYLLANLINKVPKGYKSPVINYDDGYIHFQNPVRHMTEVAVKNVSAWPTEHVKGLKFEGQVRFLKGTKSAFIDEKGLEAIKEYFPNYSLSELNATHFILNERPQEYVKLICDFIKVNRYKSLQEHIRHVENFSSAELEARHNAEHERQMEELRQLTQTTPTAEQVKTIDNLASKVDLSATERQQQQNKEITV

Alcohol acetyltransferase that catalyzes the synthesis of ethyl acetate from ethanol and acetyl-CoA. Can also function as a thioesterase by hydrolyzing acetyl-CoA in the absence of ethanol, as well as esterase hydrolyzing ethyl acetate.

A0A1F4

EYS_DROME

Protein eyes shut (Protein spacemaker)

MSNVHQFDTQTMAESPQIRRDMGRLCATWPSKDSEDGAGTALRAATPLTANGATTTGLSVTLAPKDMQRNHLLKMPTATIEKPTITATIASSSSTSTSTTRKSVTATRSLKLNPNILLPTLRILARGLLLPALILAILVGSSQAGFACLSNPCVFGVCIDGLNSSYSCYCIDGYTGIQCQTNWDECWSSPCQNGGTCVDGVAYYNCTCPEGFSGSNCEENVDECMSNPCQNGGLCRDRTNGYICTCQPGYLGSHCELDVAVCETGTGARCQHGGECIEGPGLEFTCDCPAGWHGRICQEEINECASSPCQNGGVCVDKLAAYACACPMGYTGINCEEEILICADNPCQNNALCLMEEGVPTCYCVPDYHGEKCEFQYDECQLGPRCMNGGVCIDGVDTFSCSCPPLLTGMLCECLMVGEESLDCNYTAPATQSPPRRTTTTSTMAPPTVRPVTPPETTVSPSRASEEVEIIVVTTSAPAEVVTSVLSPSSSSSSSEEGVSVEIKTPTVAPPESGSHSISVEQTTAVPAQPEPESEQEPESKPHPESESASESETETEEEIIPGTTARPPTSRSSSSSEESPSIFTTLPPLPGKPQTSASSESSGEVVTSEEYTTVPHFEVSGSKSESGSEEVTTVRPTAAPSITISVDITSSGSSSSSSESVEVFTTPAPVFVQRVTTIETSISIDYVTPTPLPETTTPRVVPVPRPTFAPEPPLDVVETTASTHHLWTEVPTTAAPFFTEYPAEVLITTHRTSAGRFTTVQPPAGVTTTSPTEDSSVELPTPHTPQIVVTILDSNEVIPSLITTTGSPTTHHHHHHHPHHEAEGTTLQPLEEDEHHHHHHHDEFTTPQPVEITTGHPLQTEDLIGVQEPAVVTTESPFAPAETTVVPVVVPATIAPLGTAAPPATPAPVPPATTTPPPSPPSLATETPTLPPTLPPVTLPPVTQPPPTIPPTPPSTQSAQTLPPPTSAINVYTTPDGPPTASQTKPSVTESSEEVEGTNTVSTGGRGSGGVPEEKAGDVDCIKLGCYNGGTCVTTSEGSRCVCRFDRQGPLCELPIIIRNAAFSGDSYVSHRIYKDIGGHESLDAVLPMHIQLKVRTRATNGLIMLAAAQGTKGGHYMALFLQKGLMQFQFSCGLQTMLLSELETPVNTGHEITIRAELDFSRNYTHCNASLLVNDTLAMSGDQPTWLKLLPPRLHTPEAILNTWLHLGGAPQAPIGLIIELPPAQSGSGFTGCLHTLRINGQAREIFGDALDGFGITECGSLACLSSPCRNGAACIKIETNDLDENGEKAEKWKCKCPTGYMGPTCEISVCEDNPCQYGGTCVQFPGSGYLCLCPLGKHGHYCEHNLEVALPSFSGSVNGLSSFVAYTVPIPLEYSLELSFKILPQTMSQISLLAFFGQSGYHDEKSDHLAVSFIQGYIMLTWNLGAGPRRIFTQKPIDFRLDAPRVPYEIKVGRIGRQAWLSVDGKFNITGRSPGSGSRMDVLPILYLGGHEIANFNTLPHDLPLHSGFQGCIYDVQLKAGQVTVPLQETRGVRGRGVGQCGTRECHRHACQHDGACLQHGATFTCICQEGWYGPLCAQPTNPCDSFNNKCYEDATCVPLVNGYECDCPVGRTGKNCEEVIRSLSDVSLTGRRSYLAVRWPYLYDGGDKLGAKRSQMVSYRNFTKKLMPPKPITTPSSHFVMKLLNEVEKQRSFSPVPLMGSKSFEEHHRVQFFFIEFQLRPLSERGLLLYFGTLNNNQDKKIGFVSLSLQGGVVEFRISGPSNHVTVVRSVRMLAIGEWHKIKMAQRGRWLTLWVEGSASSALAPSAEVLVEPDSLLYIGGLKDVSKLPHNAISGFPIPFRGCVRGLVVSGTRIVLNETNIVESRNIRDCDGTACGGDSCESGGHCWLDEKLQPHCICPEYAKGDRCEYSETCKLIPCKNNGRCLRSGRCSCPNGWGGFYCEIAMSKPTTPSFRGNSYLILPPPRIPMKDKRRGPSLYVRPREAIQVSLNFSTIEPDGLLLWSEHERSKFLGLGLEAGHLKLASNLLGSTNDTVRAPASGFIADGAWHWTSVLLDRSRLELQLDGEVIFTERLPEGGRSLGSTTPRSTLAGRRKNSSKEPTISYEDVFYLGGFPNSDSVSRRTKGRFFDPFKGCLQDIQFGAEPTAIISDFSTYQGENIGSCDLHGDEPLTV

Essential for the formation of matrix-filled interrhabdomeral space: critical for the formation of epithelial lumina in the retina. Acts together with prominin (prom) and the cell adhesion molecule chaoptin (chp) to choreograph the partitioning of rhabdomeres into an open system.

A0A1I9LM04

CNDD2_ARATH

Condensin-1 complex subunit CAP-D2 (Protein CHROMOSOME-ASSOCIATED POLYPEPTIDE D-2) (AtCap-D2)

MAPPFVFPQILRALEEDPEDNHRLFAQNPVDVTSLRPSDLEEFVKGVSFDLSDRELFCVEDQDVFDRVYSLVRSFFSLPPSCKCNLVESLRSNLSVLLPNVDSISRSVQDQEDDVPIIDRITSHRNALKIYTFFLLTVVMNEESHISSVETTKVAARGRKKQIIQSWNWEPQRGRMLNLIANSLEINLSLLFGSSDLDENYLSFIVKNSFTLFENATILKDAETKDALCRIIGASATKYHYIVQSCASIMHLIHKYDFAVVHIADAVARAESKYSDGTLAVTIIRDIGRTDPKAYVKDTAGADNVGRFLVELADRLPKLMSTNVGVLVPHFGGESYKIRNALVGVLGKLVAKAFNDVEGDMSSKSLRLRTKQAMLEILLERCRDVSAYTRSRVLQVWAELCEEHSVSIGLWNEVASLSAGRLEDKSAIVRKSALNLLIMMLQHNPFGPQLRIASFEATLEQYKRKLNELEPTEHASKESTSDGESCNGDGEIDDLHLETTTKIHQDSLSDSCQPENGEEISEKDVSVPDIGNVEQTKALIASLEAGLRFSKCMSASMPILVQLMASSSATDVENAILLLMRCKQFQIDGAEACLRKILPLAFSQDKSIYEAVENAFISIYIRKNPVDTAKQLLNLAIDSNIGDQAALEFIVNALVSKGEISSSTTSALWDFFCFNINGTTAEQSRGALSILCMAAKSSPRILGSHIQDIIDIGFGRWAKVEPLLARTACTVIQRFSEEDRKKLLLSSGSRLFGILESLITGNWLPENIYYATADKAISAIYMIHPTPETLASTIIKKSLSTVFDVVEQEEAQTDTENNKVDILTPVQVAKLSRFLFAVSHIAMNQLVYIESCIQKIRRQKTKKDKPAAESQNTEENLEATQENNGINAELGLAASDDALLDTLAERAEREIVSGGSVEKNLIGECATFLSKLCRNFSLLQKHPELQASAMLALCRFMIIDASFCESNLQLLFTVVENAPSEVVRSNCTLSLGDLAVRFPNLLEPWTENMYARLRDASVSVRKNAVLVLSHLILNDMMKVKGYIYEMAICIEDDVERISSLAKLFFHELSKKGSNPIYNLLPDILGQLSNRNLERESFCNVMQFLIGSIKKDKQMEALVEKLCNRFSGVTDGKQWEYISYSLSLLTFTEKGIKKLIESFKSYEHALAEDLVTENFRSIINKGKKFAKPELKACIEEFEEKINKFHMEKKEQEETARNAEVHREKTKTMESLAVLSKVKEEPVEEYDEGEGVSDSEIVDPSMEESGDNLVETESEEEPSDSEEEPDSAQCGTAIPRYLNQKTSGDNLIETEPEEEQSDSEPDSAQCGTTNPRSLNRKTSGDNLIETESEEEQSDSEEEPSDSEEEPDSAQCGTTNPRSLNQKTSGGEEGESESKSTESSSSIRRNLRSGSRS

