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A0A009IHW8 | ABTIR_ACIB9 | 2' cyclic ADP-D-ribose synthase AbTIR (2'cADPR synthase AbTIR) (EC 3.2.2.-) (NAD(+) hydrolase AbTIR) (EC 3.2.2.6) (TIR domain-containing protein in A.baumannii) (AbTIR) | MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR | NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide. In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR). Cleaves NADP(+), but does not cyclize the product. |
A0A023I7E1 | ENG1_RHIMI | Glucan endo-1,3-beta-D-glucosidase 1 (Endo-1,3-beta-glucanase 1) (EC 3.2.1.39) (Laminarinase) (RmLam81A) | MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEAPLLTYAYAHHLTSIDDSNVKRTDMTLQSATKGPMTALVGNEWTLRETELSPVEWLPLQAAPNPTTINEIMTEINKDIASNYTQETAKEDNYFSGKGLQKFAMLALILNKSDQTQLRNPELAQIALDKLKAAFLPYLQNEQADPFRYDTLYKGIVAKAGLPTSMGGTDDLSAEFGHSYYSDHHYHQGYFVVTAAIIHHLDPTWNADRLKAWTEALIRDVNNANDGDEYFAAFRNWDWFAGHSWAGGIKPDGALDGRDQESVPESVNFYWGAKLWGLATGNTPLTKLASLQLAVTKRTTYEYFWMLDGNKNRPENIVRNKVIGIYFEQKTDYTTYFGRFLEYIHGIQQLPMTPELMEYIRTPEFVSQEWDEKLGAIAPTVQSPWAGVLYLNYAIINPAEAYPALRKVQMDDGQTRSYSLYLTATRPHFFRRSLLAALARHGSTRRPSLPSSGDDDKHEDGFLLRFRRLNPFNLKHRIY | Cleaves internal linkages in 1,3-beta-glucan. |
A0A024B7W1 | POLG_ZIKVF | 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)] | MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL | [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 (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Inhibits the integrated stress response (ISR) in the infected cell. [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 (By similarity). In addition, host NCAM1 can also be used as entry receptor (By similarity).Interaction with host HSPA5 plays an important role in the early stages of infection as well (By similarity). 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 (By similarity). Antagonizes also the host MDA5-mediated induction of 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). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly. Disrupts host centrosome organization in a CEP63-dependent manner to degrade host TBK1 and inhibits innate immune response. [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 inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly. Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly. [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm. 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. May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes. |
A0A024SC78 | CUTI1_HYPJR | Cutinase (EC 3.1.1.74) | MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS | Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle. |
A0A024SH76 | GUX2_HYPJR | Exoglucanase 2 (EC 3.2.1.91) (1,4-beta-cellobiohydrolase) (Cellobiohydrolase 6A) (Cel6A) (Exocellobiohydrolase II) (CBHII) (Exoglucanase II) | MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSRVSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRALRGLATNVANYNGWNITSPPSYTQGNAVYNEKLYIHAIGPLLANHGWSNAFFITDQGRSGKQPTGQQQWGDWCNVIGTGFGIRPSANTGDSLLDSFVWVKPGGECDGTSDSSAPRFDSHCALPDALQPAPQAGAWFQAYFVQLLTNANPSFL | Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units. |
A0A026W182 | ORCO_OOCBI | Odorant receptor coreceptor | MMKMKQQGLVADLLPNIRVMKTFGHFVFNYYNDNSSKYLHKVYCCVNLFMLLLQFGLCAVNLIVESADVDDLTANTITLLFFTHSIVKICYFAIRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGGTTMLAAVAWTVLTFFEHPIRKIVDPVTNETEIIELPQLLIRSFYPFDAGKGITHVLVLVYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSADHLRDGDNPPPPPPPQSDNMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTKKQEALVRSAIKYWVERHKHIVRLVTAVGDAYGFALLLHMLTTTITLTLLAYQATKVNGINVYAASTIGYILYTFGQVFLFCIFGNRLIEESTSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK | Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Can form functional ion channels in the absence of an odor-binding odorant receptor (By similarity). Plays a central role in the perception of olfactory stimuli in ants and is essential for ant social organization. Required for pheromone sensing. Also required for the development and maintenance of odorant receptor neurons (ORNs) and of antennal lobe glomeruli. |
A0A044RE18 | BLI_ONCVO | Endoprotease bli (EC 3.4.21.75) (Blisterase) | MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAFYRGVKAGRGGKGSIFVWASGNGGSRQDSCSADGYTTSVYTLSVSSATIDNRSPWYLEECPSTIATTYSSANMNQPAIITVDVPHGCTRSHTGTSASAPLAAGIIALALEANPNLTWRDMQHIVLRTANPVPLLNNPGWSVNGVGRRINNKFGYGLMDAGALVKLALIWKTVPEQHICTYDYKLEKPNPRPITGNFQMNFSLEVNGCESGTPVLYLEHVQVLATFRFGKRGDLKLTLFSPRGTSSVLLPPRPQDFNSNGIHKWPFLSVQTWGEDPRGKWTLMVESVSTNRNVGGTFHDWSLLLYGTAEPAQPNDPRHSSVVPSSVSAESPFDRITQHIASQEKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV | Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. |
A0A059TC02 | CCR1_PETHY | Cinnamoyl-CoA reductase 1 (Ph-CCR1) (EC 1.2.1.44) (Coniferylaldehyde synthase) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase) | MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPIPTQKDEPIIRIQP | Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Mediates the conversion of feruloyl CoA to coniferylaldehyde. Also active toward p-coumaroyl-CoA and sinapoyl-CoA. 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. |
A0A060A682 | HAP2_TETTH | Hapless 2 (Generative cell specific-1) | MKFLAFGLIYFHFCILNRCEYITSSTIQKCYNSSNEPNNCSQKAVIVLSLENGQIANTEQVVATLNQLSDSGVNKQLQNSFIFEVTKSPVTALFPLIYLQDFNSQPLEQVIATTLFSCKDGFYDSSPTCKFQYDSKGQKILDSQGYCCYCSLSDILGMGNDLSRGKVCYALNLGAGSATAHCLKFSPLWYSAFKIQQYQLYFEVNINIYTVDSQNQKNLKQTLKLSTSNPTMKSSDNSTISKIIGTFTPTQPPADLSSYYLVKPSFPATDPRVLQGISSWMFVDKTMFTLDGTQCNKIGVSYSGFRQQSSSCSQPVGSCLQNQLENLYQSDLILLSQNKQPKYLLESQGNFNQVQFQGQTILQQGLSGSASTLITIEIDAAQIKFVTNLGIGCISQCSINNFESHSGNGKLVALVQNQGNYSAEFVLGFNCSSNVQPIQGQKLFLTANQLYNFNCSVSVNSDISAINNNCTINLYDAIGNQLDSKNILFNTTSTNHTSNQGNNTGQQQSSQEYKSSQSCSDKCSSFWSFWCYFSAGCIKEAFKSIASIAGVASALALVIFLAKNGYLVPIIRFLCCCCCKSKKKENEKNKDKTDKKSIQESCSYDRSCCSHSISQSYQVENKNKYKRSKIQRSFSSESCQDKSKKIINELSNLEETFEANKLYANIDKNSSIFEYFGFKKSFTFILYERNDILFLPQNSTILDMIGALQPQKGSYLAQKFLEIVNKNALKVVSTSPLYLLIE | During fertilization, required for the formation of intercellular membrane pores and subsequent exchange of gametic pronuclei between cells. Probably initiates the formation of intercellular membrane pores by inserting part of its extracellular domain into the cell membrane of the adjoining cell in the mating pair. Mating requires the presence of HAP2 on at least one of the two cells. Mating efficiency is high when HAP2 is present on both cells, and is strongly reduced when HAP2 is present on only one of the two cells. |
A0A061ACU2 | PIEZ1_CAEEL | Piezo-type mechanosensitive ion channel component 1 | MTVPPLLKSCVVKLLLPAALLAAAIIRPSFLSIGYVLLALVSAVLPPIRKSLALPKLVGTFVIITFLFCLAVALGVGSYQISEQVVHKNDRTYICNRSDTTLFRSIGLVRFHPTGTFESTRAFLPEIIATSAALLTIIIVMFLSHRDEQLDVVGDVVTVRSESGREQRRQRKLAAIMWSAIGNSLRRLTNFVLFLFTAYVGIVKPSLSNSIYFLAFLFISTWWSTYTPLRHGVYNQIKKFLIFYSALHFLVLYTYQIPIVHHSWLPTGSFLPRLFGLTVLMDSSCPEWWKFPFVAPDFNDDDLIMKWPLYANPIVVLVFFYLTVAQYKFTRNGSREYIDDNEYGSSVHEERFVSAGTVETNVDDVGQLISISESTASAPSGRGRGNTLLLSNASSSANDDEQGRARSRSPLRNGEEQGSIPLRKVTSQVVDRNKLSNIFNTTAPGDKESAASKGMIAVMTFVIFHSYSIALTAMMTWALLYHSIFGLILLILTCILWIFRDTRKSSFAMAPIILMYIEFLLILQYFLSMDIHAEIGDPAWMNFVGIEWTTLPVHAVIILCVQTLLTLPVFLLLRLARREKFYESLSDYERQRRINSYGTFGASKTGAGGVAVAKFQDPKSRKFAAFVEYLSNKVSVYFIFVVSVVLLVVSTCFAPNFYNILFFALWALNLIYLKFSFRLYRGLAYAFWLTLTFYTSIVIIALYIYQFPGVSQWIIRNTSLSQEWLNAIGLVDFRAIGESGALFLQLLAPIALFVVTMLQLKFFHGPWSRATSPRRAENDPPTSTTEAAAVASTSGTQGRAHAAGDTLVKKLHKLANQTIELLWRFFEVHISKIVFVIIAIFIANNINALYIPLVILLSLAICLPSAADGIFSLFMCAYLFLVALSKMIYQLDIVPELSQIDRGVGADNCSHGNISMPEWFGLKKEVEGTEPIYMLFGVIVSIIALAFQSIVIYRQRHYRASLGLPESMRAKVFPDFHHSHFDRSLKNAIQFLIDYGFYKFGLEITMIAIGIDIFNRMDALAAIQCFWLVLFALNKRVFVRRIWVFYVIYMAILYPLQFFSYVGLPPDSCIEYPWSYWIPSYSDDARFNLSYLLNLSIYGVNWPSAYLIGDFFVLLLASCQLAVFRREGEDNDSIYNDGNFVIKPENPQYDFIDTKKSYVDYFKSFVFHYGHWITLMSTLAAGIAGTSLFALGYIIFTLTMLWSGNNLYVMNSTLRSFEHTLKRWNALLGYTLFTITMKVCLQIFGCVFLSWFDQSGGWGKTLCIVRQLFSITCVNNECHVLKELEDFSKACAVETKEGNIGFDVIALSFLVFQIRIFHSWYFQHCMVEYRSEVILANRGAVLKNQLIEKEMKEQNEQQKAKFNDIRRRTEAIRERYQKQIERGAAERDFEPVTYGHAKRAGDYYMFKYDPENDDLVEPVDSFVPEVDPKATAYDRLDPGQIMYAATAHDLDLAKTVQQVKKGDTIKDPDSRALIAVSEPEARKPGGTEETDGDEDEDNKDSKVESTAKFIQKMIASALDLCSVTLNKLCREHRYVGFVLSKEKQKLKSGHSESLSNTSRKLTDIRSAVDLPSLQLVQSANDVEKMETAVSVDWQQKSSATRLLNAVVNCIGAHTDILCYFFAIMTQVMTGGLITLPLPLMSLFWGNLSNPRPSKFFWVTMITYTECVIVIKFVCQFAFMPYNSITWRTEHQMDPMSLDKLFGVSQRDSFALWDIVLLFSLFFHRYMLRKLGLWKDANLTDTFTLKEEPRSASGSDTGSPKKIAQEPKVVVTQSDTLEGTSGGEIVIPSDPNAVSNMEELDCEPPIPEKQSGPIGRFIHQLFHPKFRYIRDLYPIMFGIDVICFLIMTFGYSAFGEGGSGNVLDDVKASRIPVTLVVMLVGMTLAIIIDRALYLRKSVVGKLIYQVLMIAFLHIWVFLVLPNMTRRSAISNHVAQALYVIKSCYFLVSAWQIRNGYPELCIGNLLTHSYGMTNMIAFKVFMNIPFLFELRTAIDWTWTDTSMPLFDFFNMENFYAHIFNIKCARQFEAAYPAPRGIPKGKLVKYMMGFPIIIGVVIFIFSPLLLWSLLNQIGTISMPEKVTLRISIEGYPPLYEMEAQGSNHDNAELGMIKPDQLASLNQALTDSYTTRDTNSILRSRMSVSYLKGYTYEDILIVRFRPESEIYWPISQDSRNAMIDKLSRNTSVNFEVSLEFTRPYDPNENAALKHSKSWLVPISLDMTIRAKIQSALRGDPGHPILIPQSIPAFIQVPNQGELTLPTSIGNTIINDGNPRINTTGMEKSDEARAWFDSLTLNLEQGKSQNEKMWIATSEHPGDQNAKLWIKTANTTYSGRPYLQVVGFIDRAFPSFLAKVFKGGVIAVYLSVILVVGRGLVRGIFTTSPSTVMFTELPNADHLLKICLDIYLVREAKDFMLEQDLFAKLIFLFRSPATLIEWTRMSKKKQE | Pore-forming subunit of a mechanosensitive non-specific cation channel (By similarity). Generates currents characterized by a linear current-voltage relationship (By similarity). Plays a role in reproduction by positively regulating inter-tissue signaling to promote oocyte maturation, ovulation and fertilization, and sperm navigation from and to the spermatheca. May play a role in regulating cytosolic and endoplasmic reticulum calcium ion release. |
A0A061AE05 | PAPSH_CAEEL | Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase pps-1 [Includes: Sulfate adenylyltransferase (EC 2.7.7.4); Adenylyl-sulfate kinase (EC 2.7.1.25)] | MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSDDKEDSWPMMDDINQSIPIVLPISDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLESGNWLLGGDVAVVQKIQFNDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLAEHKNPILLLHPLGGWTKDDDVPLDIRIKQHEAVIAERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQKPGSPDALYETTHGAKVLSMAPGLSALHILPFRVAAYDKTAKKMSFFDTSRKEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGYYKSLQNSN | Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). Required for normal growth and development. Involved in several aspects of both embryonic and postembryonic development, including molting, changes in cell shape, and patterning of epithelial and muscle cells. |
A0A061I403 | FICD_CRIGR | Protein adenylyltransferase FICD (EC 2.7.7.108) (AMPylator FICD) (De-AMPylase FICD) (EC 3.1.4.-) (FIC domain-containing protein) (Huntingtin-interacting protein E) | MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITILKEQRSEYYHVLEVANEGDVRPFIRFIAKCTEVTLDTLLLATTEYSVALPEAQPNHSGLKETLPVRP | Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context. The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place. Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity. Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). |