Essential protein. Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes (By similarity). The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity). Required for fertility, growth and euchromatin organization, but not for sister chromatid cohesion. Necessary to maintain normal structural integrity of the meiotic chromosomes during the two nuclear divisions of gametogenesis, especially to maintain compaction of the centromeric repeats and 45S rDNA. Seems also involved in crossover formation during meiotic prophase I. Prevents centromeric and pericentromeric heterochromatin repeats association. Contributes to the induction of stress-responsive genes in response to stress treatment.

A0A1I9LMX5

PCEP9_ARATH

Precursor of CEP9 (PCEP9) [Cleaved into: C-terminally encoded peptide 9.1 (CEP9.1) (CEP9a); C-terminally encoded peptide 9.2 (CEP9.2) (CEP9b); C-terminally encoded peptide 9.3 (CEP9.3) (CEP9c); C-terminally encoded peptide 9.4 (CEP9.4) (CEP9d); C-terminally encoded peptide 9.5 (CEP9.5) (CEP9e)]

MKLLSITLTSIVISMVFYQTPITTEARSLRKTNDQDHFKAGFTDDFVPTSPGNSPGVGHKKGNVNVEGFQDDFKPTEGRKLLKTNVQDHFKTGSTDDFAPTSPGHSPGVGHKKGNVNVESSEDDFKHKEGRKLQQTNGQNHFKTGSTDDFAPTSPGNSPGIGHKKGHANVKGFKDDFAPTEEIRLQKMNGQDHFKTGSTDDFAPTTPGNSPGMGHKKGDDFKPTTPGHSPGVGHAVKNDEPKA

Extracellular signaling peptide that represses primary root growth rate and significantly inhibits lateral root formation. Modulates leaf morphology. Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways.

A0A1I9LN01

LAF3_ARATH

Protein LONG AFTER FAR-RED 3 (EC 3.5.-.-)

MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKDVSASVLATYVGGKQLYP

Required for phyA-controlled responses to continuous far-red light (FRc) conditions, including the inhibition of hypocotyl elongation and the regulation of XTH15/XTR7 expression.

A0A1J1DL12

RIDA_DERFA

2-iminobutanoate/2-iminopropanoate deaminase (EC 3.5.99.10) (Allergen Der f 34) (Enamine/imine deaminase) (allergen Der f 34.0101)

MSPKRIISTPLAPQPIGPYSQAVQVGNTVYLSGQIGMNVRTNEMVTGPIRDEAQQAFTNMKAVVEASGAKMSDVVKVNIFIRNFNDFPAINDVMKEFFQSPFPARSTVGVAELPKNARVEIESIVVIE

Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase (By similarity). Preferentially digests Leu and Met in cooperation with L-amino acid oxidase, but digests Phe poorly.

A0A1L3THR9

CDA_PESTX

Chitin deacetylase (EC 3.5.1.41)

MLAPLFAALLAGAATASPIQERQSSVPVGTIITACTVPNTFALTFDDGPFAYTSELLDLLSSNGVKATFFLNGQNWGSIYDYTSVVTRMDAEGHQIGSHTWSHADLATLDAAGITSQMTQLETALTSILGKVPTYMRPPYFSTNALALSTLGGLGYHVINANIDTLDYEHDDDTIGVAFTNFQNGLASGGTVSLMHDVHAQTVHVLVQEAINAIKAKGLTPVTVGTCLGDASANWYKSGGGSGTTPPPATGGPSPDDTCGGSNGYVCQNSQCCSQWGWCGTTSEYCAAGCQAAYGPCT

Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate. May play a role in evasion of the host immune response plant chitinases liberate chitin molecules from the fungal cell wall which act as elicitors of the plant immune response, deacetylation of the liberated chitin neutralizes elicitor activity.

A0A1L4BJ46

HEMI1_HEMLE

Phospholipase A2 hemilipin (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A(2)) [Cleaved into: Phospholipase A2 large subunit; Phospholipase A2 small subunit]

MTFLILTILATVTPSLYSHVVQRELRVNFEPLAGQRDSWPVARAAMVTFDARSEKAREFSECRMINSMHELSRELMDSPEHTVKRASKEEMDDLVQRCSGSAEGRSWFIWPDTKWCGPGTDAKNESDLGPLEADKCCRTHDHCDYIGAGETKYGLTNKSFFTKLNCKCEAAFDQCLKESIDRAEGSAKSSMEGLHSFYFNTYSPECYEVKCSRKRDAECTNGIAIWKDSYKS

Scorpion venom phospholipase A2 (PLA2) that shows high hydrolytic activities towards lecithin and acts as an effective blocker of all angiogenesis key steps in vivo and in vitro. It has no effect on apoptosis and does not display hemolytic, inflammatory or neurotoxic effects. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

A0A1L4BJ98

DTPLD_HEMLE

Dermonecrotic toxin Hl-PLD1 (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)

MAHCYYNSKRGCNRVMKTVALVVLISTVMVEESRGDSQEDKKRPIWNIGHMVNAVKQIEEFLDLGANALEADVTFDDNGNPKWTYHGTPCDCFRDCLRWEYVDEYLKRIRELTSPGSSKFRKGFILLMLDLKISKLSDNAKSKAGKEIADMIIKRLWSGSGEKAQLYIVLSFPYVNDIEFVRAFRERVKSKGFASEAEKRIGWDISGNEDLGKIRDAYQKLGITDNVWQSDGITNCLTRSHDRLAEAVCKRDSDKEWPSLKKVYYWTVDKQSSMKEALKVGVDGMITNDPDDLVAVLNEFSGTHRLANINDSPWQKIPRPKSNC

Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with a high activity. It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). In vivo, shows dermonecrotic activity when intradermally injected into rabbit skin and is lethal to mice. Induces increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). Does not show hemolytic activity (at up to 50 ug).

A0A1L4BKS3

TERL_BPG20

Terminase, large subunit (DNA-packaging protein) (DNA-packaging protein gp80) (Gene product 80) (gp80) [Includes: ATPase (EC 3.6.4.-); Endonuclease (EC 3.1.21.-)]

MKRLRPSDKFFELLGYKPHHVQLAIHRSTAKRRVACLGRQSGKSEAASVEAVFELFARPGSQGWIIAPTYDQAEIIFGRVVEKVERLSEVFPTTEVQLQRRRLRLLVHHYDRPVNAPGAKRVATSEFRGKSADRPDNLRGATLDFVILDEAAMIPFSVWSEAIEPTLSVRDGWALIISTPKGLNWFYEFFLMGWRGGLKEGIPNSGINQTHPDFESFHAASWDVWPERREWYMERRLYIPDLEFRQEYGAEFVSHSNSVFSGLDMLILLPYERRGTRLVVEDYRPDHIYCIGADFGKNQDYSVFSVLDLDTGAIACLERMNGATWSDQVARLKALSEDYGHAYVVADTWGVGDAIAEELDAQGINYTPLPVKSSSVKEQLISNLALLMEKGQVAVPNDKTILDELRNFRYYRTASGNQVMRAYGRGHDDIVMSLALAYSQYEGKDGYKFELAEERPSKLKHEESVMSLVEDDFTDLELANRAFSA

The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer. Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. {ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000305|PubMed:28100693}.

A0A1L5YRA2

TPIS_SCYPA

Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Allergen Scy p 8) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase) (allergen Scy p 8.0101)

MANQRKFFVGGNWKMNGDKAAIDGIISFMKGPLNADTEVVVGCPQCYLMYTREHMPANIGVAAQNCYKTAKGAFTGEISPAMIKDCGCEWVILGHSERRNVFGEPDQLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQDVHAKLRQWLRDNVSPQVAESTRIIYGGSVSAGNCKELAKTGDIDGFLVGGASLKPDFVTIINARA

Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids.

A0A1L6K371

JUGN4_JUGNI

11S globulin (11S legumin) (allergen Jug n 4) [Cleaved into: 11S globulin acidic chain; 11S globulin basic chain]

MAKPILLSISLCLVALVNGCLAQSGGRQQPRFGECKLKRLVALEPSNRIEAEAGVIESWDPNNQQFQCAGVAVVRRTIEPNGLLLPQYSNAPQLLYIVKGRGITGVLFPGCPETFEESQQGQSRIRPSLRSASFQRDRHQKIRHFREGDVIAFPAGVAHWCYNDGDTPVVAVALMDTTNNANQLDQNPRNFYLAGNPDDEFRPQGQQEYEQHRRQQQHQQRHGEPGQQQRGSGNNVFSGFDADFLADAFNVDTETARRLQSENDHRRSIVRVEGRQLQVIRPRWSREEQEREERKERERERESESERRQSRRGGRDDNGLEETICTLRLRENIGDPSRADIYTEEAGRISTANSHTLPVLRWLQLSAERGALYSDALYVPHWNLNAHSVVYALRGRAEVQVVDNFGQTVFDDELREGQLLTIPQNFAVVKRARNEGFEWVSFKTNENAMVSPLAGRTSAIRALPEEVLANALQIPREDARRLKFNRQESTLVRSRPSSSRSSRSERRAEV

Seed storage protein.

A0A1L6Z3A0

TPS8_PSEAD

Pseudolaratriene synthase, chloroplastic (EC 4.2.3.180) (Terpene synthase 8) (PxaTPS8)

MSRFTSATHGLNLSIKMPISVSQVPSIRSNTSKYELQKLRSTGRSVLQTRRQLAIINMTKRSEADDNDGVERRKGVFHPNLWDDGFIQSLSTVYHEQASYRERAERLIGEVKAVFDSISMGDGDQFISPSAYDTAWVARVPAIDGSSRPQFPQAIDWILLNQQQDGSWGSQSHLSLTHRLTDTLACVIALASWKIESVQIDEGLDFITRGVEKLQSESVPAEFEIIFAELLNQAKSLQLSLPYEHSCLQSLWRKQEPILANGLMDSVAKRSLSSLEEMQDHRMNTDSDGTMHVESFLSSPAVAARVLMRTGNPICLAYLNNVLNKFGDYVPGMYPVDLFQRLWMVDNVERLGIDRHFKKEIQVTLDYVYSYWNGKGIGCGRDSLSPDLNSTSLGFRTLRLHGYNVSADVLEHFKDRDGKFVCSSNPTVGEIRSVLNLYRASLLAFPGEKVMEEAETFARRYLEEIVQKIPPSKFSREIEYVLEFGWQSTVPRWEARSYIDFHGLDTYSPWTIYEMASEKFLELAKLEFNIFNSLQHTELQYLSRWWNDSGMSQMRFTRHRNVEYYTMASCIAMEPSQSAFRIGFTKLCGIATCIDDIYDTYGTIDELKLFREAVKRWDPSAIESLPEYMKSVYMVLYELVNEMAQDTERTQGRDTLDYARNAWEAIIDAHLVEAEWIASGHIPTFEEYLENSKVTSGLHIAILPILTLDVPLPDQLPLQEIDTLSRFHHLASTIGRLSGDMNAYKIDLAHGEESSCISCYMKDNPGTTEGDAHNYANVTISYLMKELNLELMGQHNRVSFLRTSKKPAFDIYRASNYMYKYRDGYTIADKETKNLVMRTLVQAVSL

Converts geranylgeranyl diphosphate to an new 5,7-fused bicyclic diterpene, named pseudolaratriene. Catalyzes the first committed step in pseudolaric acid B (PAB) biosynthesis. PAB exhibits antiproliferative activity by inhibiting microtubule polymerization, and has demonstrated antitumor properties against several cancer types (Probable).

A0A1L7NQ96

KET3E_ARTGO

Ketose 3-epimerase (EC 5.1.3.-) (D-allulose 3-epimerase) (D-AE) (L-ribulose 3-epimerase)

MKIGCHGLVWTGHFDAEGIRYSVQKTREAGFDLVEFPLMDPFSFDVQTAKSALAEHGLAASASLGLSDATDVSSEDPAVVKAGEELLNRAVDVLAELGATDFCGVIYSAMKKYMEPATAAGLANSKAAVGRVADRASDLGINVSLEVVNRYETNVLNTGRQALAYLEELNRPNLGIHLDTYHMNIEESDMFSPILDTAEALRYVHIGESHRGYLGTGSVDFDTFFKALGRIGYDGPVVFESFSSSVVAPDLSRMLGIWRNLWADNEELGAHANAFIRDKLTAIKTIELH

Catalyzes the reversible C-3 epimerization of several ketoses. Shows the highest enzymatic activity for the epimerization of L-ribulose to L-xylulose. Is also able to convert D-allulose (also known as D-psicose) to D-fructose and, to a lesser extent, L-tagatose to L-sorbose, D-ribulose to D-xylulose, L-allulose to L-fructose and D-tagatose to D-sorbose.

A0A1L8F5J9

NMDZ1_XENLA

Glutamate receptor ionotropic, NMDA 1 (GluN1) (N-methyl-D-aspartate receptor subunit NR1) (NMD-R1)

MGTMRLFLLAVLFLFSFARAGCDPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLNATSVTHRPNAIQMALSVCEDLISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTVPPYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEEKESKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDMTGAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYPDGVTGRIEFNEDGDRKFANYSIMNLQNRKLVQVGIFNGSYIIQNDRKIIWPGGETERPQGYQMSTRLKIVTIHQEPFVYVRPTTSDGTCREEYTINGDPIKKVICNGPNETIPGRPTVPQCCYGFCVDLLIKLAREMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLNILKSHENGFMEELDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKASFRSITSTLASSFKRRRSSKDTVNVVV

Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:16214956, PubMed:19524674, PubMed:21677647, PubMed:25008524, PubMed:26912815, PubMed:27135925, Ref.11, PubMed:28232581). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable).