A0A067CMC7 | HTP3_SAPPC | Endonuclease Htp3 (EC 3.1.31.-) (Host targeting protein 3) (RxLR effector protein Htp3) | MLEVPVWIPILAFAVGLGLGLLIPHLQKPFQRFSTVNDIPKEFFEHERTLRGKVVSVTDGDTIRVRHVPWLANGDGDFKGKLTETTLQLRVAGVDCPETAKFGRTGQPFGEEAKAWLKGELQDQVVSFKLLMKDQYSRAVCLVYYGSWAAPMNVSEELLRHGYANIYRQSGAVYGGLLETFEALEAEAREKRVNIWSLDKRETPAQYKARK | Effector involved in the disease saprolegniosis in salmonids and other freshwater fish, resulting in considerable economic losses in aquaculture. Within the host fish cells, Htp3 is released from vesicles into host cytosol where it degrades nucleic acids. |
A0A067XGX8 | AROG2_PETHY | Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 2) (DAHP synthase 2) (PhDAHP2) (Phospho-2-keto-3-deoxyheptonate aldolase 2) | MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMIWVGERTRQLDGAHVEFLRGIANPLGIKVSHKMDPDELVKLIDILNPQNKPGRITVITRMGADNMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTTKAPCGLKTRSFDSIRAELRAFFDVHEQEGSYPGGVHLEMTGQNVTECVGGSRTITYNDLSSRYHTHCDPRLNASQALELAFAIAERLRRRRLGPKFSL | Involved in the production of volatile organic compounds (VOCs). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). |
A0A067XH53 | AROG1_PETHY | Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 1) (DAHP synthase 1) (PhDAHP1) (Phospho-2-keto-3-deoxyheptonate aldolase 1) | MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQSLTRLDSTSGLYYDCSAHFLWVGERTRQLDGAHVEFLRGIANPLGIKVSDKMDPSALVKLIEILNPQNKAGRITIITRMGAENMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTIKAPCGLKTRPFDSIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNVTECIGGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRLGSQSVLGQ | Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). |
A0A067XR63 | XTH7_DIOKA | Xyloglucan endotransglucosylase protein 7 (XET protein 7) (EC 2.4.1.207) (DkXTH7) (Xyloglucan endotransglucosylase/hydrolase protein 7) (XTH protein 7) | MNAEGGNLHREFEITWGDGRARIHNNGGLLTLSLDRASGSGFRSKNEYLFGRIEIQIKLVAGNSAGTVATYYLSSEGPTHDEIDFEFLGNSSGEPYTLHTNVFSQGKGNREQQFFLWFDPTMDFHTYTILWNPQRIIFYVDETPIREFKNLERHGIPFPRSQAMRVYSSMWNADDWATRGGLVKTDWTKAPFTASYRSYKADACVWSGEASSCGSQDSNPSDKWWMTEELNATRMKRLRWVQKKYMVYNYCVDKMRFPEGLAPECNIS | Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits. |
A0A067XRK9 | XTH6_DIOKA | Xyloglucan endotransglucosylase protein 6 (XET protein 6) (EC 2.4.1.207) (DkXTH6) (Xyloglucan endotransglucosylase/hydrolase protein 6) (XTH protein 6) | MASSLTLPMAMAFTLLALSFASAMGGSMNSSRFDELFQPSWAFDHFVYEGEVLKMKLDNYSGAGFSSKGKYLFGKVTVQIKLVEGDSAGTVTAFYMSSDGTNHNEFDFEFLGNTTGEPYLVQTNVYVNGVGNREQRLNLWFDPTKDFHSYSLLWNQRQVVFMVDETPIRVHSNLEHRGIPFPKDQPMGVYSSIWNADDWATQGGRIKTDWSHAPFVASYQGFAIDACECPAAVAATDNARRCSSSAEKQFWWDMPTLSELSLHQSHQLIWVRANHLVYDYCTDTARFPVTPAECEHHRH | Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall restructuring during postharvest fruit softening. |
A0A067YMX8 | XTH8_DIOKA | Xyloglucan endotransglucosylase protein 8 (XET protein 8) (EC 2.4.1.207) (DkXTH8) (Xyloglucan endotransglucosylase/hydrolase protein 8) (XTH protein 8) | MAASPYSIFAVQLLLLASWMLSSSSSNFNQDFNIAWGGGRARILNNGELVTLSLDKASGSGFRSKNLYLFGKIDMQLKLVPGNSAGTVTTYYLSSEGSVRDEIDFEFLGNLTGEPYTLHTNVYSHGKGEREQQFRLWFDPAADFHTYSILWNSKTIVFYVDQTPVREFKNMESIGVPYLRQPMRLFSSIWNADEWATRGGLIKTDWTQAPFTTSYRNFRADNACVWAAKASSCGLAAGGNAWLSVELDAKSRGRLRWVRRNQMIYDYCVDGKRFPRGVPPECKLNLHI | Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants causes accelerated dark-induced leaf senescence and higher lipid peroxidation of the leaf cells. Overexpression in transgenic tomato plants promotes fruit ripening and softening. Probably involved in cell wall restructuring during postharvest fruit softening. |
A0A068B6Q6 | CA18_CONBE | Conotoxin Bt1.8 | PDGRNAAAKAFDLITPTVRKGCCSNPACILNNPNQCG | Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin inhibits mammalian alpha-3-beta-2/CHRNA3-CHRNB2 nAChR (IC(50)=9.4 nM (rat), IC(50)=8.8 nM (human)), as well as the subunit chimera alpha-6/alpha-3-beta-2-beta-3 nAChR (CHRNA6/CHRNA3-CHRNB2-CHRNB3)(IC(50)=2.1 nM (rat), IC(50)=1.7 nM (human)). Binds to rat alpha-6/alpha-3-beta-2-beta-3 more rapidly than to alpha-3-beta-2, and dissociates more rapidly from alpha-3-beta-2 than from alpha-6/alpha-3-beta-2-beta-3. |
A0A068J840 | UGT1_PANGI | UDP-glycosyltransferase 1 (UGTPg1) (EC 2.4.1.363) | MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKYSNLKEILPVGFLDRTSCVGKVIGWAPQVAVLGHESVGGFLSHCGWNSTLESVWCGVPVATWPMYGEQQLNAFEMVKELGIAVEIEVDYKKDYFNMKNDFIVRAEEIETKIKKLMMDENNSEIRKKVKEMKEKSRAAMSENGSSYNSLAKLFEEIM | Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway. Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1 from protopanaxatriol (PPT). Triggers C20-OH glycosylation of ginsenoside Rg3 to produce ginsenoside Rd. Mediates the conversion of protopanaxadiol (PPD) to the ginsenoside compound K. catalyzes the production of 20S-O-beta-(D-glucosyl)-dammarenediol II form dammarenediol II (DM). |
A0A068Q5Q5 | DEPOL_BPKNT | Depolymerase, capsule K1-specific (EC 4.-.-.-) (Gene product 34) (gp34) (K1-ORF34 protein) (Probable tail spike protein) | MALIRLVAPERVFSDLASMVAYPNFQVQDKITLLGSAGGDFTFTTTASVVDNGTVFAVPGGYLLRKFVGPAYSSWFSNWTGIVTFMSAPNRHLVVDTVLQATSVLNIKSNSTLEFTDTGRILPDAAVARQVLNITGSAPSVFVPLAADAAAGSKVITVAAGALSAVKGTYLYLRSNKLCDGGPNTYGVKISQIRKVVGVSTSGGVTSIRLDKALHYNYYLSDAAEVGIPTMVENVTLVSPYINEFGYDDLNRFFTSGISANFAADLHIQDGVIIGNKRPGASDIEGRSAIKFNNCVDSTVKGTCFYNIGWYGVEVLGCSEDTEVHDIHAMDVRHAISLNWQSTADGDKWGEPIEFLGVNCEAYSTTQAGFDTHDIGKRVKFVRCVSYDSADDGFQARTNGVEYLNCRAYRAAMDGFASNTGVAFPIYRECLAYDNVRSGFNCSYGGGYVYDCEAHGSQNGVRINGGRVKGGRYTRNSSSHIFVTKDVAETAQTSLEIDGVSMRYDGTGRAVYFHGTVGIDPTLVSMSNNDMTGHGLFWALLSGYTVQPTPPRMSRNLLDDTGIRGVATLVAGEATVNARVRGNFGSVANSFKWVSEVKLTRLTFPSSAGALTVTSVAQNQDVPTPNPDLNSFVIRSSNAADVSQVAWEVYL | Functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a lyase activity that specifically degrades the K1-type polysaccharides of Klebsiella pneumoniae capsule. |
A0A072TH68 | KI104_MEDTR | Kunitz type trypsin inhibitor 104 | MSTRSLTIFILAHVWLLMATTSIAQFVIDTSGEPVEDDEEYFIRPAITGNGGGSTLVTGNGPCPLHVGLDNTEGTLGVAVKFTPFAPQHDDDDVRLNRDLRVTFLTSTSCGQSTDWRLGEKDATSGRRLIVTGRDNGAGSQGNFFRIVQTQTGGTYNIQWCPTEACPSCKVQCGTVGVIRENGKNLLALDGDALPVVFQKE | Protease inhibitor involved in the control of mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). |
A0A072UR65 | CHT5B_MEDTR | Class V chitinase CHIT5b (MtCHIT5b) (EC 3.2.1.14) | MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTASVYSYSGSTWIGYDNPFTVSIKVGFAQALKLRGYFFWVAGLDTLDWKIATQASKAWKLV | 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 reduce hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay. |
A0A072VDF2 | CCR1_MEDTR | Cinnamoyl-CoA reductase 1 (Mt-CCR1) (EC 1.2.1.44) (Caffeoyl-CoA reductase) (EC 1.2.1.-) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase) | MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETVKSLQDQGHLSIPNKEDSLAVKS | Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Mediates the conversion of feruloyl-CoA to coniferylaldehyde. Also active, with a lower efficiency, toward coumaroyl-CoA, caffeoyl CoA and sinapoyl-CoA. Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). |
A0A075BSX9 | HLNO_SHIS7 | (S)-6-hydroxynicotine oxidase ((S)-6HN oxidase) (EC 1.5.3.5) (6-hydroxy-L-nicotine oxidase) (6-HLNO) (L-hydroxynicotine oxidase) (LHNO) | MTEKIYDAIVVGAGFSGLVAARELSAQGRSVLIIEARHRLGGRTHVVNFLGRPVEIGGAGVHWCQPHVFAEMQRYGFGFKEAPLADLDKAYMVFADGQKIDVPPATFDEEYTTAFEKFCSRSRELFPRPYSPLDNHEVSNLDGVSARDHLESLGLNELQLASMNAELTLYGGAPTTELSYPSFVKFHALASWDTITFTDSEKRYHVQGGTNALCQAIFDDCRADSEFGVPVEAVAQTDNGVTVTLADKRVFRALTCVLTLPTKVYADVRFEPPLPPEKRAFIEHAEMADGAELYVHVRQNLGNTFTFCDDPNPFNAVQTYAYDDELGTILKITIGRQSLINLENFDAIAAEIRKIHGDVEVLEALPYNWAMDEYARTSYPAMRKGWFSRYKDMAKPENRLFFAGSATADGWHEYIDGAIESGIRVGREIRHFMKATA | Involved in the degradation of L-nicotine. Catalyzes the oxidation of (S)-6-hydroxynicotine (6-hydroxy-L-nicotine) to 6-hydroxypseudooxynicotine. Oxidation of the pyrrolidine ring of (S)-6-hydroxynicotine leads to the formation of the optically inactive 6-hydroxy-N-methylmyosmine, which hydrolyzes spontaneously to 6-hydroxypseudooxynicotine. Acts with absolute stereospecificity on the L-form of 6-hydroxynicotine. Also involved in the degradation of nornicotine, and catalyzes the oxidation of 6-hydroxynornicotine to 6-hydroxymyosmine, which hydrolyzes to 6-hydroxypseudooxynornicotine. In vitro, converts (S)-nicotine into N-methylmyosmine, which spontaneously hydrolyzes spontaneously into pseudooxynicotine, but catalytic efficiency is about 1900-fold higher with (S)-6-hydroxynicotine. |
A0A075D5I4 | PINMT_RAUSE | Picrinine-N-methytransferase (RsPiNMT) (EC 2.1.1.-) (Gamma-tocopherol-like methyltransferase PiNMT) (RsTLMT) | MAEKQQAVAEFYDNSTGAWEVFFGDHLHDGFYDPGTTATIAGSRAAVVRMIDEALRFANISDDPAKKPKTMLDVGCGIGGTCLHVAKKYGIQCKGITISSEQVKCAQGFAEEQGLEKKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPIVIVSYAHRNLSPSEGSLKPEEKKVLKKICDNIVLSWVCSSADYVRWLTPLPVEDIKAADWTQNITPFYPLLMKEAFTWKGFTSLLMKGGWSAIKVVLAVRMMAKAADDGVLKFVAVTCRKSK | S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline. Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine). Accepts also, with low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates. |
A0A075D657 | PINMT_VINMI | Picrinine-N-methytransferase (VmPiNMT) (EC 2.1.1.-) (Gamma-tocopherol-like methyltransferase PiNMT) (VmTLMT) | MYTCSIIIYILTFWQLSKIKKQVAAAEKQVMTVTEKQEAVAEFYDKSTDAWEVFFGEHLHDGFYEPGTTATIPGSKVAVVRMIDELLRFAGISDDPEKKPKTMLDVGCGLGGTCLHVAKKYDIKCTGITISPEQVKCAQDLAATQGLESKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPVVIAGYAARNLSPSEESLKPEEKMVLEKICDHIVLSWLCSTGDYVKWLTPLPVQDIKVWDLTQNITPFYPLCIKEAFTWKSFTSLLKMGGWSAIKVVFAVKMMAMAAEEGLLKFAAVTCRKSK | S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline. Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine). Accepts also, with low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates. |
A0A075F7E9 | LERK1_ORYSI | G-type lectin S-receptor-like serine/threonine-protein kinase LECRK1 (OsLecRK1) (EC 2.7.11.1) (OsRLCK134) | MVALLLFPMLLQLLSPTCAQTQKNITLGSTLAPQGPASSWLSPSGDFAFGFRPVEGNTSFYLIAVWFNKISDKTVVWYAKNTDQDPSIVEVPSDSFLQLTNDGALSLKDRSGQEGWNPQVTGVAYASMRDTGNFVLLGADGTTKWQTFDMPSDTILPTQVIPCNKTRNKSLRARLDIDDYSSGRFLLDVQTDGNLALYLVAVPSGSKYQQYWSTDTTGNGSELVFSETGKVYFALTDGTQINISSDAGIGSMADYFHRATLDPDGVFRQYVYPKKANAGILGGETWTALSMQPQNICHAIVSDVGSGVCGFNSYCTFDGTRNQIASCQCPPWYKFFDEQKKYKGCKQDFQPHSCDLEEATALAQFELRPIYGVDWPLSDYEKYEPIGQDDCGRLCVIECFCAMAVYNQSTSTCWKKKLPLSNGNMADYVQRTVLLKVPSSNSSQFMISTSSNKWKRNRKHWVLGSSLILGTSILVNFALISIFLFGTYCRITTKKNIPLSQASSKSQLPLKTFTYKELEKATAGFHEILGAGASGVVYKGQLEDELKTNIAVKTIHKLQPETEKEFMVEVETIGQTFHKNLVRLLGFCNERAERLLVYEFMTNGPLNRLLFDNSRPHWNTRVHIALGVARGFLYLHDECSKQIIHCDIKPQNILLDDNLVAKISDFGLAKLLLTNQTRTKTGIRGTRGYVAPEWFKNIGISTKVDVYSFGVILLELVCCRRNVELEVVDEEQTIVTYWANDCYRSGRIDLLVEGDDEAIYDIKKVERFVTVALWCLQEDPSMRPNMLKVTQMLDGAVAIPSPPDPCSFISSLP | Involved in innate immunity. Required for the expression of defense-related genes PR1A, LOX2 and CHS1 upon biotic stresses. Required for basal resistance to the fungal blast (M.grisea), bacterial blight (O.oryzae pv. oryzae, Xoo) and the herbivorous insect brown planthopper (N.lugens, BPH). May be involved in several defense signaling pathways. Involved in the promotion of seed germination. Required for the expression of alpha-amylase genes during seed germination. Involved in resistance against the brown planthopper (BPH). Member of the BPH3 (BPH resistance locus 3) cluster which contains LECRK1, LECRK2 and LECRK3. |