A0A1L8FDW4

PEX5_XENLA

Peroxisomal targeting signal 1 receptor (PTS1 receptor) (PTS1R) (PTS1-BP) (Peroxin-5)

MAMRGLIEAECGGSNPLMKLTNHFTQDKALREEGLQHVSWPPGATVVSKPLGEATEDELVSEFLHTRAPSLQSRAPHTFKMDGLLAEMQEIEQSSFRPEPLRAPGVADLALSEQWSAEFLGVEVDPVEEEDWSREFTEQADPHASPSRWAEEYLQQSEEKLWLGESEGAMAEKWTEEYQPEDDLQREAKSLVSQVTDPKLANTQFLQFVKRIGDGELSFSHAPSTPSQTVSQAEQWSEQFVHEQAEQWVDQFAPLEKDFEKAKAAVESDVDFWDKLQEEWEEMAKRDAEAHPWLSDFQDLSSKSIDKGYMFEDNNPFSEVSLPFEEGLKHLREGDLPSAVRLFEVAVKRDPQHMEAWQYLGTTQAENEQELAAISALRRCIDLKPDNLSALMALAVSYTNECLQQQACHTLREWLRHNPKYSHLVKEESSSNASRARSFGTLLSDSVFSDVRELFLSAVNSDPSQVDPDVQCGLGVLFNLSGEYQKAVDCFTAALGQRPDDYLLWNKLGATLANGNDSEAAVEAYRRALQLQPGFIRSRYNLGIACINLGAHREAIEHFLEALSMQQQSGGCESAMSDNIWSTLRMALSMIGQSDLYSSADARDLATLQAAFPPHSAAQ

Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the pex13-pex14 docking complex along with cargo proteins. Pex5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle. In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with pex7. Interaction with pex7 only takes place when pex7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. Pex7 along with PTS2-containing cargo proteins are then translocated through the pex13-pex14 docking complex together with pex5.

A0A1L8G2K9

SPRTN_XENLA

DNA-dependent metalloprotease SPRTN (EC 3.4.24.-) (Protein with SprT-like domain at the N terminus) (Spartan)

MGDMQMSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGVEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVETLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINGRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGSFVKVKEPENYPQKRKRKNDPTISEVNSSSHVKGKSNGVDIRTVIPFSGTGYKLFEPNKSDAPLKILNINPTKDKAAVPLLNHTPPSTNINGTFLTNKIGSAKSTPAQSILTKVSVANTKVFINLNGSPIKLPSGSKNKSHQISSKQKSVLPFFKMQKDNSFDLTLPSPSIQSTSQKPQKDISFGFTLPSQSFPSTSPGSNSENKEPLYKKLQMNDRESFIIHSGNKTNVNDNKSCTGPAATTASGLNHTIKVSCPVCGTEVLECKINDHLDTCTSSGPQKDILLDVSLPLQSFPSTSQGSNSAIKEPLYKKLQINDKDSFIIHSGNKTNVNDNKSCTRPAATTASGFNHTIKVCCPVCGTDVLQDKINDHLDTCLQNCNT

DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (By similarity). Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis (By similarity). Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as top1, top2a, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs. May also act as a 'reader' of ubiquitinated pcna: facilitates chromatin association of rad18 and is required for efficient pcna monoubiquitination, promoting a feed-forward loop to enhance pcna ubiquitination and translesion DNA synthesis (By similarity). Acts as a regulator of translesion DNA synthesis by recruiting vcp/p97 to sites of DNA damage (By similarity).

A0A1L8GSA2

TET3A_XENLA

Methylcytosine dioxygenase tet3-A (EC 1.14.11.80)

MMETQPTSLPHVLPQDVYEFCDDRKSLGRLRVSEMPAESNGDGGGSKGDGAAVVAKEVPEQSNKKRKRCGVCVPCLRKEPCGACYNCVNRSTSHQICKMRKCEQLKKKRVVPLKGVEAVNKDDSKNQAKEQVPNVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKKECDSTLPSKACEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPTIPNHTAATNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSVSMQLYEKFNYETNRDSSGHPEGNAPSCPEDLNTLKTALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSSQKDSQESSFPGLGQVSKELVQKSYPKEEVLNLENKNLCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNECPNSSSQPLINTCDQLTHFPTAKGNQLPIFPMACNELFQNQQSQLYTGKNALPVPQSPRQTSWEQNKKPSYQEGQYIPENLSQSSSVLPSDASTPQKTEFLQQWIQNADLLKSPSDPMTGLKQLLGNTDEYIKSVFKGPEALPNKIKHVKTKRTIKSIKKKSSDFLKMSPDQQLSQLLQENDFHHNAQAALQQHLHHKRNLFVDPNTMEACAQEQQNWWVPKSQKLPVSKTTENPVKERKKRRQRSPSQKQVEPKPKPPRKQVQIKKPRMKEGNAVFMPVSQISLDAFRGAEKEENQLKEMNLEKSLSNNIQPDLLESQSILVTGSQANIENRKTVNTQETCNENQASNGKASNFALCVNQANSLGAKDSCPTPSTDDASSSSGQGDSANQHTNVGDVPGQNDLSCLDDKFEDLLRQFEAEFGEDFSLPGSEAPSQNGVGPPKQQISGDPQFKMPFPSQLLPSENSTRPDAHSNPALSNNPISHNVSHNLDSLFSSKSPKKIKIESSGAITVVSTTCFYSEENQHLDGTPTKSDLPFNPTLSGFLESPLKYLTSPTKSLIDTPAKMAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEDRFGEKGEAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRALGDSLYSDITETITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEEFLNDNFQDLATKVAPVYQMLAPQSYENQVNNEEVAIDCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTIGRIPEDEQLHVLPLYKVSSTDEFGSEDGQAEKIRKGGIQVLASFPREVRKLSEPAKSCRQRQLDAKKAAAEKKKLQKEKLVSPDKTKQEPADTKMCQQNPGVPQQQTKPCVKVEPSNHYNTYKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKFALPPFGFYGFPNNPVVPNQFMNYGTSDARNSGWMNNSFEKKPDVQSLADGMNQSYGSELPEQSYRRSSEVPHHYSLQNPNSQKSFNISHRTTPSPMETTPYSNLPCYNKVIKKEPVCDPLVDPFQRANSVHSQSPGVNHSLQTSDLPFKANGALPSSGRSNAEGPCSMSLPNDKSGLEKRDYFGVHSNVPALKDKQWTPYGTDVPVGQRDSLDAQSPGKVWSSCKLSDSPAVLPSFASTQTKNWNGRQASLNQGLKEPMPFQEKLWNSVAASDRCSVTPSDRSSVTPCAELQDKNWASFPNPVGNSLKTESSQNHWDPYSLDDNMDDGQSKSVKEEEDEEEIWSDSEHNFLDKNIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPARISLVFYQHKNLNQPNHGLALWEAKMKLLAERARVKEEEAARLGIKQEVKSLGKKRKWGGAATTETPPVEKKDFIPTRQATTILTDSATTAFSYAYTKVTGPYSRFI

Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes, including pax6, rax, sox9 and six3. May also contribute to the regulation of target genes in ways that do not require its enzyme activity.

A0A1L8HU22

NEIL3_XENLA

Endonuclease 8-like 3 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil3) (Endonuclease VIII-like 3) (Nei-like protein 3)

MEALPPQVLKPLDCMSIYSRHREPENRHNELSTGRCGRGHVIFSSMKALQPQVLKPTGSHANLQQVLYAPAATIITAPASSHNDLSSLTGCSYAGVETLGKELFIYFGLKAMRVHFGMNGSMRINQPMKKGQENGRPIPIAVLEVQLTKDLICFYESTVDVRNASECQEKIRFFEELDVCSSKFSFPRAECEIKKQRTRMLCDILLDQMILPGVGNIIKNEALFDSGLHPGVQAGLLTDEQVSHLVKMTRDFTLLFYKCRKSGSALYKHYKVYKRPNCGQCGTKITVCRLGEHNRMTYFCPKCQKDKPQHVDVSKLPTRNSLIGWVQRTASNANEHVATSKEEHWACAVCTLINKPSDKQCDACLTLRPEVSSLAVSDEAAELNTDLVKYPCNNFAKVLPELKLNRRTAFGNTTLVLTDFGAKEGLADKNSQQNILNRSTFDVPLNNKYYHTKTPSNKRSNENEHWTNTLNAVNGHSAASNNVFNHPQKKLKTGHTTSNTIHLSSTISSPQSKMTGDAAAKTGNPQCSAHNVPCALQVVRKEGENKGRSFYTCSLPRERRCQYFEWADLHFPFCNHGKRCIVRTVLKIGPNNGKNFYVCPMGKDKQCNFFEWAKTE

DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA). Mediates interstrand cross-link repair in response to replication stress: recruited to replication stress sites via interaction with ubiquitinated CMG helicase and acts by mediating DNA glycosylase activity. Cleaves one of the two N-glycosyl bonds comprising the interstrand cross-link, which avoids the formation of a double-strand break but generates an abasic site that is bypassed by translesion synthesis polymerases.