A0A075F932 | SYT1_ANSCY | Synaptotagmin-1 (Synaptotagmin I) (SytI) | MVSESHHEALAAPPATTVAAAPPSNVTEPASPGGGGGKEDAFSKLKEKFMNELNKIPLPPWALIAIAIVAVLLILTCCFCLCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQDDDAETGLTDGEEKEEPKEVEKLGKIQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEYKVAMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQIVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQPEEEVDAMLAVKK | Calcium sensor that participates in triggering neurotransmitter release at the synapse (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. May play a role in dendrite formation by melanocytes (By similarity). May play a role in regulating the secretion of hormones relevant to the reproduction and egg-laying of female geese. |
A0A075FBG7 | ELS_MARVU | 9,13-epoxylabda-14-ene synthase, chloroplastic (EC 4.2.3.189) (Manoyl oxide synthase) (EC 4.2.3.190) (Miltiradiene synthase) (EC 4.2.3.131) | MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTRIDDFFDHGGSREESYKILDLVQEWKEKPAEEYGSKEVEILFTAVYNTVNDLAEKAHIEQGRCVKPLLIKLWVEILTSFKKELDSWTEETALTLDEYLSSSWVSIGCRICILNSLQYLGIKLSEEMLSSQECTDLCRHVSSVDRLLNDVQTFKKERLENTINSVGLQLAAHKGERAMTEEDAMSKIKEMADYHRRKLMQIVYKEGTVFPRECKDVFLRVCRIGYYLYSSGDEFTSPQQMKEDMKSLVYQPVKIHPLEAINV | Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-ene, from (+)-copalyl diphosphate ((+)-CPP) to miltiradiene and from 8-hydroxycopalyl diphosphate (LPP, labda-13-en-8-ol diphosphate) to manoyl oxide. |
A0A075QQ08 | IF4E1_TOBAC | Eukaryotic translation initiation factor 4E-1 (NteIF4E1) (eIF4E-1) (Eukaryotic translation initiation factor 4E2-T) (eIF4E2-T) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) | MVDEVEKPASLEESKTNTREVEEGAEEVIESDDTMSSLGNPCKAMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTVEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCASGGKWTMSFSRGKSDTCWLYTLLAMIGEQFDCGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDSIGFIFHDDAKKLDRAAKNRYSV | 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. 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. Key component of recessive resistance to potyviruses (Ref.2). |
A0A075TJ05 | OTASE_ASPNG | Ochratoxinase (OTase) (EC 3.4.17.-) (Amidohydrolase 2) (Amidase 2) (Carboxypeptidase Am2) | MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL | Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine. Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products. |
A0A075TMP0 | PATD_PENEN | Alcohol dehydrogenase patD (EC 1.1.1.-) (Patulin biosynthesis cluster protein D) | MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKCNEAFAAMMEGSVRFRAVITM | Alcohol dehydrogenase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatD catalyzes the conversion of neopatulin into E-ascladiol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A075TMP8 | PATI_PENEN | Cytochrome P450 monooxygenase patI (EC 1.-.-.-) (Patulin biosynthesis cluster protein I) (m-hydroxybenzyl alcohol hydroxylase) | MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMTKYPEVQAKAHAQIDSIIGHNRSPAWSDWSKLPYINMIIKESHRWRPVSPLGVPHAVAEDDHIDGKLIPQGSSIVLNVWGMHHDSDRWQEPEHFQPERFADFPALASGYAGSERRDHLGYGAGRRICPGIHLAERNLIIGIAKLLWAFEFLEPLGSDSDISAHSGASKGFLHCPKDYGCVIRLRSPEKRETIMREFAEAQEVFARFD | Cytochrome P450 monooxygenase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatI catalyzes the conversion of m-hydroxybenzyl alcohol into gentisyl alcohol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A075TR33 | PATO_PENEN | FAD-linked oxidoreductase patO (EC 1.-.-.-) (Patulin biosynthesis cluster protein O) | MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGHYHRHLPTYTSAGGMAIAQITNSSFLLTPLTLPAYTAAATKKLLGPFLQDLHQLNISYTLNVTESASYFQHYMKLIEPNPTQLVQNAQYGGRLLPLDLIERNNSQLTDAVQKLTADGVTFVGIGLNVSSSVTGDIWNSVLPGWRTAAMTVILTTSWPLGANLTKMKILADKMTTKWVPILTALSPESGCYMSEADPQQPDWKQTFYGRNYDSLYAIKTKYDPLQTFYATTAVGSEDWQVEAGGRLCQATRKN | FAD-linked oxidoreductase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatO acts with patJ in the vacuole to convert gentisyl alcohol to isoepoxydon. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A075TR41 | PATJ_PENEN | Probable oxidoreductase patJ (EC 1.-.-.-) (Patulin biosynthesis cluster protein J) | MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVVIDDAGK | Probable oxidoreductase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatJ acts with patO in the vacuole to convert gentisyl alcohol to isoepoxydon. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A075TRC0 | PATK_PENEN | 6-methylsalicylic acid synthase (6MSAS) (EC 2.3.1.165) (Non-reducing polyketide synthase patK) (Patulin biosynthesis cluster protein K) | MHSVSPSTYPSGGTSPAPADTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAVGEIPEMRWEPYYRRDPRNAKELKKTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIRLGESQVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVAQDGKTNGIMAPNAKAQQLAARTALNVAGVDPSTVRYVEAHATSTPLGDPTEISAIAGVYGTNRPADDPCYIGSIKPNIGHLEAGAGVMGFIKAILTIQKGVLPPQANLTNLNSRIDWKTAGVKVVQEATPWPSSDPIRRAGVCSYGYGGTVSHAVIEEFNPILRPDPLDDGAATGPGLLLLSGPQEKRLALQAKTLREWMTADGKDNNLSEILTTLATRRDHHDYRAALVVDDHLDATQVLQALANGTDHSFTTQSRVLGADVSKDVVWVFSGHGAQWPDMGKQLIHNPVFFAAIQPLDELIQAEIGLSPIELLRTGDFESSDRVQILTYLMQIGLSAILQSNGITPQAVIGHSVGEIAASVVAGALTSAEGALIVTRRALLYRQVMGKGGMILVNLPSAETEEILGRRQDLVVAIDSSPSSCVVAGDKDIVAETAEAFKARGVKTFTVKSDIAFHSPTLNVLMDPLRDALGQALAPTVHIKLYSTALVDPRGQDVRDLEYWTGNMVNRVRLTSAIQAAVEDGYRLFLEVSTHPVVSHSINETLMDAGLEDFAVIPTLLRKKPTEKHILHSIAQLHCRGAEVNWAAQMPGRWATGLPTTTWMHKPIWRKIETAPLHTGLTHDVEKHTLLGQRIPVPGTDTFVYTSRLDNETKPFPGSHPLHGTEIVPAAGLINTFLKGTGGQMLQNVVLRVPVAINAPRSVQVVVQQDQVKVVSRLISSDPSLSDDDASWVTHTTAYWDRKVLGSADRIDLAAVKARLTTKLADNFSIDYLDKVGVSAMGFPWAVTEHYRDTKQMLARVDVNPAVLGDDPLPWDSSSWAPVLDAATSVGSTVFQTAALRMPAQIERVEIFTSEDPPKISYLFVEEASDSVPTSHVSVLSETGEVLAKFTAMRFSEIEGTPGVSGSMESLVHQIAWPPATPAEEPLLITKVILVSPDATARAQYAATLPTQVQSFQFSTTEDFFSNASSLPLEKGTVVAYIPGEVASLAEVPAASESFTWNLLELIKFIVNGSLPIKVFTLTSSVGDGQTPTALAQSPLIGLARIIASEHPDLGSLIDIEEPKIPLSTMRYIQGADVIRISDGIARVSRFRSLPRTKLRPASEGPRLLPRPDGTYLITGGLGILGLEVADFLVEKGARRLLLISRRALPPRRTWDQVSEDLQPTIAKIRLLESRGASVHVLPLDITKPDAVEQLSTALDRLSLPAVQGVVHAAGVLDNEMVLQTTRDAFNRVLAPKIAGALALHEVFPPKSVDFFVMFSSCGNLVGFTGQASYGSGNAFLDTLATHRARLGDSGAVAFQWTAWRGLGMGSSTDFINAELEAKGITDVTRDEAFAAWQHLAKYDIDHGVVLRSLAIDDGEPVPVPILNDIVVRRVSELSGSAQAAAGSSGNDAVPSSGPELKAYLDEKIRGCVAKVLQMTAEDVDSKAALADLGVDSVMTVTLRRQLQQTLKIPVPPTLTWSHPTVSHLVVWFAEKIGK | 6-methylsalicylic acid synthase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatK catalyzes the first step of the pathway which is the synthesis of 6-methylsalicylic acid via condensation of 1 acetate and 3 malonate units. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A075TRK9 | PATE_PENEN | Patulin synthase (EC 1.1.-.-) (Dehydrogenase patE) (Patulin biosynthesis cluster protein E) | MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARKEIVLSAGAFQSPQLLMVSGVGPAATLKAHNIPLVADRPGVGQNMQDHIIYAPSYRVNVITQSALLNEEFEAQANRDYNERAAGIYANPTSDILAWEKIPEPKRSAWFSNHTRQVLAEYPDDWPEVEFLTMGGYFGYQRNYIRDNPSDGYNYASLAVSLCTPRSRGNVTITSPDAGVPPVINPNWLTDPVDVELAVAAFKRTRDFFNTTAIKPILIGPEYFPGSQVATDAEILDHVRKSFDTIFHASCTCAMGLANDTQAVVDSKARVIGVEALRVVDASALPFLPPGHPQSTLYALAEKIACEISGNC | Patulin synthase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatE catalyzes the last step of the pathway which is the conversion of E-ascladiol to patulin. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A075TRL5 | PATH_PENEN | Cytochrome P450 monooxygenase patH (EC 1.-.-.-) (Patulin biosynthesis cluster protein H) (m-cresol hydrolase) | MEPFLLLLLVLLPAIVLVRYAFTYGHRTSTMPIGPPTLPFIGNIHQITKKYTHIKFTEWAAQYGGLYMLKIGNGNMAVITDRRLVKEVLDRKSGIYSHRPHSFVSHDLITKGNHLLVMHYGDQWRTFRRLVHQHLMETMVENHHTKIVNAEAIQLVRDYMIDPEHHMAHPKRYSNSITNSIVFGIRTANREGANMRRLYKLMEEWSEVMETGATPPVDLFPWLKLLPQWLFNNYIDRAKAIGVQMETLYVDILNKVIKRREDGHNNGTFMDKVLDSQEKHNLPWHQLAFIGGVLMEGGSDTSSSLTLAIVQALIQNPDVQRKAHAEIDAVVGHNRSPVWEDFEKLPYINMIIKEGHRWRPILPLCFPHALGEDDWVDGKFLPKGTIVVVNTWGMHMDPSQPDDPAAFIPERFAKHPQLAPDYVPGTWERRDHYGYGVGRRICPGIHLAERNMFLGIAKLLWAFDFQPGEGPIDSDPVTGYHNGFLYCAKDYSCRPVIRNEVIRDTIEREYATATADVFSRFTEG | Cytochrome P450 monooxygenase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatH catalyzes the conversion of m-cresol into m-hydroxybenzyl alcohol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A075TXZ1 | PATG_PENEN | 6-methylsalicylic acid decarboxylase (EC 4.1.1.52) (Patulin biosynthesis cluster protein G) | MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILDKAKL | 6-methylsalicylic acid decarboxylase part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatG catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable). |
A0A076FFM5 | F8H1_OCIBA | Flavonoid 8-hydroxylase 1, chloroplastic (ObF8H-1) (EC 1.14.15.-) | MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLPVVPEEKTAMIVFYCIPVTPGYSRLIYAGARNFAVQIDRFVPRWITHMSHNLIFDSDLFLLHVEEQKLKDLDWHKSCYIPTKADGQVVAFRRWLNKYGGTQVDWRNNFTPALPPTPSREQLFDRYWSHTAECSSCSVACKRLNALEIGLQAMSLVFVAMAAAVSAPATRYSMVAMAVLSFLASKWLSHFIHKTFYNHGYDHAFV | Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. Catalyzes the 8-hydroxylation of salvigenin (SALV) to produce 8-hydroxysalvigenin (8-OH-SALV). Can also use cirsimaritin (CIRM) as substrate with low efficiency. |
A0A078CGE6 | M3KE1_BRANA | MAP3K epsilon protein kinase 1 (BnM3KE1) (EC 2.7.11.1) | MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDSPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIRYMKGADSSSEKDGEGSQDIAESVSAEKVGMSKTNSKSKLGVGSFRSEKDQSSASDIGEERADSEDDIMSDQGPTLSIHDNKSSLQSSTCSISSDAKGTSQDGKSEPDGNLEMEASEGRRKASATKQVGKESSIQMQQRSHSFGPKGEDRGLRKAVKTPSSYGGNELTRFSDPPGDACLHDLFHPLNKVPEGKLNEASASTPASNANQGDSPVADGGKNDLATKLRARIAQKQMEGETGHSNDGGDLFRLMMGVLKDDVIDIDGLVFDEKASPDNLLPLQAVEFSRLVSSLRPSETEDAIVTSCQKLVAMFRHRPEQKVVFVTQHGFLPVMDLLDSPKSRVTCAVLQLINEIIKDNIDFQENACLVGLIPLVMSFAGPERDRSREIRKEAAYFLQQLCQSSSLTLQMFIACRGIPVLVGFLEADYAKYRSMVHLAIDGMWQVFKLKRSTPRNDFCRIAAKNGILLRLINTLYSLNEATLLASEGRSGQLDQHEALLSVIDHPDVLKTRPGGGEEPSNSQRSDLYQPDGDRPRSSSAALDATEDVKQHHRISISSNRTSTDKIQKLAESASNGYAVTQPEQVRPLLSLLEKEPPSRHVSGQLDYVKHIAGLEKHESILPLLRASIDTMPRYFSKTMSKKVMAIEGAASASGVLSGSGVLNARLGSDTSSGLLSHMVTTLSAEVASQYLEKVADLLLEFARADTTVKSYMCSQSLLSRLFHMFNRVEPPILLKILKCTNHLSTDPNCLESLQRADAIKHLIPNLEVKEGNLVDQIHHEVLSALFNLCKINKRRQEQAAENGIIPHLMLFVMSDSPLKQYALPLLCDMAHASRNSREQLRSHGGLDVYLSLLDDEYWSVIALDSIAVCLAQDNDNRKVEQALLKDDAIYTLVNFFQSCPERHFVHILEPFLKIITKSSRINTTLAVNGLTPLLIARLDHQDAIARLNLLKLIKAVYEHHPRPKQLIVENDLPQRLQNLIEERREGQHLGGQVLVKQMATSLLKALHINTVL | Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells. Required for the normal functioning of the plasma membrane in developing pollen. Involved in the regulation of cell expansion and embryo development (By similarity). |
A0A087WPF7 | AUTS2_MOUSE | Autism susceptibility gene 2 protein homolog | MDGPTRGHGLRKKRRSRSQRDRERRSRAGLGTGAAGGIGAGRTRAPSLASSSGSDKEDNGKPPSSAPSRPRPPRRKRRESTSAEEDIIDGFAMTSFVTFEALEKDVAVKPQERAEKRQTPLTKKKREALTNGLSFHSKKSRLSHSHHYSSDRENDRNLCQHLGKRKKMPKGLRQLKPGQNSCRDSDSESASGESKGFQRSSSRERLSDSSAPSSLGTGYFCDSDSDQEEKASDASSEKLFNTVLVNKDPELGVGALPEHNQDAGPIVPKISGLERSQEKSQDCCKEPVFEPVVLKDPHPQLPQLPSQAQAEPQLQIPSPGPDLVPRTEAPPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRPPRPQSPSHLLQQTLPPVQSHPSSQSLSQPLSAYNSSSLSLNSLSSRSSTPAKTQPAPPHISHHPSASPFPLSLPNHSPLHSFTPTLQPPAHSHHPNMFAPPTALPPPPPLTSGSLQVPGHPAGSTYSEQDILRQELNTRFLASQSADRGASLGPPPYLRTEFHQHQHQHQHTHQHTHQHTFTPFPHAIPPTAIMPTPAPPMFDKYPTKVDPFYRHSLFHSYPPAVSGIPPMIPPTGPFGSLQGAFQPKTSNPIDVAARPGTVPHTLLQKDPRLTDPFRPMLRKPGKWCAMHVHIAWQIYHHQQKVKKQMQSDPHKLDFGLKPEFLSRPPGPSLFGAIHHPHDLARPSTLFSAAGAAHPTGTPFGPPPHHSNFLNPAAHLEPFNRPSTFTGLAAVGGNAFGGLGNPSVTPNSVFGHKDSPSVQNFSNPHEPWNRLHRTPPSFPTPPPWLKPGELERSASAAAHDRDRDVDKRDSSVSKDDKERESVEKRHPSHPSPAPPVPVSALGHNRSSTDPTTRGHLNTEAREKDKPKEKERDHSGSRKDLTTEEHKAKESHLPERDGHSHEGRAAGEEPKQLSRVPSPYVRTPGVDSTRPNSTSSREAEPRKGEPAYENPKKNAEVKVKEERKEDHDLPTEAPQAHRTSEAPPPSSSASASVHPGPLASMPMTVGVTGIHAMNSIGSLDRTRMVTPFMGLSPIPGGERFPYPSFHWDPMRDPLRDPYRDLDMHRRDPLGRDFLLRNDPLHRLSTPRLYEADRSFRDREPHDYSHHHHHHHHPLAVDPRREHERGGHLDERERLHVLREDYEHPRLHPVHPASLDGHLPHPSLLTPGLPSMHYPRISPTAGHQNGLLNKTPPTAALSAPPPLISTLGGRPGSPRRTTPLSAEIRERPPSHTLKDIEAR | Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The PRC1-like complex that contains PCGF5, RNF2, CSNK2B, RYBP and AUTS2 has decreased histone H2A ubiquitination activity, due to the phosphorylation of RNF2 by CSNK2B. As a consequence, the complex mediates transcriptional activation (By similarity). In the cytoplasm, plays a role in axon and dendrite elongation and in neuronal migration during embryonic brain development. Promotes reorganization of the actin cytoskeleton, lamellipodia formation and neurite elongation via its interaction with RAC guanine nucleotide exchange factors, which then leads to the activation of RAC1. |
A0A087X1C5 | CP2D7_HUMAN | Putative cytochrome P450 2D7 (EC 1.14.14.1) | MGLEALVPLAMIVAIFLLLVDLMHRHQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREAMVTRGEDTADRPPAPIYQVLGFGPRSQGVILSRYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFADQAGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLPHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAKKEKAKGSPESSFNDENLRIVVGNLFLAGMVTTSTTLAWGLLLMILHLDVQRGRRVSPGCPIVGTHVCPVRVQQEIDDVIGQVRRPEMGDQAHMPCTTAVIHEVQHFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWKKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELCAVPR | May be responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It may be involved in the metabolism of codeine to morphine. However, another study could not confirm it. |
A0A088MIT0 | BRKP2_PHYNA | Bradykinin-related peptides [Cleaved into: Nattererimorphin; [Val1,Thr6]-bradykinyl-Ser,Pro,Ala; Bradykinin; Des-Arg9-bradykinin; [Hyp3]-bradykinyl-Val,Asp] | MAFLKKSLFLVLFLGVVSLSFCEEEKREEHEEEKRDEEDAESLGKRYGGLSPLRISKRVPPGFTPFRSPARSISGLTPIRLSKRVPPGFTPFRSPARRISEADPGFTPSFVVIKGLSPLRGKRRPPGFSPFRVD | [[Val1,Thr6]-bradykinyl-Ser,Pro,Ala]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). [[Hyp3]-bradykinyl-Val,Asp]: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB). |
A0A088MLT8 | IQIP1_MOUSE | IQCJ-SCHIP1 readthrough transcript protein | MRLEELKRLQNPLEQVDDGKYLLENHQLAMDVENNIENYPLSLQPLESKVKIIQRAWREYLQRQDPLEKRSPSPPSVSSDKLSSSVSMNTFSDSSTPDYREDGMDLGSDAGSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDDRGYRDDGCPAREPGDVSARIGSSGSGSRSAATTMPSPMPNGNLHPHDPQDLRHNGNVVVAGRPNASRVPRRPIQKTQPPGSRRGGRNRASGGLCLQPPDGGTRVPEEPPAPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSARLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK | May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments. May also play a role in axon outgrowth and guidance. |
A0A089QRB9 | MSL3_MYCTU | Mycolipanoate synthase (EC 2.3.1.252) (Mycocerosic acid synthase-like polyketide synthase) (MAS-like PKS) (Mycolipanoic/mycolipenic acids synthase-like polyketide synthase) | MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVGDPVEYASLAAVYGTEGPCALTSVKTNFGHLQSASGPLGLMKTILALRHGVVPQNLHFCRLPDQLAEIDTELFVPQANTSWPDNTGQPRRAAVSSYGMSGTNVHAILEQAPVSEPAASGPELTPEAGGLALFPVSATSAEQLHVTAARLADWVDQNGNAGSRVSMRDLGYTLSCRRAHRPVRTVVTASSFDELSAALRDVAGDQIPYQPAVGHDDRGPVWVFSGQGSQWPGMGTELLVAEPVFAATVAAMEPVIARESGFSVTEAMSAPQTVSGIDRVQPTIFAVQVALAAALKSYGVRPGAIIGHSLGEAAAAVVAGALSLHDGLRVICRRSRLMSRIAGSGAMASVELPGQQVLSELAIRGISDVVLSVVASPTSTVVGGATQSIRDLVAAWEQQDVLAREVAVDVASHTPQVDPILDELLEVLAEVDPTAPEIPYYSATLWDPRERPSFTGEYWVENLRYTVRFAAAVQAALKDGYRVFGELAPHPLLTYAVEQNAASLDMPIATLAAMRRGEQLPFGLRGFVADVHNAGAKVDFSVQYPDGRLVDAPLPSWTHRTLMLSREDSHRSHTGAVQAVHPLLGAHVHLLEEPERHVWQAGVGTGAHPWLGDHRIHNVAAFPGAAYCEMALAAARTTLGELSEVRDIKFEQTLLLDEQTVVSSAATIAAPGILQFAVESHQEGEPARRASAMLHALEEMPQPPGYDTNALTAAHESSMSGEELRKMFNSLGIQYGPAFSGLVAVHTARGDVTTVLAEVALPGAIRSQQSAYASHPALLDACFQSVLVHPEVQKATVGGLMLPVGVRRLRNYHSTRSAHYCLARVTSSSRAGECEADLDVFDQAGTVLLTVEGLRLAAGISEHERANRVFDERLLTIEWERGELPEVPQIDAGSWLLLSASEADPLTAQLADALNAVGAQSTSVASASDVAQLRSLLGGRLTGVVVVTGPPTGGLTQCGRDYVSQLVGIARELAELPGEPPRLFVVTRSAASVLPSDLANLEQAGLRGLMRVIDSEHPHLGATAIDVDNDETVAALVASQLQSGSQEDETAWRNGIWYTARLRPGPLRPAERRTAVVEYRRDGMRLQIRTPGDLESLEFVTFDRVAPGPGEIEVAVTASSVNFADVLVAFGRYPTFEGYRQQLGIDFAGVVTAVGPDVTEHRIGDHVGGMSANGCWSTFVRCDARLAVTLPPELPVAAAAAVPTASATAWYALHDLARICSDDKVLIHSGTGGVGQAAIAIARAAGCEIFATAGSAQRRQLLHDMGVEHVYDSRSTEFAEQIRGDTDGYGVDVVLNSLPGAAQRAGIELLAFGGRFVEIGKRDIYGDTRLGLFPFRRNLSLYAVDLALLTHSHPHTVRRLLKTVYQHTVEGTLPVPQTTHYPIHDAAVAIRLVGGAGHTGKVVLDVPRTGEGVAVVPPEQVRTSRPDGAYLVTGGLGGLGLFLAGELAAAGCGRIVLNSRSTPSPHATRVIERLRAAGADIQVECGDIADAATAHRVVAVATASGLPVRGVLHAAAVVEDATLANVTDELIDRCWAPKVHGAWNIHRATAAQPLEWFCLFSSAAALVGSPGQGAYAAANSWLDAFAHWRRAQGLPATSIAWGAWAEIGRATALAEGTGAAIAPAEGARAFQTLLRYGRAYSGYAPIMGTPWLTAFAQRSRFAEAFHATGQNQPATGKFLAELGSLPREEWPRTVRRLVSDQISLLLRRTIDPDRPLSDYGLDSLGNLELRTRIETETGIRVSPTKITTVRGLAEHVCDELAAAQSAPV | Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids required for the synthesis of a major class of polyacylated trehaloses. Catalyzes the elongation of CoA esters of long-chain fatty acids by incorporation of three methylmalonyl (but not malonyl) residues, to form trimethyl-branched fatty-acids. |
A0A096MJN4 | SEPT4_RAT | Septin-4 (Apoptosis-related protein in the TGF-beta signaling pathway) (Arts) (Bradeion beta) (Brain protein H5) (CE5B3 beta) (Cell division control-related protein 2) (hCDCREL-2) (Peanut-like protein 2) | MIKHFLEDNSDDAELSKFVKDFPGSEPCHPTESKTRVARPQILEPRPQSPDLCDDDVEFRATLWSQPSDSQQYFCPPAPLSPSSRPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWRPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPSEVDRKKCKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQRQMKETH | Filament-forming cytoskeletal GTPase. Pro-apoptotic protein involved in LGR5-positive intestinal stem cell and Paneth cell expansion in the intestines, via its interaction with XIAP (By similarity). May also play a role in the regulation of cell fate in the intestine (By similarity). Positive regulator of apoptosis involved in hematopoietic stem cell homeostasis via its interaction with XIAP (By similarity). Negative regulator of repair and hair follicle regeneration in response to injury, due to inhibition of hair follicle stem cell proliferation, potentially via its interaction with XIAP (By similarity). Plays an important role in male fertility and sperm motility (By similarity). During spermiogenesis, essential for the establishment of the annulus (a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum) which is a requisite for the structural and mechanical integrity of the sperm (By similarity). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (By similarity). Required for dopaminergic metabolism in presynaptic autoreceptors potentially via activity as a presynaptic scaffold protein (By similarity). |
A0A096MJY4 | MEF2C_RAT | Myocyte-specific enhancer factor 2C (Myocyte enhancer factor 2C) | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVTIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNIQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT | Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). |
A0A096MK47 | MLIP_RAT | Muscular LMNA-interacting protein (Cardiac Isl1-interacting protein) (CIP) | MTSCVLAGSIETTPKVSPGDSEAKPLIFTFVPTLRRLPTHIQLADTSKFLVKIPEEPTDKNPETVNRFEYSDHMTFSCESKEERDQRILDYPSEVSGKNSQRKEFNTKEPQGMQKGDLFKAEYVFIVDSDGEDEATCRQGEQGPPGATGNIATRPKSLAISSSLASDVVRPKVRGVDVKVSSHPEIPHGIAPQQKHGQLTSPTTSEQLAHKPPAFSFVSPTNQKTPPVPAKVSGTTVLEEFHIRRLDVHGASEEETATYFHTTAHDSPLPAWKGASTLVFSPSAQLPGSSLCGSNVADHTRGLAPEAQKKVSTSSALNPREDVRTSPSPASGASLRSPSASYIPVRIVMHSLSPSPKPLTSSSHGSLSTVCSQTSSSGNLSKSGLKSPVPSRLSLLTAILKSNPSHQRPLSPASCPTFSLNSLASSTLTLDQKIKQTPSTPKKSLSSCSLTTGSTEQEQASAESHQPCHLSFFSKTTPLSQAQPPSPPALASSSYAATDTEKIPGSTLRSSTTPPQSQTDLFSLADVPSVTPGLSPLSSSKGRKDGDLRAPEKNRNICTRPSTLSFIPPINESTALSSSGKCFHPSPALSDLIDRSKRTCSQRHSDQRPNPSALPTPPVSRAGSASHPHLGYSILPPESSLTQALQRSPSALHPSCGSATCPSRTGMPDSTASNRSSRVSTPSLPVSLTRTKELISPCALSMSAGPENKKPKQYKTKSSYKAFAAIPTNTLLLEQKALDEPARTESNSKASVSDLPVELCFPAQLRQQTEELCATIDKVLQDSLSMHSSDSPSRPSQTMLGSETIKTPTTHPRAAGRETKYANLSSSSSTTSESQLTKPGVIRPVPIKSKLFLKKEEEVYEPNPFSKYLEDSSGLFSEQDMAIPHKPVSLHPLYQSKLYPPAKSLLRPQTLSHADCLTPGPFSHLSSFSLRDEQEKSPTLLSQDTYNKPGHPMVTIPEHDTLDSKE | Required for myoblast differentiation into myotubes, possibly acting as a transcriptional regulator of the myogenic program (By similarity). Required for cardiac adaptation to stress through integrated regulation of the AKT/mTOR pathways and FOXO1. Regulates cardiac homeostasis and plays a role in the protection against cardiac hypertrophy. Binds chromatin (By similarity). May act as a transcriptional cofactor for ISL1, repressing its transcriptional activity (By similarity). May also repress MYOCD transcriptional activity (By similarity). |
A0A096P8D3 | IDH_OSTTA | Isocitrate dehydrogenase (NAD(+)), mitochondrial (OtIDH) (EC 1.1.1.41) | MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDAATMKLVQWRQGGFGMAAHNYDGDVLTDELAQVHKSPGFITSNLVGVHEDGTLIKEFEASHGTVADMDEARLRGEETSLNPLGMVEGLIGAMNHAADVHNIDRDRTHAFTTKMRTVIHQLFREGKGTRDLCGPSGLTTEQFIDAVAERLDA | Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable). |
A0A097PTA8 | DEFCO_COPCI | Fungal defensin copsin | MKLSTSLLAIVAVASTFIGNALSATTVPGCFAECIDKAAVAVNCAAGDIDCLQASSQFATIVSECVATSDCTALSPGSASDADSINKTFNILSGLGFIDEADAFSAADVPEERDLTGLGRVLPVEKRQNCPTRRGLCVTSGLTACRNHCRSCHRGDVGCVRCSNAQCTGFLGTTCTCINPCPRC | Antimicrobial peptide that acts against Gram-positive bacteria (Listeria spp., Enterococcus spp., B.subtilis, B.anthracis, P.aeruginosa). Is not active against Gram-negative bacteria. It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio), probably anchoring lipid II to the membrane, thus inhibiting cell wall synthesis. The interaction with lipid II involves the third position of the pentapeptide. Shows bactericidal activity at about 2-fold minimal inhibitory concentrations (MIC), but does not form pore across the membrane. |