A0A1L8HV70

DCK1_XENLA

Deoxycytidine kinase 1 (XldCK) (EC 2.7.1.74) (Deoxyadenosine kinase 1) (EC 2.7.1.76) (Deoxyguanosine kinase 1) (EC 2.7.1.113)

MATPPKRICIDVPASPSGNKCKVKRISIEGNIAAGKSTFVNILKKANEEWDVVPEPIARWCNIQSCKDEFEELTTSQKSGGNLLQMMYEKPERWSFTFQSYACLSRIRAQLKALGGKLKEAENPVLFFERSVYSDRYIFASNLYEAECMNETEWTVYQDWHDWMNSQFGADLELDGIIYLRAIPEKCLNRVYTRGREEEQGIPMEYLEKLHYKHETWLHHRTLRTDFEYLQEIPILTLDVNEDFRDNKQKQESLIEKVKEFLSTL

Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine with highest activity against deoxycytidine followed by deadenosine and deoxyguanosine. Shows only very minor activity against deoxyuridine and deoxythymidine.

A0A1P8AQ95

STMP4_ARATH

Secreted transmembrane peptide 4 (Phytocytokine STMP4) (Precursor of secreted transmembrane peptide 4)

MTKNMTKKKMGLMSPNIAAFVLPMLLVLFTISSQVEVVESTGRKLSWAFNGAPIVFTPPSSSCGGSPAAVMASEWMPRRPCRRTRPPGTNIPVSQSP

Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (By similarity). Prevents general growth and development.

A0A1P8ASY1

JHS1_ARATH

DNA replication ATP-dependent helicase/nuclease JHS1 (Protein EMBRYO DEFECTIVE 2411) (Protein JING HE SHENG 1) [Includes: DNA replication nuclease JHS1 (EC 3.1.-.-); DNA replication ATP-dependent helicase JHS1 (EC 3.6.4.12)]

MPPRKKPKSSALKSNKQSSANHSSQPSTFGIQQLFLRHIQNSQSTSNSHTSTADPVDQQNVNGLASDTAVLTPQNPLGTSNEKPDESKDMDQQLTEASPKISKNLKRFSPGMLIKQSQDDCGGEITWKISPVNERLRAAAKNIPKMMDLTENSLGVKSSTIRPCSLNKLVQKQCPTSGITSKVEQWLSSPSKKASKRPAFATNRVMERVNPSPDAEFEIVNTSSSGNSPFQTPPSLSCPHNKLPCTVTCSGACGSMGAGQHKKALLELLDQVEDVIAVDDKTTDDVGIVMPQARVKDDIISSVVDCAVDEGPVSLPKMQNSINPDSYFLVLEVSEKRGSGSSSKGQCPYKVLRLLDEHTGVECALYLWDEWFYSTVSPGDSINVIGEFDGDGKCDVDRQNNFLIVHPDTLVAGTRVAASFGCPRRTVLDERLRSNEHATVALLGTLQHQVFQAGLSQESPSVDGLQEYASTVIEKSIESLYACGVHEGDVRSTLFKAIPKMLNWIEHFRYSKDSEVSKVDFGSTIGKKAVKVSEVIDIEEMSWAPKYGLKGMIDASVRVIVESDMNTVNEKIMPLEFKSGKAPSGQSSIEHSAQVILYTLLMSERYLKHIDNGLLYYLQSDQTQGISVQRSDLVGLIIRRNELANDILVASTTQQLPPMLRNPNICRNCRHLDVCTIYHKADGGNTESSGLGDVFDTHVSHLSTLHFNFLRHWDRLIDLEGREMQLLRKDIAHPHGSKGSHSASYLSSMVLDVTNGFQHHNSHKETRFIYRFVRQKSSESRERVTSEDMIRTGNLATDDLDCKLRTGDRVILRTEVSHLTVANGIIADISRTHISVSLSKRLRLPWSEPSSEVSNLSHELWRIYKDEFMTSFSVMRFNLMQLFVQNGHNIRKMIVDLEPPRFDNGSILSQDPAISYIWSEKSLNNDQRQAILKILTAKDYALILGMPGTGKTSTMVHAVKALLIRGSSILLASYTNSAVDNLLIKLKAQGIEFLRIGRDEAVHEEVRESCFSAMNMCSVEDIKKKLDQVKVVASTCLGINSPLLVNRRFDVCIIDEAGQIALPVSIGPLLFASTFVLVGDHYQLPPLVQSTEARENGMGISLFRRLSEAHPQAISVLQNQYRMCRGIMELSNALIYGDRLCCGSAEVADATLVLSTSSSTSPWLKKVLEPTRTVVFVNTDMLRAFEARDQNAINNPVEASIIAEIVEELVNNGVDSKDIGIITPYNSQASLIQHAIPTTPVEIHTIDKYQGRDKDCILVSFVRSREKPRSSASSLLGDWHRINVALTRAKKKLIMVGSQRTLSRVPLLMLLLNKVKEQSGILNLLPGDLKP

Essential protein required during embryogenesis. Key enzyme involved in DNA replication and damage repair, shoot apical meristem (SAM) maintenance, and development. Involved in Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is atypical: it cannot load onto its tracking strand internally and has an absolute free 5'-end requirement (By similarity).

A0A1P8AUY4

MDN1_ARATH

Midasin (AtMDN1) (Dynein-related AAA-ATPase MDN1) (MIDAS-containing protein 1) (Protein DWARF AND SHORT ROOT 1)