A0A0A0LLY1 | SRBP1_CUCSA | Small RNA binding protein 1 (CsSRBP1) | MASSSVEFRCFVGGLAWATDSNSLEKAFSVYGEIVEAKIVSDRETGRSRGFGFVTFLEEEAMRSAIEAMNGHILDGRNITVNEAQQRGGGGGGGYNRGGGYGGRRDGGGFSRGGGGGYGGGGGGGYGGGRDRGYGGGGGYGGGRDSRGSGGGGSEGGWRN | Possibly has a role in RNA transcription or processing during stress (By similarity). Binds sequence non-specifically to RNAs and DNAs (By similarity). Mediates cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which regulate growth and development, as well as responses to environmental inputs, including pathogen attack can compromise zucchini yellow mosaic virus (ZYMV) and tobacco rattle virus (TRV) infections at the early stage. |
A0A0A1C3I2 | HMGR1_PANGI | 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG-CoA reductase 1) (Hydroxymethylglutaryl-CoA reductase) (PgHMGR1) (EC 1.1.1.34) | MDVRRRLPPKLRRPLPITESSHHHRKTPFPADVDRSPSPTPKASDALPLPLYLTNGIFFTLFFSVAYYLLHRWRDKIRSSTPLHIVTLSELAAIVSLIASFIYLLGFFGIDFVQSFVSRADVDVDIDVEPDILEADRRPCSKLMDQPPPPPVVMSSEEDEEIVKSVVSGKTPSYSLESKLGDCYRAASIRREAVQRTTGRSLLGLPLDGFDYESILGQCCEMPIGYVQIPVGIAGPLLLNGCEYVVPMATTEGCLVASTNRGCKAIYACGGATGILLKDGMTRAPVVRFSTAKRASDLKFFLEDPLNFDTLAVVFNKSSRFARLQSIQCSMAGKNLYIRFCCSTGDAMGMNMVSKGVQNVLEFLQSDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITDDVVKKVLKTTVPALVELNMLKNLAGSAVAGALGGFNAHAANIVSAVFIATGQDPAQNIESSHCITMMEAINNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGANKESHGSNSRLLATIVAGSVLAGELSLMSAIAAGQLVRSHMKYNRSSRDMSKIGS | Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Promotes triterpenes accumulation in roots. |
A0A0A1C930 | HMR2A_PANGI | 3-hydroxy-3-methylglutaryl coenzyme A reductase 2-A (HMG-CoA reductase 2) (Hydroxymethylglutaryl-CoA reductase) (PgHMGR2) (EC 1.1.1.34) | MDVRRRPVKSLSSAKTATAGEPPKSQQQHPKASDALPLPLYLTNGLFFTMFFSVMYFLLHRWREKIRNSTPLHVVTLSELAALVLLMASVIYLLGFFGIGFVRSVIRPSPDAWDILEDDNAINEEDSRREPCAEAIDCSLPPKPKIVHMVPQKALNPKSAFADMMVEQPALAIAPLTEEDEEIVKSVVTGKIPSYSLESKLGDCKKAASIRREALQRITGKSLAGLPLDGFDYKSILGQCCEMPVGYVQIPVGIAGPLLLNETEYSVPMATTEGCLVASTNRGCKAIYASGGATSVLLRDGMTRAPVVRFSTVKRAAELKFFLEEPLNYDTPAHVFNKSSRFGRLQGIKCAVAGKNLYIRFTCSTGDAMGMNMVSKGVQNVLDFLQSDFPDMDVMGISGNYCSDKKPAAVNWIEGCGKSVVCEAIIKEEVVKKVLKTNVAALVELNMLKNLAGSAVAGALGGFNAHASNIVSAVYISTGQDPAQNVESSHCITMMEAVNNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGASKESPGSNSRLLASIVAGSVLAGELSLMSALAAGQLVKSHMKYNRSSKDITKLSS | Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. |
A0A0A1H8I4 | AIS_PSESP | Aconitate isomerase (AI) (EC 5.3.3.7) | MFPRLPTLALGALLLASTPLLAAQPVTTLTVLSSGGIMGTIREVAPAYEKATGVKLDIAAAPSMGDTPQAIPNRLARNEPADVVLMVGSALDKLVASGQVAKDSRVDLGQSFIAMAVRQGAPKPDISNMDAFKQTLEKAQSVAYSDSASGVYLSRILFPRMQLDKSFMAKARMIPAEPVGAVVARGEAQLGFQQLSELKAVPGIDIVGLIPDQAQKMTLYSGAMVSKSQHPEAARALLQYLASKDAAKAIEDSGLKPVPAQP | Involved in assimilation of trans-aconitic acid. Preference for cis-aconitic acid is 14-fold higher than for trans-aconitic acid. Not active on intermediates of tricarboxylic acid (TCA) cycle including citric acid, succinic acid, fumaric acid, and 2-oxoglutaric acid or on other dicarboxilic acids including itaconic acid, formic acid, citraconic acid or maleic acid. |
A0A0A1HA03 | 708C1_FAGES | UDP-glycosyltransferase 708C1 (EC 2.4.1.360) (C-glucosyltransferase a) (FeCGTa) (UDP-glucose:2-hydroxyflavanone C-glucosyltransferase) | MMGDLTTSFPATTLTTNDQPHVVVCSGAGMGHLTPFLNLASALSSAPYNCKVTLLIVIPLITDAESHHISSFFSSHPTIHRLDFHVNLPAPKPNVDPFFLRYKSISDSAHRLPVHLSALSPPISAVFSDFLFTQGLNTTLPHLPNYTFTTTSARFFTLMSYVPHLAKSSSSSPVEIPGLEPFPTDNIPPPFFNPEHIFTSFTISNAKYFSLSKGILVNTFDSFEPETLSALNSGDTLSDLPPVIPIGPLNELEHNKQEELLPWLDQQPEKSVLYVSFGNRTAMSSDQILELGMGLERSDCRFIWVVKTSKIDKDDKSELRKLFGEELYLKLSEKGKLVKWVNQTEILGHTAVGGFLSHCGWNSVMEAARRGVPILAWPQHGDQRENAWVVEKAGLGVWEREWASGIQAAIVEKVKMIMGNNDLRKSAMKVGEEAKRACDVGGSSATALMNIIGSLKR | UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin, 2-hydroxyeriodictyol and 2-hydroxypinocembrin) and phloretin. No activity with flavanones, flavones or flavonols. Exhibits C-glycosylation activity toward 2',4',6'-trihydroxyacetophenone and phloretin using UDP-glucose as sugar donor. Can use UDP-galactose as sugar donor, but catalytic efficiency is 14-fold lower toward UDP-galactose than toward UDP-glucose. |
A0A0A1I6E7 | NDB4S_ANDCR | Antimicrobial peptide AcrAP1 | MEIKYLLTVFLVLLIVSDHCQAFLFSLIPHAISGLISAFKGRRKRDLDGQIDRFRNFRKRDAELEELLSKLPIY | Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). |
A0A0A1I6N9 | NDB4T_ANDCR | Antimicrobial peptide AcrAP2 | MEIKYLLTVFLVLLIVSDHCQAFLFSLIPNAISGLLSAFKGRRKRNLDGQIDRFRNFRKRDAELEELLSKLPIY | Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM). |
A0A0A6ZFY4 | UGT29_PANGI | UDP-glucosyltransferase 29 (UGTPg29) (EC 2.4.1.365) (UDP-glucosyltransferase 94B1) (PgUGT94B1) (UDP-glucosyltransferase 94Q2) (PgUGT94Q2) | MDNQNGRISIALLPFLAHGHISPFFELAKQLAKRNCNVFLCSTPINLSSIKDKDSSASIKLVELHLPSSPDLPPHYHTTNGLPSHLMLPLRNAFETAGPTFSEILKTLNPDLLIYDFNPSWAPEIASSHNIPAVYFLTTAAASSSIGLHAFKNPGEKYPFPDFYDNSNITPEPPSADNMKLLHDFIACFERSCDIILIKSFRELEGKYIDLLSTLSDKTLVPVGPLVQDPMGHNEDPKTEQIINWLDKRAESTVVFVCFGSEYFLSNEELEEVAIGLEISTVNFIWAVRLIEGEKKGILPEGFVQRVGDRGLVVEGWAPQARILGHSSTGGFVSHCGWSSIAESMKFGVPVIAMARHLDQPLNGKLAAEVGVGMEVVRDENGKYKREGIAEVIRKVVVEKSGEVIRRKARELSEKMKEKGEQEIDRALEELVQICKKKKDEQ | Component of the dammarane-type triterpene saponins (e.g. PPD-type ginsenosides or panaxosides) biosynthetic pathway. Glycosyltransferase that catalyzes the conversion of ginsenoside Rh2 to ginsenoside Rg3. Triggers the biosynthesis of ginsenoside Rd from ginsenoside F2. |
A0A0A7EPL0 | PIAL1_ARATH | E4 SUMO-protein ligase PIAL1 (EC 2.3.2.-) (Protein EMBRYO DEFECTIVE 3001) (Protein INHIBITOR OF ACTIVATED STAT-LIKE 1) | MVIPATSRFGFRAEFNTKEFQASCISLANEIDAAIGRNEVPGNIQELALILNNVCRRKCDDYQTRAVVMALMISVKSACQLGWFPERETQELLAIIDLMWNGFSCPENVTSCVNSPVTLISQVIERFYPCVKLGHILVSFEAKPESKMMMKDFHISKKMPHSPKQKVGLFVVRTEDISRSNCIVHPQGVSFLLNGKGIDKRVNISMESGPQLPTNVTALLNLGANLLQAIGCFGGSYLIAIAFMDVIPLPNKPLLKDYVHPEVVGSNSDCDIIEGPSRISLSCPISRTRIKLPVKGHVCKHLQCFDFWNYVNMNTRRPSWRCPHCNQSVCYTDIRVDQKLRKILEEVGRNAADVVISADGTWMVETENDEDVELVPETTHDHGDPNSFINLGPTVKNPARDENEMETSTQVEEHNPCLSEIQGPSNDTHRPASDYTMLNQSHTSTNTLPQLPRTLNAFDGQQFVNLPQVINTRDSPASQALPMTFSPTPSPQDILATNAANFGTSMPAAQSSQFQGSHVTSLGNCEGRTSDLMARWNHIYGRVQTQFPPAPLSHHHYSMQNQSPSPAQQRPVPSYIAHPQTFHVNYGENADQRWMPSSIAHPQTLPVNYGGNTNQRPIPSSIAHPQTLPVNYRGNTDHRSTPYSITHLQTLLNYGGNADQRPMPSSITNLQTLPATYGGYAHQRPMSSSITHPRTSPVNYGGTPDQRPMPSSITHPQTLPVSYGGTTDQILNPGGAMGQFSSREFMNLTPANTENWRPQSRMRGSVAPGTGYDHMIIHPTRPVHPQAQTPPAPLSTSYDGADEIQAFIGHPSYPVSNNETQAGTSSLPVAEGLGYSGSFWSMPPETW | Together with MOM1 and PIAL2, regulates transcriptional gene silencing (TGS) independently of changes in DNA methylation. E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates. Involved in stress responses (e.g. osmotic, salt and abscisic acid ABA) and sulfur metabolism. |
A0A0A7EQR3 | GCE_CERUI | 4-O-methyl-glucuronoyl methylesterase (EC 3.1.1.117) (Glucuronoyl esterase) (GE) | MFKPSFVALALVSYATAQASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHCAWPSSLTPQLNAFINRFLLDQSATTNVFTTNNQFGKVQWNAANWITWTTPTLT | Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. |
A0A0A7GEY4 | GGPPS_GEOAI | Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) | MISEIIKDRAKLVNEKIEELLKEQEPEGLYRAARHYLKAGGKRLRPVITLLSAEALGEDYRKAIHAAIAIETVHNFTLVHDDIMDEDEMRRGVKTVHTLFGIPTAILAGDTLYAEAFEILSMSDAPPENIVRAVSKLARVCVEICEGQFMDMSFEERDSVGESEYLEMVRKKTGVLIGISASIPAVLFGKDESVEKALWNYGIYSGIGFQIHDDLLDISGKGKIGKDWGSDILEGKKTLIVIKAFEEGIELETFGKGRASEEELERDIKKLFDCGAVDYARERAREYIEMAKKNLEVIDESPSRNYLVELADYLIERDH | Catalyzes the addition of 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGPP). Catalyzes the synthesis of geranylgeranyl pyrophosphate as a major product and of farnesyl pyrophosphate in smaller amounts. |
A0A0A7HFE1 | CAS10_STRTR | CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) (ssDNase Cas10) (EC 3.1.-.-) (Cyclic oligoadenylate synthase) (EC 2.7.7.-) (StCas10) | MKKEKIDLFYGALLHDIGKVIQRATGERKKHALVGADWFDEIADNQVISDQIRYHMANYQSDKLGNDHLAYITYIADNIASGVDRRQSNEESDEDASAKIWDTYTNQADIFNVFGAQTDKRYFKPTVLNLKSKPNFASATYEPFSKGDYAAIATRIKNELAEFEFNQAQIDSLLNLFEAILSFVPSSTNSKEIADISLAEHSRLTAAFALAIYDYLEDKGRHNYKEDLFTKASAFYEEEAFLLASFDLSGIQDFIYNIATSGAAKQLKARSLYLDFMSEYIADSLLDKLGLNRANLLYVGGGHAYFVLANTEKTVETLVQFEKDFNQFLLANFQTRLYVAFGWGSFAAKDIMSELNSPESYRQIYQKASRMISEKKISRYDYRTLMLLNRGGKSSERECEICHSVENLVSYHDQKVCDICRGLYQFSKEIAHDHFIITENEGLPIGPNACLKGVAFEKLSQESFSRVYVKNDYKAGTIKATHVFVGDYQCDEIHKYAALSKNEDGLGIKRLAVVRLDVDDLGAAFMAGFSRQGNGQYSTLSRSATFSRSMSLFFKVYINQFASDKKLSIIYAGGDDVFAIGSWQDIIAFTVELRQNFIKWTNGKLTLSAGIGLFADKTPISLMAHQTGELEEAAKGNEKDSISLFSSDYTFKFDRFITNVYDDKLEQIRYFFNHQDERGKNFIYKLIELLRNYESEEKMNVARLAYYLTRLEELTDKDERDKFKQFKKLFFKWYTNNESDRKEAELALLLYVYEIRKD | CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. This subunit has a weak ssDNase activity that is dramatically activated by the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA). Target RNA and ssDNA are cleaved simultaneously, although RNase activity (of Csm3) is much faster. RNA cleavage by Csm3 is not required for ssDNase activity as Csm complex with inactive Csm3 still has ssDNase activity however as the cleaved target RNA products dissociate away ssDNase activity decreases. Self-recognition, with subsequent repression of the ssDNase activity, occurs when the 5' handle of the crRNA bases pairs with the 3' flanking sequence of the target RNA (which would occur if the CRISPR locus were transcribed as an anti-pre-crRNA). This protein has low activity on dsDNA which is not stimulated by the Csm complex. When associated with the ternary Csm effector complex (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic oligoadenylates (cOA) from ATP, producing cyclic triadenylate (cA3) up to cyclic hexaadenylate (cA6), which is the active cOA. The enzyme is also able to cyclize pppA3 up to pppA6. cOAs are second messengers that induce an antiviral state important for defense against invading nucleic acids. Synthesis of cOA can occur with AMP plus ATP, 2'dATP or 3'dATP (but no other nucleotides), and requires a free 3'-OH ribose moiety. |
A0A0A7HIF0 | CSM3_STRTR | CRISPR system Cms endoribonuclease Csm3 (Csm3 RNase) (EC 3.1.-.-) (CRISPR type III A-associated RAMP protein Csm3) | MTFAKIKFSAQIRLETGLHIGGSDAFAAIGAIDSPVIKDPITNIPIIPGSSLKGKMRTLLAKVYNEKVAEKPSDDSDILSRLFGNSKDKRFKMGRLIFRDAFLSNADELDSLGVRSYTEVKFENTIDRITAEANPRQIERAIRNSTFDFELIYEITDENENQVEEDFKVIRDGLKLLELDYLGGSGSRGYGKVAFEKLKATTVFGNYDVKTLNELLTAEV | CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. This subunit has the target ssRNA endonuclease activity it cleaves multiple sites in the target RNA at 6 nucleotide intervals. The number of cleavage sites in the target RNA correlates with the number of Csm3 subunits in the Csm effector complex. In the Csm complex target RNA and ssDNA are cleaved simultaneously, although RNase activity (of Csm3) is much faster. RNA cleavage by Csm3 is not required for ssDNase activity as Csm complex with inactive Csm3 still has ssDNase activity however as the cleaved target RNA products dissociate away ssDNase activity decreases. |