MAIDGSFNLKLALETFSVRCPKVAAFPCFTSILSKGGEVVDNEEVIHALGDAFLHPEFTVPLVHCFLPIIRNVVDRVVGLLRLVDDLKSSIDYSDDVSSVLDNAMTEGISVIDFYVRRGQRLELHECACLAFSRALHFNTSLLGSILNYFEKAPPPYERILVKDIVSESRMEATDAYLLCLRVSYRFLVIRPEVFSKLWDWSCYLDSMKRLSECPRQQRHFLEKYRDAVWCGIQILSVVLRCSDRLAGCFGFEEEEALSCLLRWEEFCQDIEIEKAGLYIQLPTYTALKSLQQFNTLVPGINKRQSAGLEADEPQMKIRRLDTWDVNSFSEPFEIHSRVKKSFEMVSLAVSQKRPVLLYGPSGSGKSALIRKLADESGNHVVFIHMDDQLDGKTLVGTYVCTDQPGEFRWQPGSLTQAIMNGFWVVLEDIDKAPSDVPLVLSSLLGGSCSFLTSQGEEIRIAETFQLFSTISTPECSVSHIRDAGNSLSPLWRRIVVYPPDRESLQSILGARYPNLGPVAEKLIETFETINSALRPQFSSSTTENSATFSSPSRFSLRDLLKWCERVHGLPSYDGHAVYQEAADIFSASNMSVKNRVAVSEIVASIWNVAVPESQDKPPIQEFSGILKIGRVSLPLGETASHDRSRFVETRTSTRLLEKIARSVEYNEPVLLVGETGTGKTTLVQNLAHWIGQKLTVLNLSQQSDIVDLLGGFKPIDPKLMCTMVYNEFNELARDLKIKDDSKIMKWLQDNFRAKKWHTFLTGLLDIIKGIEGRITERMEGKIGEARSRSGRKRKKPEEELKNCACLRTKVNKIRQQIHSGGMVFTFVEGAFVTALREGHWVLLDEVNLAPPEILGRLIGVLEGVRGSLCLAERGDVMGIPRHLNFRLFACMNPATDAGKRDLPFSFRSRFTEYAVDDDICDDDLEIFVRRFLGGRGSDSKLVANIVWFYKEAKRLSEESLQDGANQKPQYSLRSLYRALEYAIKAEAIGGFQKALYDGFSMFFLSLLDASSAKIVEPIIKRISGENIRSQPLQRYLGELKGSSDKFVGSYVKTKSVIDHLNHLAHAIFIKRYPVLLQGPTSSGKTSLVKYLAAISGNKFVRINNHEQTDIQEYLGSYMTDSSGKLVFHEGALVKAVRGGHWIVLDELNLAPSDVLEALNRLLDDNRELFVPELSETISAHPNFMLFATQNPPTLYGGRKILSRAFRNRFVEIHVDEIPEDELSEILTTKCSIANSHASKMVEVMKDLQRNRQSSKAFAGKHGYITPRDLFRWAYRFRTYDGTSHEELAREGYYILAERLRDDTEKVVVQEVLERHFRVSLAKDDLYNMELPRLDSIQNRKFTWTQSMRRLFFLIDRSYKLREPVLLVGDTGGGKTTICQILSDVKKKRLHILNCHQYTETSDFLGGFFPVRDRSKLITEYENQVKQLELSQALTPFGQDIVICGDISRAEVSIKSVEVALEKYKNGSVIGVAATPQDVDFLEKIRNNMVMLYQKWRAIFVWQDGPLVEAMRAGNIVLVDEISLADDSVLERMNSVLETDRKLSLAEKGGPVLEEVVAHEDFFVLATMNPGGDYGKKELSPALRNRFTEIWVPPITDTEELRSIAFSGLSSLKESNVVDPIINFWEWFNRLHTGRTLTVRDLLSWVAFVNMATESLGPAYAILHGAFLVLLDGLSLGTGFSGRDGQDLREKCFAFLLQQLELFASDTLPLELSRMELYGWGDSKAICEKSKSVRHEGMFGIDPFFISKGDENPEIGGFEFLAPTTHRNVLRVLRAMQLSKPILLEGSPGVGKTSLILALGKYSGHKVVRINLSEQTDMMDLLGSDLPVESDEDMKFAWSDGILLQALKEGSWVLLDELNLAPQSVLEGLNAILDHRAQVFIPELGCTFECPPTFRVFACQNPSTQGGGRKGLPKSFLNRFTKVYVDELVEDDYLFICRSLYPSVPSPLLSKLIALNRQLHDGTMLYRKFGHDGSPWEFNLRDVIRSCQFMQEAIHDLEVESFLNVLYIQRMRTATDRKEVLRIYKAIFDKTPSINPYPRVQLNPAYLVVGTAAIKRNLNQSNIASEQLKLLPEIRQNLEAVAHCVQNKWLCILVGPSSSGKTSVIRILAQLTGYPLNELNLSSATDSSDLLGCFEQYNAFRNFRLVMTRVEHLVDEYNSLLLQSSQEALFSNRSGLVSRWLSYLNKIDSSLVENPLFFLNDSETLSTLEEVVEDLEQVLKEGVLPVSWSKKYLEQISKTILQLQTHEKKQSTKFEWVTGMLIKAIEKGEWVVLKNANLCNPTVLDRINSLVEPCGSITINECGIVNGEPVTVVPHPNFRLFLSVNPKFGEVSRAMRNRGVEVFMMGPHWQLNEDGSNCEELVLRGVERFLALSGIPGYKLVTSMAKAHVHAWLNGQSFGVRITYLELEQWVHLFQLLLMNGNQLLWSLQLSWEHIYLSSLGVTDGKEVVDFVRETYLSDVELSELDSFMGGDLYLPGGWPKPFNLRDLTWYSRETTVRQNCMYLEFLGAQYASHQPKISDNVKSRDRELAAGEPRIIYSIDSWTLKKVLFPKALIGSSCAPDAANFENDLASKMLLFAANWTIEQATEEDIQLYLAWFSWFGSRLQQHCPFLLCFLNTLKVEFEHPIWNHISRCRKNLKFLCRLDPDAVPIPMLSSKLIDVAASNDQSKPYSKSLFESLNSVGVLRRSYQQWLVESNDNHTDVSTFTRFLDSLRVLEKKILCEIVGAPSFSVLIQLYTEVIDNHSFFWSGLVSSSDEYLLFSFWSLIKSIKKMHSFFPGEVQVVLEESKNINNIVLHGHPEKSMLWAYGGHPSLPVSAELFHKQQEFLQLCSTVWPLKSESDEHGNDHLTKAIPFSGPELCLLALEGLCISSYIADEDDVDYVAAVQLDEIYQTFLERLKLEKKRLEDKMGFSEIDNTENITASCCVFCPEIVTTGSGFSSWVKTCFIASSESCSLDVELLAALQHLLVARPTEHQDLVDIRKLLKPALEYSLSSTRPPQTLVAHQKLLWAIDAHASELGVDTKIAGFALEIWYWWHSVLWKNSQIGLMNISDTGNCQILSPSMLIQPVKTATVAQILENVFSVKDYSVQSMKLLSASRYLWKSSQPYQEMPGSLLSIARSLFQQIIYTHQKSFESETFVAIKSVFHAIEKKQNKMDGIQNLISLIGSSSHNKLKSVTHSFVGPLAKRLYSDSSSNALCPTFVEFYCNLGLAWLYLGGLRFHLLNSLDVIDPAMKITCKLLKLEEKISSLELNIKVRGECGYLSGLLYSGNNDESSEHTLSKLKTEHKRLQRKVIFRSDPKKYQDLRRALDEFAGFLTRPISLVNDIEVLDWNQVVEQVFNWQETAISFIDRMSSDYSEYVDITQPIQVSVYEMKLGLSLFVSGALLGKLLNRFDIDMVDSVMETIYALMRFPRDSSIASTTYTECLPPLHLSHGANSRAKSLGLDVGLLHKLISVSSAEDSRKASELQLKVALYKNLHARVLQFVANTGLLDEASFELLDKIYVELARIWMEMKFQAKTKADNLPGLYKFRSRDFKIDSVMEVDISALGKYFPNESFSEWQEYLADDDTKNVKDMTHIDQDEENLEDDWDLIQEHLDSIYSTHNELFGFCDLSEKSGRFCITDSRRLDSFTDSYELGVSMIKGLRGLFTSSLDAKLVPEHLLRLCLENKKNFTSNYQSASKYNFYKDLDGPELGKMVKFLTPLQQRINSLLQEREDHPGLQKLSGVLQMLLAIPSSTPLAKALSGLQFLLCKVHKLQEEGCKLPISDLLEPIISLASSWQKVEFERWPTLLDEVQDQYELNARKLWLPLFSVLFQKDAVEISEHENESISQSLVEFIETSNVGEFRRRLQLLFCFLLQLSMGSSLGIYSSDSHKRRVEMCYNIFGFYIQFLPVVMEQLDLNRKNVETELKEVLKLCRWERPDNYLYNETTKRTRQKVKKLIQKFTDMLRLPVMLVKPDLTKERAQFLPLLDPDLMDGASDMRIEVLVSALDAEQLRDRSSWYVVWWNKLKESVGRFHQEMHYKTLLMGAEHQYSSPVYQGDWKNLWSTVARIGETIAGCSDLWRNSDRDVAKKRALFELLKLLESSGLQKHKFENIEMSNHFKGLLYQPAYDPKHLLLLTHTKSNIHPSMGVEDQNKENSLVEWRVANEFYFKSLASVQLMLNIDRKHSDVTAEQVKRAISFLNHLVEIQRQQRKSAYAFAELFNRFRQCVLSLARLLGDSVGADRKDDSVFSFPQNQHAVFNCLWLQKQLFDNITAMLLEESALLRTVGSTHLDSCQAVKTSSRSLLSFIEILIPIAQNSKASLDRLLLDCNGFIITPSSSLKQFVTQHMVQVLRQNFDQLTDLENQISSFCENNEKSYCRDVLLSQFSPVFKEGKLLAENLNCLLNVRDQSTGMEPKERLFLEENLASIFANVKDVIGKLCSYKDGSLSQEEEMNITTWDGLFKKAENDLNLDNLCKLLSESFGSIEQLLNSSGVLSAGVGDQLKQLQAFLDLLLSFGDCYLKEFLAISKTVSLITHVLASVLADLFTKGFGISKNEEDDDSKVDKSEAAEGTGMGDGVGAKDVSDQIEDEDQLHGTDKKEEEEKEQDDVLGKNKGIEMSDEFDGKEYSVSEDEEEDKEDEGSEDEPLDNGIGDVGSDAEKADEKPWNKDEEDEEENMNEKNESGPSIVDKDTRSRELRAKDDGVETADEPEESNTSDKPEEGNDENVEQDDFDDTDNLEEKIQTKEEALGGLTPDVDNEQIDDDMEMDKTEEVEKEDANQQEEPCSEDQKHPEEGENDQEETQEPSEENMEAEAEDRCGSPQKEEPGNDLEQEPETEPIEGKEVMSEDMMKPNFRNDNISGVESGSQNPHGSNVLGAGSTAPQENLSATDVTDELTDSMDLPSSSNTEMNLMMTNMANGETLTDNLPKMEFPQNQSSTAQQTKVNPYRNVGDALKEWKERVRISSDLGEKQEAENEMEDPDASEYGFASQFDAGTSQALGPALPEQVNTDMREGESEEEKLAGNQDDVSPMDIDDLNPENKPAVQSKPSISNSIAEQVQEPDTDRTHQENSPIHNFGDGNSRMDSMVSVDNTFLGEEACNLDRMQVTDNDSESNQDNQEDPDARSNAVVLWRRCELLTAKPSQELAEQLRLILEPTLASKLSGDYRTGKRINMKKVIPYIASHYRKDKIWLRRTKPNKRDYQVVIAVDDSRSMSESGCGDFAIRALATVCRAMSQLELGSLAVASFGKQGSIKMLHDFGQSFTTESGIKMISNLTFKQENLIEDQPVVNLLRNMNEMLENLASTRRQSYGSNPLQQLVLIIGDGKFHEREKLKRTVRSFLQQKRMVVYLLLDDAEQSVFDLADYVYDGERRPYKKMNYLDSFPFPYYIVLRDIEALPRTLGDVLRQWFELMQSSRD

Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. Functions at successive maturation steps to remove ribosomal factors at critical transition points, first driving the exit of early pre-60S particles from the nucleolus and then driving late pre-60S particles from the nucleus (By similarity). Required for female gametophyte development. Involved in the expression regulation of genes related to plant growth and development.

A0A1P8AW69

KTN81_ARATH

Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.1

MAKRGYKLQEFVAHSGNVNCLSIGKKTSRLLLTGGDDYKVNLWSIGKTTSPMSLCGHTSPVDSVAFNSEEVLVLAGASSGVIKLWDLEESKMVRAFTGHRSNCSAVEFHPFGEFLASGSSDTNLRVWDTRKKGCIQTYKGHTRGISTIEFSPDGRWVVSGGLDNVVKVWDLTAGKLLHEFKCHEGPIRSLDFHPLEFLLATGSADRTVKFWDLETFELIGTTRPEATGVRAIAFHPDGQTLFCGLDDGLKVYSWEPVICRDGVDMGWSTLGDFCINEGKFIGCSYYRNSVGIWVSDISELEPYGAVSEDKNECMVKRFSVLNDQSERMGSGPRGSVSPDYETREIKNIYVDCGNLNVAQNPGSLKATLPLESGKVATMVSEKQNAAYFGPAGDKYSSTSRDSDSGEESSYSERESIPFSRTKSGMLLRPAHVRKTLAKFEESKQSAVVQSATRKKSGLAVEEEPQTQNAFLSEQNASKPFDAEDSIIKGITNKFEKALSSEPPTDEANRMFLKPPRIHRSSNSKYNDTRRAMSADPATFGKGGMENSGDVEDIPSKTERVLSREKPGDEQKNTEYPSGSRELNPVKIVEGVNVVSGRTRSLVEKFERGEKTTHTEGASTTIEQNNNAVQEDPRKTSRQTGETPVISTRRARSTPARVMPIVLNRDSNVTSDEPPLTQPARTSSFPVMPVILNQASNVTYDEPSVALTQESRTSHARILPVTFNQATNITSEEASVTLRRQRRNSAARVRPVLLSQATSHECPVTSVRPLRTSPARVMPTKLNQSVNMTSDTSHIASMHRVSPTQMLATPTVIDQVADMTLDETHATQIQPACDNMPQKEEPNISDREDDSDITENLMLTHNEFLSTLQSRLTKLQIVRHFWERSDVKGAIGALRKLTDQSVQADVISILTEKIEILTLDMFSQLVPVLTSLLGSRTERPVNVSLDMLLKLVAVFGTVIRSTVSAPRIVGVDLHANERLEICQICSAGLHKIQRILPVLARRGGLITRKAQELNLVLQEP

May participate in a complex which severs microtubules in an ATP-dependent manner (By similarity). Microtubule severing may promote rapid reorganization of cellular microtubule arrays (By similarity). Confers precision to microtubule (MT) severing by specific targeting of KTN1 to MT cleavage sites such as crossover or branching nucleation sites. Together with other KTN80s, regulates cell elongation by modulating MT organization. {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:28978669}.

A0A1R3RGK0

OTAA_ASPC5

Highly reducing polyketide synthase otaA (EC 2.3.1.-) (Ochratoxin A biosynthesis cluster protein A)