A0A0A7HIX6 | CSM6A_STRTR | CRISPR system endoribonuclease Csm6 (EC 3.1.-.-) (CRISPR type III-A associated protein Csm6-1) | MKILISAVGTTDPISNNHDAALLHIARNYRPDKIVLVYSQEMMVKQDLINKVLLSIEGYNPIIEIDSTILNNDEVFLFDKMYEVMGQIVQKYTNDDNEIILNLSSGTPQIISALFALNRINDYNTQAIQVATPKNRANREYTALTESEIDALIMENQDNRLDFVDRSIKDKSEKFTQALVKRHLRSLIASFDYQAAEAIINRKEYNKLLSKKKIAYIREKLYDFSRVFKNQSILSDILSFPLDDSQKKALNYYLMIDVLKEREHIADVLIKAKSLAEFVIEETIKKDHEGLIVFDGNLPKLNPSFPDCEAILDDIDKKMKKSRGIEDTEERIFSVQSTLNLLSYLNILEFYEYDSQLQTAINGILSLNGERNKVAHGLSEIDTRLLSRKKLKQLSENLRLLLVDCLGIDSSYFNYYDKQNKELIKMLE | CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host this Csm effector complex restricts ssRNA phage MS2, suggesting it may target RNA viruses in vivo. This protein is not part of the Csm complex. Csm functions as a non-specific ssDNase. Base-pairing between crRNA and target RNA to form a ternary Csm complex activates a ssDNase activity target RNA cleavage suppresses the ssDNase, a temporal control that prevents uncontrolled DNA degradation. Viral RNA transcripts probably tether the Csm complex to the viral genome, recruiting Cas10 ssDNA activity which is able to degrade DNA in the transcription bubble, spatially controlling the DNase activity. A single-strand-specific endoribonuclease (ssRNase) that is approximately 1000-fold stimulated by cyclic oligoadenylate (cOA) although several species of cOA are synthesized by this organism only cyclic hexaadenylate (cA6) stimulates the ssRNase activity. Cleaves preferentially within GA or AA dinucleotides, although the presence of cA6 broadens the preference. Linear oligoadenylates do not activate the RNase. |
A0A0B0QJR1 | HEPT_APHF2 | tRNA nuclease HepT (EC 3.1.27.-) (Toxin HEPN) (tRNA nuclease HEPN) | MTNIEPVIIETRLELIGRYLDHLKKFENISLDDYLSSFEQQLITERLLQLITQAAIDINDHILSKLKSGKSYTNFEAFIELGKYQILTPELAKQIAPSSGLRNRLVHEYDDIDPNQVFMAISFALQQYPLYVRQINSYLITLEEEND | Toxic component of a type VII toxin-antitoxin (TA) system. Upon cloning in E.coli inhibits cell growth for several hours eventually cells recover and start growing. Cleaves the last 4 nucleotides from the tRNA acceptor stem (shown in vitro with E.coli tRNA-Glu(UUC)) only cleaves intact tRNA. Has no activity on mRNA. Neutralized by coexpression with cognate antitoxin MntA, which is due to di-AMPylation of the RNase. |
A0A0B4J1F4 | ARRD4_MOUSE | Arrestin domain-containing protein 4 | MGGEAGADGPRGRVKSLGLVFEDESKGCYSSGETVAGHVLLEAAEPVALRGLRLEAQGRATSAWGPSAGARVCIGGGSPAASSEVEYLNLRLSLLEAPAGEGVTLLQPGKHEFPFRFQLPSEPLATSFTGKYGSIQYCVRAVLERPQVPDQSVRRELQVVSHVDVNTPPLLTPMLKTQEKMVGCWLFTSGPVSLSVKIERKGYCNGEAIPIYAEIENCSSRLVVPKAAIFQTQTYLASGKTKTVRHMVANVRGNHIGSGSTDTWNGKMLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKRLMLELPLVIGTIPYSGFGRRNSSVASQFSMDMCWLALALPEQPEAPPNYADVVSEEEFSRHVPPYPQPSDCDGEACYSMFACIQEFRFQPPPLYSEVDPHPGDAQETQPVSFIL | Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates. Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (By similarity). Through an ubiquitination-dependent mechanism also plays a role in the incorporation of SLC11A2 into extracellular vesicles. May play a role in glucose uptake (By similarity). Participates in innate immune response by promoting IFIH1/MDA5 activation through interaction with TRIM65 (By similarity). |
A0A0B4J1G0 | FCG3A_MOUSE | Low affinity immunoglobulin gamma Fc region receptor III-A (IgG Fc receptor III-A) (CD16-2) (FcgammaRIV) (CD antigen CD16a) | MWQLLLPTALVLTAFSGIQAGLQKAVVNLDPKWVRVLEEDSVTLRCQGTFSPEDNSIKWFHNESLIPHQDANYVIQSARVKDSGMYRCQTALSTISDPVQLEVHMGWLLLQTTKWLFQEGDPIHLRCHSWQNRPVRKVTYLQNGKGKKYFHENSELLIPKATHNDSGSYFCRGLIGHNNKSSASFRISLGDPGSPSMFPPWHQITFCLLIGLLFAIDTVLYFSVRRGLQSPVADYEEPKIQWSKEPQDK | Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Binds with intermediate affinity to both IgG2a and IgG2b. Can bind to IgG2a and IgG2b monomers. Does not display binding to IgG1 or IgG3. Recognizes neutralizing virus-specific IgGs displayed on the cell surface of infected cells and triggers antibody-dependent cellular cytotoxicity (ADCC). Confers protection to lethal influenza virus infection. On splenic dendritic cells, uptakes antigen immune complexes and efficiently divert them into MHC class I and II antigen presentation pathways to provide for superior priming of CD4-positive and CD8-positive T cell immune responses. Mediates neutrophil activation by IgG complexes redundantly with FCGR2A. Plays a role in promoting bone resorption by enhancing osteoclast differentiation following binding to IgG2a. Also acts as a receptor for the Fc region of immunoglobulin epsilon (IgE). Binds with low affinity to both the a and b allotypes of IgE. Has also been shown to bind to IgE allotype a only but not to allotype b. Binds aggregated IgE but not the monomeric form and bound monomeric IgG is readily displaced by IgE complexes. Binding to IgE promotes macrophage-mediated phagocytosis, antigen presentation to T cells, production of pro-inflammatory cytokines and the late phase of cutaneous allergic reactions. Mediates enhanced ADCC in response to afucosylated IgGs. |
A0A0B4J1N3 | GP15L_MOUSE | Protein GPR15LG (Protein GPR15 ligand) (Protein GPR15L) | MRLLALSGLLCMLLLCFCIFSSEGRRHPAKSLKLRRCCHLSPRSKLTTWKGNHTRPCRLCRNKLPVKSWVVPGALPQI | Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15. May be a tumor suppressor together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). May regulate keratinocyte proliferation. In addition, through activation of Mas-related G protein-coupled receptors (MRGPRs) contributes to pruritogenesis by activating itch-selective sensory neurons and mast cells degranulation. Has antimicrobial activity against Gram-positive bacteria, including Staphylococcus aureus and Actinomyces spec., and Mycoplasma hominis and lentivirus. |
A0A0B4J2F0 | PIOS1_HUMAN | Protein PIGBOS1 (PIGB opposite strand protein 1) | MFRRLTFAQLLFATVLGIAGGVYIFQPVFEQYAKDQKELKEKMQLVQESEEKKS | Plays a role in regulation of the unfolded protein response triggered by endoplasmic reticulum (ER) stress resulting from the presence of unfolded proteins in the ER lumen. |
A0A0B4J2F2 | SIK1B_HUMAN | Putative serine/threonine-protein kinase SIK1B (EC 2.7.11.1) (Salt-inducible kinase 1B) | MVIMSEFSADPAGQGQGQQKPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARKKFWQILSAVEYCHDHHIVHRDLKTENLLLDGNMDIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCESLIRRMLVVDPARRITIAQIRQHRWMRAEPCLPGPACPAFSAHSYTSNLGDYDEQALGIMQTLGVDRQRTVESLQNSSYNHFAAIYYLLLERLKEYRNAQCARPGPARQPRPRSSDLSGLEVPQEGLSTDPFRPALLCPQPQTLVQSVLQAEMDCELQSSLQWPLFFPVDASCSGVFRPRPVSPSSLLDTAISEEARQGPGLEEEQDTQESLPSSTGRRHTLAEVSTRLSPLTAPCIVVSPSTTASPAEGTSSDSCLTFSASKSPAGLSGTPATQGLLGACSPVRLASPFLGSQSATPVLQAQGGLGGAVLLPVSFQEGRRASDTSLTQGLKAFRQQLRKTTRTKGFLGLNKIKGLARQVCQVPASRASRGGLSPFHAPAQSPGLHGGAAGSREGWSLLEEVLEQQRLLQLQHHPAAAPGCSQAPQPAPAPFVIAPCDGPGAAPLPSTLLTSGLPLLPPPLLQTGASPVASAAQLLDTHLHIGTGPTALPAVPPPRLARLAPGCEPLGLLQGDCEMEDLMPCSLGTFVLVQ | Probable serine/threonine-protein kinase. |
A0A0B4K692 | NEP2_DROME | Neprilysin-2 (EC 3.4.24.11) [Cleaved into: Neprilysin-2, soluble form] | MQTVIQNPNWWRRRNKLEKSLLVSLGIMFVVLATGFGLWIGKVLRTSPPSNPQATALHGDSTTINQVPTGTASKGKSGDSGDVCLTQECIHTASTVLRKMKPEVEPCDNFYEFACGTYLEEENIPDDKVSISTFSVISDKLQEQLKDIITAERPETEPKHFRLPNLLYKACMNKTLIETLGPEPITRVAERLGGWPLIKGDSWNADDSWTWQEQVKKFRTAGFSMDYIIDFSIGVDLQNSTKRLIDLDQSSLALSREYLVKGFNETLVTAYYKYMVDIAVLFGANRDLAKTELLLSLEFEMALANISWPNEKRRNSSELYNLRTPAQLQAAYPYVQWVDYMNALLPEGLNVAEDEMINLSVPSFFEDLGKLLAKTPKRVIANYMFWRIHGFSVGFLSEEFRKRQLQYATALSGRQEQEARWKECVDIATSSMDEVCEDDFDSLGISVGSLYVGKHFHKDSKANALEMVNEIRNVFNDILDEVNWMDAKTKKEAKLKLHSMATHIGYPDEMLDNEKLAAYYAKLDIDPDKYFESFLGMNIFGTDYSFNKLRLPVNKTDWVRHARPAIVNAFYSSLENSIQFPAGILQGHFFNAQRPKYMNFGAIGYVIGHEITHGFDDQGRQFDVKGNLRDWWHPDTQKAYLAKAKCIIEQYGNYTERATGLNLNGINTQGENIADNGGVKESYIAYRRWAEKHGPEAKLPGLDYTPEQMFWVAAGQTWCAKYRKESLKMRITTGVHSPSEFRVLGSLSNMKDFAKDFHCPEGSPMNPVQKCEVW | Metalloendoprotease which cleaves peptides such as tachykinin peptide TK-2 at the amino side of hydrophobic residues. Functions in female fertility, embryogenesis and memory formation. Required in females for normal patterns of egg laying, probably due to its function in sperm retention and preventing sperm displacement by rival ejaculates. Also required for normal patterns of hatching due to its important role in early embryonic development. Required in the dorsal paired medial neurons for the proper formation of middle-term memory. Also required in the mushroom body neurons where it functions redundantly with neprilysins Nep3 and Nep4 in normal long-term memory formation. |
A0A0B4K7J2 | RBP2_DROME | E3 SUMO-protein ligase RanBP2 (EC 2.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) | MFTTRKEVDAHVHKMLGKLQPGRERDIKGLAVARLYMKVQEYPKAIEYLNGYLRVRDDAVGHNMIATCYSRLNPPDVTEALQHYQRSIQIDPRQSEVVIDACELLVKENNASITECARYWLDQANSLDLSGNKQVFNLRMRVNLADSNGERDDTSGGDGEQNTLEILMYKELQARPQDVNIRIQLLRSYVEKMKIDQAFNYALKTELESKNCTSQSNEWYEQIWMVLFKIEMAKDVKKNWRFWHFALHTLDRLVQLSLEGSGLADSSKQLFRLDQYLFKFSTSIERSGDAPQRDLHQACIDHFTGQLLLHAVTLIFKREVLANKNKWMSTLRSALPLLLLGYQVRPIDDSSTNQWIKHCDAEQKQLIQMWRPQGAFRCAQLGRTLLGCLDRSQMEIKNDRENAEFDENKNSGNSMPGLFADSEELLASAHQQCLDKSWRSQIYQQLFTHAEHKLKDTSSHLVRNLRLQLPLFEWPNLAHIENYELQALVLPPHSLAQHVYLALGTDPNKLGDAPRVVFYEGFQRDVKQNLNYCGQDSISQVDVDLYLYATTIQTRRKLQIQREVYDSSNLGNRNAAARPHMMPFANLVGQLGAPEQSNWWDLVVRLNSNQLITEGNRAEQRAQLQHGLEAVRGVNGPKADAIIIFQLGKILNSRSDRSSLEARIDTLYRQGFSILRHQHNQQMESYVRVFKYGSAGSTAAWQDLQSLAEEAVTYFSEKMFRIGQYEQFLDEVRGLHLPMAYFLQSEACHHLEESSKLPRTSRDRYSERRRECLQKTQKLIKNDDKHPLIAAMHRHQQDRNSRGIDNSFGSPDVHNNSSAYEDAEDDFYSHAAFSANRSRRQLEVTPVTPIVMAQPSQEMEQAVKQISKSLCVLKDDVSVGMEAMRQDIKVLTEKFTGLEDLLKKIKISSRDTPTRDVDPAAALGLDDLFIIEDALAEHQQQQQHQQQQSHNQGAIHPVVPNPYTSGFYNGMPNTPSAQERFLQGPYGSPMFNQNQMYNYYAAQAQAQAQAQFLRTPPAPGSIPPPNMFGPRNPNFGLPSMFPPPTVPSVAPYIDAMGNFTQPPPSLIPPPAQPAAPPAPLNILESKPVVALPTPGFFNTTTPVFGASPIQVPQSKPLTVPTVPIPSTAPAPPIAGTVNPPATTAVPPPVHIPQVAPSVPAQPPAPAPVSVPSMFNRALNNQPVEKEPPANVVITSSDPLPKPTTASVQPTLSVTIPAQHIKPSLVQAPEQPAQSAQPAQPSVSGVGSLSFNFGSKSSESPFSFKTQVAKAAAEKQKEQEEAEQNQSGATDPNKTLPQDTSADDYDPRPDFKPIIPLPDEVEVRTGEEGEDIKFTSRAKLFRYVDKEWKERGTGVIKILCDKATGVSRVLMRRDQTHKVCANHTITADITINVANQDKDKKSLLWAANDFADEQVTLERFLVRFKTGELAEEFRVAFTKASEAAKSKETVKPTVNTAEKGSTATAPAAFKSFVTSTPAANSLINKPQEQTKTQPNPDPPATAAKSLFGTLSVSAAPATSAPASATPFASFSFTPNGSSGFGTSTASPFGNLSFGTASAVGSGNNTTLFTTALIKDNTVQGKTLQQESQLNKSNSSDAEEEYVPTAQFVPVIALPDIVEVVTGEENEDVLFEHRAKLLRWDKEANEWKERGLGNMKLLRDRTDPNKVRLLMRREQVHKLCCNQRLLPETKFTYATNCKAAVTWGAQDYSDEELTTALLAVRFKSQDICQQFLEAVQKAQQSIGNEPKKEEVPSAAGEKEKPIKGFGDAFKPKAGSWNCQACYTNNGQDQLYCLACQEPKDATVPPKQSGLDQGNALNLTTSSSNKFSFGFASSATLPATGGFSFGGATQPKEKPAVAVVTASASAPTSVQTAALGFGKSSMTSGFGDAFKPAVGSWSCSACYVNNPGESLYCSACDAPKNDTVPQKEKSLGSGLNLPPTSKFSFGFGAAAAGDKDQAGDGATFNFAAMPAAVAPTTSIGSSSFTFSMTKPKPDQQQPNSTAAKEDEDNDSQEVEEEENNTYFSPVIPLPDKIDVKTGEEDEELLYVHKAKLYRLNESDWKERGLGDVKILRHRQTKKLRVVMRREQVFKICLNHVLNENVVYREKTETSWMFAVHDFSEGESVLERFTLRFKNKEVAQGFMEAIKNALNETAKPIEDSPVVGSVSQSTEANKPSQKNDGAAKSRGGESEVLDVGKTSSVRPTTHEVIPPLPMTLPLLTLPQPLAKPNDYQTPATILFKGSSLSRNNSSASEASKTPSSAFIFGSTDKSEPGKDAGPLANLQKLASGEGQGNVLGSIFRSGSSNENSSDGSVKFFFGGGNKAAEQQKKDSSESVFGGNKADSQSPATQEAPKLAFGGIAAPVFGDANPFGGHKVNLQKSDGKEEPKSIIGGTPLLFGGSNAFGIPKIETQSPAKDFVFGSAPAFGQMATFSFTAAKNEKEKDITSNNTTDLKAEGKEKKELVPETTSTFADLAKTGSTFADLASNPGGTFADLANKTGNDFANLSANSQGTTVGFNKSAGGGFYNLTHQNAFKNFESPQATEECDDDGDATTDDNYDPHYDAIVELPDEIVVTTGEENETKLFGERAKLYRYDAESKQWKERGVGEIKVLEHPELQTFRLIMRQEQIHKLVLNMNISASLQMDYMNAQMKSFLWAGYNYAVDAEGKVDTEGVLERLACRFAKEEIASEFLNTVNSCIKRAKALQGDEENKNDDAPEEQASS | E3 SUMO-protein ligase (By similarity). Component of the nuclear pore complex (NPC), a complex required for trafficking across the nuclear envelope. Required for nuclear import of nuclear localization signal (NLS)-containing proteins in an importin alpha/importin beta-dependent manner, but also for the nuclear import of specific proteins such as phosphorylated Mad or the sesquiterpenoid juvenile hormone receptor Met as part of the juvenile hormone signal transduction pathway. Plays a role in nuclear mRNA export by recruiting the mRNA transport complex composed of Nxt1 and sbr/Nxf1 to the NPC. Essential during germline development for transposon silencing and piRNA biogenesis probably by regulating piwi localization to the nucleus. During oogenesis, required to form granules that modulate the biogenesis of annulate lamellae containing nuclear pore complex components. |
A0A0B4KEE4 | KOI_DROME | Klaroid protein | MSENTYQIETRRRSRSKTPFLRSSCDHENCEHAGEEGHVHHLKRKSAAPNVQTIIEEHIVESSISKKTRAKAFAQLTSDYSSDDMTPDAKRKQNSITATVTSILTKRSGGATSTPRNRSQLETTQNTLNSAQEKLNQSNGNLSSGNVSDYLAYIEYRDAGEYWNKTPKTDYTYSELSPHRRQLAPGIVAMPNMSRKSLENHNDRVNYMVQQNPAQEEFIRRRYQSKYTQQVNYDSADELDATFGQQKQSWWLIRLIQLVVSSITTVWSRVTNLSATETTAYQNYHAKRQQSQQVGLWWKIVQTIGGGLASLLRYLYVFIGSVLSLDTWLLRSSDAENKSKKRFLIFLLILLPLLLLSGWLLLQEDQRSAYVQRAEALLPLPLSIFGSLRSRFSNAGATLKSWMEVPTVRSPQREAEAIKVNMASIEQNIQKALTAEEYENILNHVNSYVQQLVELKMQQHSKELAPQQIELFVKLMKENLKQIMYKTELSEKDLSDLAIKLKLELQSSGGWQDGAKLSQANLEEITKLIKAEVHLHESHYTIQLDRIDFASLLERILAAPALADFVDARISLRVGELEPKESSGSSDAEVQIERLNREIAFIKLALSDKQAENADLHQSISNLKLGQEDLLERIQQHELSQDRRFHGLLAEIENKLSALNDSQFALLNKQIKLSLVEILGFKQSTAGGSAGQLDDFDLQTWVRSMFVAKDYLEQQLLELNKRTNNNIRDEIERSSILLMSDISQRLKREILLVVEAKHNESTKALKGHIREEEVRQIVKTVLAIYDADKTGLVDFALESAGGQILSTRCTESYQTKSAQISVFGIPLWYPTNTPRVAISPNVQPGECWAFQGFPGFLVLKLNSLVYVTGFTLEHIPKSLSPTGRIESAPRNFTVWGLEQEKDQEPVLFGDYQFEDNGASLQYFAVQNLDIKRPYEIVELRIETNHGHPTYTCLYRFRVHGKPPAT | Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Is required to nuclear migration in eye and to anchor klar in the nuclear membrane. |
A0A0B4KGY6 | NOVA_DROME | RNA-binding protein Pasilla | MESIMKVAMDKAAEQLIQQFGFDYLQQQLQLQHQNQHNSSPQQPQHQQLEPENEHLTYQYQQSKPTHMQQLACNYQPRHSTTTSSPSSTHSLASGGGSSSNSSNSSSSDSSSINISHISNISNISNIGNISNSNHSNAAYSLAVHSYQKQIESPANPSHVPHHQMDLSPLSENGSPNGTPGAQTPTATASGNTAAALASAAAAAAAATSGGNGSSITNCNSNNSSSSSNAQQQLQLGNYKTNSCWCYGESVCSGIEVEIENNNNNHIHHGETTYHMKILVPAVASGAIIGKGGETIASLQKDTGARVKMSKSHDFYPGTTERVCLITGSTEAIMVVMEFIMDKIREKPDLTNKIVDTDSKQTQERDKQVKILVPNSTAGMIIGKGGAFIKQIKEESGSYVQISQKPTDVSLQERCITIIGDKENNKNACKMILSKIVEDPQSGTCLNVSYADVSGPVANFNPTGSPYATNQNAINSSTASLNSTLGTTIGGANSAASLLVNGTGINLSINLGSPNPAPNLAVATQLLEHIKVAMRGSGYSETVTNEVVAALSVLAKYGVLGMGVGVSHTNGAHSTLGNFLGVTTLDQQTAAAASAATASNVFGAVGQVNLEQYAAAVASAAAASRPTQSQLDAAAVQFDPFRHLGSATAPAATPVSLNNNSFGLTATTGTATTAQLGGLSKSPTPGDLSSKDSKNVEVPEVIIGAILGPSGRSLVEIQHVSGANVQISKKGIFAPGTRNRIVTITGQPSAIAKAQYLIEQKINEEETKRARQIPLTTVVN | Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion (By similarity). Plays a role in long-term memory formation by processing the unspliced Orb2-isoform A (Orb2A) mRNA and thereby controlling Orb2A protein abundance. |
A0A0B4LFY9 | STING_DROME | Stimulator of interferon genes protein homolog (dSTING) (dmSTING) | MAIASNVVEAGNAVRAEKGRKYFYFRKMIGDYIDTSIRIVATVFLADLLLRLYRCVVEYGSNGRYYLPEDRLWIILRRSCTYNNRSIYLIVGFLLVAFFRISVTGNYRNVMPTTLFLFQMPLYWIWSFTDMDQSTLSYSHWIRDSHGLDYAAGMASNYFHGYLKLSLPERKDDGLKHRLAMYEDKNNVTFGIKRLVILIPDEMFVNGVLESHLLDKAEPLETQFINRAGVYRPFKHDVYRMNKKVNGRTYYFAVEGATPMISFFDATYSNLSGTWQMQELKREIWIKFYKHLKELITTWPETRDLVELIIYNSHDSKGNLVDVGELLVAHMQNKTKTIDEISN | Facilitator of innate immune signaling that binds cyclic dinucleotides produced in response to infection by bacteria and/or viruses, and promotes the activation of the NF-kappa-B transcription factor Rel (Relish). Recognizes and binds cyclic di-GMP (c-di-GMP), a cyclic dinucleotide messenger produced by bacteria such as L.monocytogenes, leading to activation of the peptidoglycan recognition protein (IMD) signaling pathway and activation of Rel (Relish). Innate immune response is triggered in response to double-stranded RNA from viruses delivered to the cytoplasm: Sting acts by specifically binding cyclic dinucleotides 3',2'-cGAMP and 2',3'-cGAMP produced by cGlr1 and cGlr2 in response to RNA virus in the cytosol. Has a strong preference for 3',2'-cGAMP compared to other cyclic dinucleotides such as 2',3'-cGAMP or 3'3'-c-di-GMP. Upon binding to 3',2'-cGAMP, activates an antiviral immune response, leading to the activation of Rel (Relish). Activated in brain in response to Zika virus infection, leading to autophagy. |
A0A0B4U9L8 | VMF1_VIPAA | Zinc metalloproteinase-disintegrin-like protein F1 (EC 3.4.24.-) (Fibrinogenase 1) (Metalloproteinase F1) (P-IIIa metalloproteinase F1) (Snake venom metalloproteinase) (SVMP) (VaF1) | MLQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPQKLTALLKGAIQQPEQKYEDAMQYEFKVNGKPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNDAHLTASISACNGLKGHFQLRGETYLIEPLKIPDSEAHAVYKYENVEKEDEGPKKCGVTQTNWKSDEPIKASQFILTPEQRAYMNANKYIKLAIVVDNVMFRKYTGNFTAIRTRIYEIVNTLNLIYTILNIHIALVFLEIWSKGDSINVQSVVDVTLNSFGEWRERDLLNRKRHDNAQLLTGINFNGDTIGFGFVGSMCIPKKSVGIVQDHSKTHLLVATTMAHELGHNLGINHDGDSCTCQANSCIMAAKLSHQPSYQFSDCSINELWMYLISHTPRCILNEPLTTDVVSPAVCGNYVVEEGEECDCGSLWYCRNPCCDAATCKLKPGAECGDGVCCYQCRFVTAGTVCRPARSECDIPEYCSGQSVECPMDHIQKNGKPCLMNHGYCYNGRCPIMIHQCIALWGPGTTVSSDVCFQRNESGQGYSYCRRENNQNIPCAPQDVKCGRLYCKFHNVNTLPCNFKYSDFAPDYGLVDHGTKCGDGKVCNSNRQCVDVNTAY | Zinc metalloprotease that has fibrinogenolytic activity. Does not have hemorrhagic activity in rats. Cleaves insulin B chain at '38-Ala-|-Leu-39' and '40-Tyr-|-Leu-41' bonds. Hydrolyzes only partially and weakly isolated extracellular matrix (ECM) bovine fibronectin and basal membrane (BM) protein human collagen IV in vitro. Murine laminin is not hydrolyzed, neither isolated nor in a solubilized BM preparation. Nidogen is hydrolyzed at '350-Ser-|-Phe-351' bond in a solubilized BM preparation. Hydrolyzes plasma proteins involved in blood coagulation in vitro. Has alpha-fibrinogenase activity cleaving human fibrinogen alpha chain at '432-Lys-|-Leu-433' bond, but does not cleave beta or gamma chains. Does not cleave fibrin. Hydrolyzes only partially bovine prothrombin at '200-Ser-|-Gly-201' bond, factor X (FX) heavy chain, and very slowly, FX light chain and plasminogen in vitro, without activating any of them. Has no effect in plasma thrombin generation. Does not inhibit platelet aggregation induced by collagen in vitro. May have a delayed pathological action as an anticoagulant in envenomed patients after they received serotherapy as it is not recognized by the venom antiserum. |
A0A0B5A051 | PT1L_HUMLU | 2-acylphloroglucinol 4-prenyltransferase (EC 2.5.1.136) (Aromatic prenyltransferase PT1L) (Humulus lupulus prenyltransferase-1-like) (HlPT1L) | MELSSVSSFSLGTNPFISIPHNNNNNLKVSSYCCKSKSRVINSTNSKHCSPNNNNNNNTSNKTTHLLGLYGQSRCLLKPLSIFSCKDQRGNSIRASAQIEDRPPESGNLSALTNVKDFVSVCWEYVRPYTAKGVIICSSCLFGRELLENPNLFSWPLIFRALLGMLAILGSCFYTAGINQIFDMDIDRINKPDLPLVSGRISVESAWLLTLSPAIIGFILILKLNSGPLLTSLYCLAILSGTIYSVPPFRWKKNPITAFLCILMIHAGLNFSVYYASRAALGLAFVWSPSFSFITAFITFMTLTLASSKDLSDINGDRKFGVETFATKLGAKNITLLGTGLLLLNYVAAISTAIIWPKAFKSNIMLLSHAILAFSLFFQARELDRTNYTPEACKSFYEFIWILFSAEYVVYLFI | Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the first prenylation step in the beta-bitter acid pathway. Uses dimethylallyl diphosphate (DMAPP) as the prenyl donor. |
A0A0B5A886 | GP_SFTSV | Envelopment polyprotein (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)] | MMKVIWFSSLICLVIQCSGDSGPIICAGPIHSNKSAGIPHLLGYSEKICQIDRLIHVSSWLRNHSQFQGYVGQRGGRSQVSYYPAENSYSRWSGLLSPCDADWLGMLVVKKAKESDMIVPGPSYKGKVFFERPTFDGYVGWGCGSGKSRTESGELCSSDSGTSSGLLPSDRVLWIGDVACQPMTPIPEETFLELKSFSQSEFPDICKIDGIVFNQCEGESLPQPFDVAWMDVGHSHKIIMREHKTKWVQESSSKDFVCYKEGTGPCSESEEKACKTSGSCRGDMQFCKVAGCEHGEEASEAKCRCSLVHKPGEVVVSYGGMRVRPKCYGFSRMMATLEVNPPEQRIGQCTGCHLECINGGVRLITLTSELRSATVCASHFCSSASSGKKSTEIHFHSGSLVGKTAIHVKGALVDGTEFTFEGSCMFPDGCDAVDCTFCREFLKNPQCYPAKKWLFIIIVILLGYAGLMLLTNVLKAIGVWGSWVIAPVKLMFAIIKKLMRTVSCLVGKLMDRGRQVIHEEIGENGEGNQDDVRIEMARPRRVRHWMYSPVILTILAIGLAEGCDEMVHADSKLVSCRQGSGNMKECITTGRALLPAVNPGQEACLHFTAPGSPDSKCLKIKVKRINLKCKKSSSYFVPDARSRCTSVRRCRWAGDCQSGCPPHFTSNSFSDDWAGKMDRAGLGFSGCSDGCGGAACGCFNAAPSCIFWRKWVENPHGIIWKVSPCAAWVPSAVIELTMPSGEVRTFHPMSGIPTQVFKGVSVTYLGSDMEVSGLTDLCEIEELKSKKLALAPCNQAGMGVVGKVGEIQCSSEESARTIKKDGCIWNADLVGIELRVDDAVCYSKITSVEAVANYSAIPTTIGGLRFERSHDSQGKISGSPLDITAIRGSFSVNYRGLRLSLSEITATCTGEVTNVSGCYSCMTGAKVSIKLHSSKNSTAHVRCKGDETAFSVLEGVHSYIVSLSFDHAVVDEQCQLNCGGHESQVTLKGNLIFLDVPKFVDGSYMQTYHSTVPTGANIPSPTDWLNALFGNGLSRWILGVIGVLLGGLALFFLIMFLLKLGTKQVFRSRTKLA | [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity). Plays a role in the packaging of ribonucleoproteins and polymerase during virus assembly. [Glycoprotein C]: Structural component of the virion that interacts with glycoprotein N (By similarity). Acts as a class II fusion protein that is activated upon acidification and subsequent repositioning of the glycoprotein N (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By similarity). They are able to attach the virion to the host cell receptor CD209/DC-SIGN and to promote fusion of membranes with the late endosome after clathrin-mediated endocytosis of the virion (By similarity). |
A0A0B5A8P4 | INS3A_CONGE | Con-Ins G3 (Insulin 3) [Cleaved into: Con-Ins G3 B chain; Con-Ins G3 A chain] | MTTSFYFLLVALGLLLYVCQSSFGNQHTRNSDTPKHRCGSELADQYVQLCHGKRNDAGKKRGRASPLWQRQGFLSMLKAKRNEAFFLQRDGRGIVEVCCDNPCTVATLRTFCH | This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock. It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor (INSR) and assembly of the hormone's hexameric storage form (By similarity). Despite lacking this segment, it both binds and activates human insulin receptor (long isoform (HIR-B)) with a high potency (EC(50)=242 nM). In vivo, intraperitoneal injection of this peptide into zebrafish lowers blood glucose with a lower potency than human insulin. In addition, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency (By similarity). When tested on a mouse model of diabetes, this insulin also lowers blood glucose with a 10-fold lower potency than human insulin (By similarity). |