MTFTSHPQSEPLAIIGLACKYANDINSPLDLYQQVMAARSMHGPMPPSRMDAAFYYHPSSEATGTTYAKGGYFLQSDLNAFDSPFFQLSEIDVLAMDPQQKMLLENVYHALENAGIPLKDAVSSSTSVFVGCSNNDHLALANADLLLALKGKGTGTSPSILANRISWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSTMSIISGVNLMEHPAPTMYLSSLGVLSPDGRSMSFDARANGYGRGEGLGTVIIKPLTAALRDGNRIRAIVRSTGSNQDGRTPGITVPSPTAQERLIREVYKAADLDPSRTGYVEAHGTGTPVGDPLEVQAISAALGMSRDSPLYVGSVKSVVGHLEGGAGMAGLISATMAVESKTIPPVAGLQTLNPRIPQRPDLKFAKEATPWPREDVRRASINSFGFGGTNAHVVLEDVEGFFSDLFGQQLPGALQLSEVTSKALVPSAMKSAVNGIPADQPPKESSVNRLFVISAFDEAGIQRNAASLASHLESMRAITGSDGEERLLNDLCHTLNEKRTRFDWRSYHVADSIDSLRNSLQNPRPIRQSPAEKVVRFIFTGQGANWAGMAYDLLVYPLFRRRIQEAAIFLKELGSDWDLYERIASQSGELDEPTFAQSSCVAVQVALVDLLASWNVTPQTVVGHSSGEIAAAYCAGQISRQAAWKVAFCRGQVCARRTDGQGRMLAAAMPVTQLEQLVARVNKGQSTAVKVGCYNSPKNLTLTGRAEDILRAKLELDDVGALNRLLPVKVAYHSDYMRDAAPEYLDLLGDLDFGDSIHADAGIKMVSSVTGRAVSAGEAQQPSYWVDNLVSPVRFSTALLASMDDPSATGAREDALIEIGPHSTLRTAIKETFADVREFQSIQYGSLLKRYETDGSTILRTFGMLVCSGHKISLAAINDRRVGAKKTPRLLTGLPSYAFDHSRSMRGTSRRIEQAKFPAYKRHELLGVPVEDTNPVEQRWRNILRPDDLPWLRMNRMNGQIHFPGVAYLLMATEAAIQRVGNTVAISGVRLGNVSMLAPLPIPDSAAGVEIQFSIYPMKIHANSGTDWSTFRIVSYDSAEKTWTEHCVGSVRVETGPHESHEPHPGNATREECTESVDIAQMYSRFTTAGMDFGEYLRNIQEMKLSPDHQACTATITAPDIPCQAHDHYSLHPCTFESILHALLHLCKSSQGPMVTTYIEEVLVLSPQDTGVCGFEACAQTQRASATTWRSDVTITANTGRQQIRVTGLDLVQLPPSEDASDAESFYVVKWKPDVKLLTSVDALRDSASMYVAQHLPTLDEHEGFQLASGIFLLDTMDYVTRTGLPALPQHHQAFMQWMEKECRSIADGTVPLLDTALFEGIRASPDRRRELLARVAQLSARGELLVRVGTQMVPILEQKIDCLEVMFGPDNLMDRTYEEGLPGQIAPSVAGYLHCLAHAQTGIKVLEVGAGTGSATKVILDSLKPTERQDGGGLVSSVSTYHFTDISAAFFEKARARFPDWADILRPKVLNIELDPADQGFEMGSYDLVIATHVLHATADLSVSLKNIRGLLKEGGDLIVIENIQPDLMCSPLAFGLLPGWWRSVEPYRKTNPLITKDQWDQELRNAGLQSRLLIDDTDEGVNEMTAFVASRVREPPATQHVCSIIYSSRYGGQYELASQVARDLPPSCTASLVDLADISPEHTSTIGIVLVGYQGLDLSELSAHEYDRVNFLLTAFHRLLWVTCDEDEVPKSAMASGLVRTARWERDHDGVNFILLGISHRVPSASAAVSQMIRVCDHAFFSHELVPRNAEFRLEGSVLLTNRLFPATGINECIASSSRPRSKQVALEAVQHPVKLTSIGPHQPNGFHFVEDPQVDEPLLPDEVKIQIRAVGLDESDVEEMNRLIPGESAGSQGTGVVVEVGPAVHDIHVGDRVMALRTGHSGSLQTVLRTHSSAVTQVPEGLSLADAAAVPLPFTTAYHGLVNVARLEPQDTILIHNAGGATGQAAVQFACMLGATVYATVESDAQRQALLDYGVDRSRLLDGPSFAQQLARRGAKGSVDVLFNLSRESLEDRDLACLSQFGRLVGVHGQGSLPAGPTNRSYATVSIRELVQVRPKALHGTLRTISDLLTSRAIRPITPVRAGYSELQTVLSQIRQGNAGPWVLEPRANDTIPVAMKPLGDYQFDPCASYLLIGGFGGIGRSVVRWMLTRGAKNFIFLSRSGASSVPAKQLCADLLDAGCGVSDTVCDVTDATAVENALQQCGKSMPPIRGCLQCSMVLEDSMLSNMSHAQFLNAITPKVQGTIHVASALSSVKSNLDFFVLLSSSAGIIGNRGQANYSAANAFLDAFAAHLVSRGYPATSISLGSVLSVGWVAENQDRLPIALSYGAISEDLLLAILEYHMDPSWGAAQSPGTCHTVAGVRSARDFQRQSIPLPGFMAYPLFSPLRAIAGASQTAEEVAEAPIAQGLRGATSMEDAVELVTRAIVYKLARIMALSAKEIDAQRSLASYGVDSLVTVDLKAWFQREVGATVASGDLLGDSTIVQLAQQAAGGSRLVSVAMKGTE

Highly reducing polyketide synthase part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties. OtaA catalyzes the condensation of one acetate and 4 malonate units to form the isocoumarin group. The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable).

A0A1S3PBB7

KNG_SALSA

Kininogen [Cleaved into: Bradykinin]

MKLGVRLCVLVVFSLQLWGPGQGQELEPEQVLAFCDDKDVEAAVDLALVKYNQKLPYGNQLALYQILESSKAQNDSCTQYFVEFNSRVTDCPAGGDKVWRDCDYLPTGNKVPRPCKATVHMSETDKKVLAVFCDPVEAPVVAERTTCLGCPREIDVESEDLKDPLTYSITRFNADSDSSHHFILNSVGFATRQVVAGFRYRLMFDMRKSNCSKADHKELNDECHPDPDVELAHCNSTVDVAPWRHETAEANVECAPGPLDNFDVFRRRPPGWSPLRNFNNFAEVKTTQASTASAKEESSEESQERSPSAVTMANPEPALPSVAPTTAAESPFHCPSKPWKQFVPPTTLRPAQEKSPTPLPVVEEGLSDLDLLGKK

Inhibits papain and ficin (cysteine proteinases) but not trypsin (a serine proteinase).

A0A1S3X835

MBP2C_TOBAC

Protein MICROTUBULE BINDING PROTEIN 2C (NtMBP2C) (Movement protein binding protein 2C) (TMV-MP30 binding protein 2C)

MYKPQQQQQLFDLQDNNGAAFDNGGTDPSCWLSHENEISRTDSSLSSSNVDPLLFNDLVQIVPLVQSLIDRKEKSSFTRRGSMTYTKMPSRESLYKKTSEVKGRNAGQSTATKKHRDQNKNVSSSQDGYAENFSTPSSTSSLTEKDREELMTLREKVEDLQKKLLEKDELLKEAEILKNEITATNAELDEMKKDISEKDFLVKTTQVQLSDALVKLADKKAAVEKLEWEAMTSSKKVERLQEDLDLLQGEISSFIQFVHALTGNDSRDSAEECNVIPYPWDQNVEIDKLNERDLQKMEAAREAYIAAVAAAKENPDEASLSAASTARSYLQSLVLRT

Prevents homeodomain proteins (e.g. STM) association to plasmodesmata and, consequently, cell-to-cell transport. Binds to RNA. Alters KN1 RNA-binding capacity. Regulates cytoskeleton (e.g. actin) organization that determinates cell shape (By similarity). Interferes with cell-to-cell transport of tobacco mosaic virus movement protein (TMV-MP) by mediating its accumulation at microtubules, thus interfering with cell-to-cell virus movement.

A0A1S3XSG2

DAO1_TOBAC

Diamine oxidase [copper-containing] 1, peroxisomal (NtDAO1) (EC 1.4.3.-) (Copper methylamine oxidase) (EC 1.4.3.21) (N-methylputrescine oxidase 2, peroxisomal) (NtMPO2) (EC 1.4.3.-)

MATTKQKVTAPSSSTAPCCPSTSILRREATAAVAGVGDGLQNWNNVPSVDDKQKKTASSALASLASTEPLSSNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLLEPDKSVVALADAYFFPPFQSSLMPRTKGGSLIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVISSNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPADPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYIEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEEFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGFFNCSPAVDVPPPSACDSESRDSDVTETSVAKSTATSLLAKL

Involved in putrescine catabolism in peroxisomes. May also be involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins) nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Oxidizes preferentially non-N-methylated amines.

A0A1S3YCW2

ADC1A_TOBAC

Arginine decarboxylase 1A, chloroplastic (EC 4.1.1.19)

MPALGCCVDAAVSPPPGYSFLWDSSLPAPEIFPSGVPPSTNTAVATTTTTHWSPAHSSALYSIDGWGAPYFTVNSSGDISVKPHGTDTLPHQEIDLLKVVKKASDPKNLGGLGLQFPLVVRFPDILKNRLESLQSVFDYAVQSQGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSCLCKGSHEGLLVCNGFKDAEYISLALVARKLMLNTVIVLEQEEELDLVIDISKKMAVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVKKLEESGMLDCLQLLHFHIGSQIPSTALLADGVGEAAQIYCELVRLGAGMKYIDCGGGLGIDYDGTKSCDSDCSVGYGLQEYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTTTRSQELSSVDLQSFVEKLNDDARADYRNLSAAAIRGEYDTCVLYADQLKQRCVEQFKDGDLDIEQLAAVDGICDFVSKAIGASDPVRTYHVNLSIFTSVPDFWAIDQLFPIVPIHKLDERPVVRGILSDLTCDSDGKIDKFIGGESSLPLHELGSNGGGGGDGGKYYLGMFLGGAYEEALGGLHNLFGGPSVLRVSQSDSPHSFAVTCAVPGPSCADVLRAMQHEPELMFETLKHRAEEFVHNDDEQEEDKGLAFASLASSLAQSFNNMPYLVTNSSCCLTAAANNGGYYYCNDENIVGVGAESAAAEEELWPYCVA

Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins) nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Required for the biosynthesis of putrescine (By similarity). Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine (By similarity).