A0A0B5AC19 | NSS_SFTSV | Non-structural protein NS-S (NSs) | MSLSKCSNVDLKSVAMNANTVRLEPSLGEYPTLRRDLVECSCSVLTLSMVKRMGKMTNTVWLFGNPKNPLHQLEPGLEQLLDMYYKDMRCYSQRELSALRWPSGKPSVWFLQAAHMFFSIKNSWAMETGRENWRGLFHRITKGQKYLFEGDMILDSLEAIEKRRLRLGLPEILITGLSPILDVALLQIESLARLRGMSLNHHLFTSPSLRKPLLDCWDFFIPVRKKKTDGSYSVLDEDDEPGVLHGYPHLMAHYLNRCPFHNLIRFDEELRTAALNTIWGRDWPAIGDLPKEV | Sequesters host STAT2 into viral inclusion bodies (Probable). Impairs IFN-stimulated phosphorylation and nuclear translocation of host STAT2, thereby suppressing type-I IFN antiviral signaling (Probable). Sequesters host TRIM25, RIGI, TBK1/IKK complex components (TBK1, IKBKE/IKKE, and IRF3) and IRF7 into viral inclusion bodies, thereby inhibiting the IFN responses (Probable). Inhibits TRIM25-mediated ubiquitination of the RIGI. The sequestration of IKBKE/IKKE, and IRF3 occurs via the interaction with TBK1. Sequestration and inhibition of host TBK1 probably participates to the cytokine storm induced by the virus. Also inhibits the phosphorylation of host TBK1. Interacts with host TNIP2 and promotes TPL2-TNIP2-p105 complex formation leading to IL-10 induction. By interacting with CDK1, induces host cell arrest at the G2/M transition to promote viral replication. Requested for the formation of the viral cytoplasmic inclusion bodies. |
A0A0B5AC95 | INS1A_CONGE | Con-Ins G1a (Insulin 1) [Cleaved into: Con-Ins G1 B chain; Con-Ins G1a A chain] | MTTSSYFLLMALGLLLYVCQSSFGNQHTRTFDTPKHRCGSEITNSYMDLCYRKRNDAGEKRGRASPLWQRRGSLSKLKARAKRNGAFHLPRDGRGVVEHCCHRPCSNAEFKKYCG | This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock. It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor (INSR) and assembly of the hormone's hexameric storage form. Despite lacking this segment, it both binds and activates human insulin receptor (long isoform (HIR-B)) with a high potency (EC(50)=16.28 nM). In vivo, intraperitoneal injection of this peptide into zebrafish lowers blood glucose with the same potency than human insulin. In addition, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency. When tested on a mouse model of diabetes, this insulin also lowers blood glucose with a 10-fold lower potency than human insulin. |
A0A0B5KYT4 | MPDE2_PENBR | Cytochrome P450 monooxygenase mpaDE' (EC 1.-.-.-) (Mycophenolic acid biosynthesis cluster protein DE') | MESLSLTWITAIAVVLYLVQRYVRSYWRLKDIPGPVLAKLTDLQRVWWVKTGRAHEFHRDMHAMYGPIVRFGPNMVSVSDPRVIPTIYPSRPGFPKGDFYRTQKPYTRNKGAMPAVFNTQDEDLHKQLRSPIASLYSMTNVVRLEPLVDETLTVLSKQLDERFVGTNDKPFDLGDWLQYFAFDSMGTLTFSRRYGFLEQGRDMHGILQEIWNFMTRVAVMGQIPWFDEIWNKNSFITLFKRPTGFGVLKVVDNFISQRVSSRENDEKADEKDMLSQFLNIQASNPHSIMPWAPRAWTFSNVMAGSDSTANVMRTMMYNLLVDRDTLKSLRAELLEAESSNGLSRSLPSWDGVRSLPYLDACVLEALRLHPPFCLPFERVVPEGGITVCETYLPAGTVVGISPYLANRDKQTFGDDADKWRPSRWLDLSREDRVKLENSILTFGAGRRTCLGKNIAILEIKKLFPMLLLNYEIEIVNPENYQTTNAWFFRQWGLHAVIRKLPAPERDDTIEQKASIPPALNIPPSSSTVDVRIIDSGTLLDLRPDLFWTPDLPGLLKVTAPTYCFLISNGSRHVLFDLAVRQDWENLPPSIVAMIKSQTVIQEPRNISDVLDSDESSLGIRSKDIEAIIWSHAHFDHIGDPSTFPPSTELVVGPGIRDTHWPGFPTNPDAINLNTDIQGRNVREISFEKTQKGATKIGSFDAMDYFGDGSFYLLDAAGHSVGHIGALARVTTSPDSFVFMGGDSCHHAGVLRPTKYLPCPLDSGDTSLPCKSDSVFTLSPALPTDYTAALRTVENIKELDACEDVFVVLAHDATLKGKVDFYPSKINDWKAKEYGKKTKWLFYKDIENAIEGQK | Cytochrome P450 monooxygenase part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. MpaDE' is an endoplasmic reticulum-bound enzyme that catalyzes the conversion of 5-methylorsellinic acid (5MOA) into the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP). MpaDE' first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB), and then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable). |
A0A0B5LB55 | MPAH2_PENBR | Type I acyl-CoA thioesterase mpaH' (EC 3.1.1.-) (Mycophenolic acid biosynthesis cluster protein H') | MSTEKFTITEHLVPGSHIREYPGSTVNQEDVLKIHVKQYTPKREGPVPDDAITFIATHGVGLPKELYEPLWDELLDQASGFHIRAIWMADVASMNQSGIHNEDKLSMDCSWMDHARDLLLMINHFRDQMPRPLVGIGHSFGGNIITNLAYLHPRLFTTLLLLDPLIQLSPPSLGFGTDAPSAINYTLWRDDVWPSREVAIRANRAIMQGMDPRCLDRMTKHFFRDLPTPLYPDVEAIKALFGTTADSTTTPVTLTTPKYHELVAQIRQNFNARDPKTGRIEVPRDTHADMDPLVAYIPLYRPEPRSTFRRLETLRPSCLWVIAGATFLNIDEIREGVKICGSGIGGSGGVPDGRVREVVLPGFGHLMPFQEVKTVAETCIVWLQQEMDRFRQTERQWKEDRDGKSHLAVEENWYKVLKPIPSGRKKRNDKGKL | Type I acyl-CoA thioesterase part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893. MpaH' acts as a peroxisomal acyl-CoA hydrolase that converts MPA-CoA into the final product MPA. The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (Probable). |
A0A0B6CGH9 | F7ODM_OCIBA | Oxoglutarate-dependent flavonoid 7-O-demethylase 1 (ObF7ODM1) (2-oxoglutarate-dependent dioxygenase 1) (ObDIOX1) (8-hydroxysalvigenin 7-O-demethylase) (EC 1.14.13.-) (Gardenin B 7-O-demethylase) (EC 1.14.13.-) | MRITLQYIKLESKNTKERDMAESKAIGRSLEVPNVQELAKGKLASVPARYVRYSDRENTTLPPLTQIPVIDMQALLHPNSFEAELNSLHKACKQWGFFQLINHGVEAAVMEKMKLEMQEFFNLPLEEKQKFRQSADDMEGYGQSFVVSDEQKLDWADGFSVISLPTYLRKPHLIPKLPAPFRDAIDAYGAQLKELAIKILGFMAEALGMDPHEMTALFEEGIQALRMNYYPPCPQPEMVSGLCPHSDAGGLTILMQVNEVEGLQVRKDGGWVPVSPLPDAFIINLGDILEIVTNGEYFSVEHQATVNGDKERLSVAAFLNPKMEDNIGPAASFISGETPAKFKTITAAEYFKGLFSKELDGKSYLDLMRIQN | Oxoglutarate-dependent dioxygenase (2-ODD) acting as a flavonoid 7-O-demethylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. Catalyzes the 7-O-demethylation of methoxylated flavones mediates the conversion of 8-hydroxysalvigenin (8-OH-SALV) to pilosin (PIL) and of gardenin B (GARD B) to nevadensin (NEV). |
A0A0B7P3V8 | YP41B_YEAST | Transposon Ty4-P Gag-Pol polyprotein (TY4A-TY4B) (Transposon Ty4 TYA-TYB polyprotein) [Includes: Capsid protein (CA); Ty4 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)] | MATPVRDETRNVIDDNISARIQSKVKTNDTVRQTPSSLRKVSIKDEQVKQYQRNLNRFKTILNGLKAEEEKLSETDDIQMLAEKLLKLGETIDKVENRIVDLVEKIQLLETNENNNILHEHIDATGTYYLFDTLTSTNKRFYPKDCVFDYRTNNVENIPILLNNFKKFIKKYQFDDVFENDIIEIDPRENEILCKIIKEGLGESLDIMNTNTTDIFRIIDGLKNKYRSLHGRDVRIRAWEKVLVDTTCRNSALLMNKLQKLVLMEKWIFSKCCQDCPNLKDYLQEAIMGTLHESLRNSVKQRLYNIPHNVGINHEEFLINTVIETVIDLSPIADDQIENSCMYCKSVFHCSINCKKKPNRELRPDSTNFSKTYYLQGAQRQQQLKSSAKEQKSWNKTQKKSNKVYNSKKLVIIDTGSGVNITNDKTLLHNYEDSNRSTRFFGIGKNSSVSVKGYGYIKIKNGHNNTDNKCLLTYYVPEEESTIISCYDLAKKTKMVLSRKYTRLGNKIIKIKTKIVNGVIHVKMNELIERPSDDSKINAIKPTSSPGFKLNKRSITLEDAHKRMGHTGIQQIENSIKHNHYEESLDLIKEPNEFWCQTCKISKATKRNHYTGSMNNHSTDHEPGSSWCMDIFGPVSSSNADTKRYMLIMVDNNTRYCMTSTHFNKNAETILAQIRKNIQYVETQFDRKVREINSDRGTEFTNDQIEEYFISKGIHHILTSTQDHAANGRAERYIRTIVTDATTLLRQSNLRVKFWEYAVTSATNIRNCLEHKSTGKLPLKAISRQPVTVRLMSFLPFGEKGIIWNHNHKKLKPSGLPSIILCKDPNSYGYKFFIPSKNKIVTSDNYTIPNYTMDGRVRNTQNIYKSHQFSSHNDNEEDQIETVTNLCEALENYEDDNKPITRLEDLFTEEELSQIDSNAKYPSPSNNLEGDLDYVFSDVEESGDYDVESELSTTNTSISTDKNKILSNKDFNSELASTEISISEIDKKGLINTSHIDEDKYDEKVHRIPSIIQEKLVGSKNTIKINDENRISDRIRSKNIGSILNTGLSRCVDITDESITNKDESMHNAKPELIQEQFNKTNHETSFPKEGSIGTKCKIPKYRQ | Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends. Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome. |
A0A0B7P9G0 | UEX_DROME | Unextended protein (Putative metal transporter uex) | MNTYFISFITIIIFANGINGTSVDTSNKLLLQKANDFNLSQNLSSSRTRRTIANSFRIVGIRLEDETVETKNGIPTVLVDKEQQFRVFGSGLEENTAITFTNEKNDYGGPCLKPATDLFTPIEVSSNGFSALYSVKFPSFINEFFICAKTAEKTTNHSKAATTTPLEHQGNSDFLKIKTFEPLIPVWLAIIIIVTCLGFSALFSGLNLGLMSMDRTELKILRNTGTEKEKKYASKIAPVRDQGNYLLCSILLGNVLVNSTFTILLDGLTSGLFAVIFSTLAIVLFGEITPQAVCSRHGLAIGAKTILVTKTVMAITAPLSYPVSRILDKLLGEEIGNVYNRERLKELVRVTNDVNDLDKNEVNIISGALELRKKTVADVMTHINDAFMLSLDALLDFETVSEIMNSGYSRIPVYDGDRKNIVTLLYIKDLAFVDTDDNTPLKTLCEFYQNPVHFVFEDYTLDIMFNQFKEGTIGHIAFVHRVNNEGDGDPFYETVGLVTLEDVIEELIQAEIVDETDVFVDNRTKTRRNRYKKADFSAFAERREVQTVRISPQLTLATFQYLSTAVDAFKKDVISELILRRLLNQDVFHNIKTKGKSKDDPSLYIFTQGKAVDFFVLILEGRVEVTIGKEALMFESGPFTYFGTQALVPNVVIDSPTQMGSLQSLNMDSKIRQSFVPDYSVRAISDVIYITIKRVLYLTAKKATLLEKSRKSGTFSSETFDDEVERLLHSITENEKPSCFAQNQSTRRLSNRSINSSPTNMNRSPDFVYNSVDEAIQDDTKLKNIKHADNVTTSISLVAAELEDLHSGEQDTTAASMPLLPKLDDKFESKQSKP | Probable metal transporter (By similarity). Acts downstream of PRL-1 and protects the nervous system against olfactory carbon dioxide stimulation. |
A0A0C3RR82 | PGMA1_PHLG1 | Methyltransferase/ribosomally synthesized type II borosin cyclic peptide precursor pgiMA1 (Type II borosin cyclic peptide biosynthesis cluster protein MA1) [Cleaved into: N-methyltranferase pgiM1 (EC 2.1.1.-); Ribosomally synthesized type II borosin core peptide pgiA1-I; Ribosomally synthesized type II borosin core peptide pgiA1-II; Ribosomally synthesized type II borosin core peptide pgiA1-III; Ribosomally synthesized type II borosin core peptide pgiA1-IV; Ribosomally synthesized type II borosin core peptide pgiA1-V; Ribosomally synthesized type II borosin core peptide pgiA1-VI; Ribosomally synthesized type II borosin core peptide pgiA1-VII; Ribosomally synthesized type II borosin core peptide pgiA1-VIII; Ribosomally synthesized type II borosin core peptide pgiA1-IX; Ribosomally synthesized type II borosin core peptide pgiA1-X; Ribosomally synthesized type II borosin core peptide pgiA1-XI; Ribosomally synthesized type II borosin core peptide pgiA1-XII] | MSSASSDSNTGSLTIAGSGIASVRHMTLETLAHVQEADIVFYVVADPVTEAYIKKNARGPCKDLEVLFDKDKVRYDTYVQMAETMLNAVREGQKVLGIFYGHPGVFVSPSRRALSIARKEGYQAKMLPGISSEDYMFADLEFDPAVHGCCAYEATQLLLREVSLDTAMSNIIWQVGGVGVSKIDFENSKVKLLVDRLEKDFGPDHHVVHYIGAVLPQSATVQDVLKISDLRKEEIVAQFNSCSTLYVPPLTHANKFSGNMVKQLFGQDVTEVSSALCPTPKWAAGSHLGDVVEYGPREKAAVDALVEHTVPADYRVLGGSLAFQQFMIDLALRPAIQANYKENPRALVDATKGLTTVEQAALLLRQPGAVFGVMKLRASEVANEQGHPVAPASLDHVAFTAPSPASLDHVAFSAPNPASLDHVAFIAPTPASLDHVAFSAPTPASLDHVSFGTPTSASLDHVAFEAPVPASLDHVAFAAPVPASLDHVAFAAPTPASLDHVAFAAPTPASLDHVAFAVPVPASLDHIAFSVPTPASLDHVAFAVPVPDHVAGIPCM | Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product (By similarity). |
A0A0C3VJP4 | SCP1_MEDTR | Serine carboxypeptidase 1 (EC 3.4.16.-) | MEKVSLYACLILNLSLLVIFPYSKASQADKLNEFILSRKSQNPPKTLSWEEGDALKTLFSSAAYVAPPQEELRLADKIVTLPGQPYGVNFDQYSGYVTVDPETGRELFYYFVESPCNSSTKPLVLWLNGGPGCSSLGYGAFQELGPFRVNSDGKTLYRNPYAWNEVANVLFLESPAGIGFSYSNTTSDYDKSGDKSTAKDSYVFLINWLERFPQYKTRDFYISGESYAGHYVPQLASTILHNNKLYKNTIINLKGISLGNAWIDDATSLKGLYDNLWTHALNSDQTHELIEKYCDFTKQNYSAICTNAMNMSMIEKGKIDSFNIYAPLCHDSTLKNGSTGYVSNDLDPCSDYYGTAYLNRPEVQKALHAKPTNWSHCSDSINLNWKDSPITILPTIKYLIDNGIKLWIYSGDTDAVGVTISRYPINTLKLPIDSTWRPWYSGKEIGGYVVGYKGLTFVTVRGAGHLVPSWQPERALTLISSFLYGILPASVSPSN | Carboxypeptidase that, together with KPI106, controls mycorrhiza establishment and arbuscule development during root colonization by arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis). |
A0A0C5B5G6 | MOTSC_HUMAN | Mitochondrial-derived peptide MOTS-c (Mitochondrial open reading frame of the 12S rRNA-c) | MRWQEMGYIFYPRKLR | Regulates insulin sensitivity and metabolic homeostasis. Inhibits the folate cycle, thereby reducing de novo purine biosynthesis which leads to the accumulation of the de novo purine synthesis intermediate 5-aminoimidazole-4-carboxamide (AICAR) and the activation of the metabolic regulator 5'-AMP-activated protein kinase (AMPK). Protects against age-dependent and diet-induced insulin resistance as well as diet-induced obesity. In response to metabolic stress, translocates to the nucleus where it binds to antioxidant response elements (ARE) present in the promoter regions of a number of genes and plays a role in regulating nuclear gene expression in an NFE2L2-dependent manner and increasing cellular resistance to metabolic stress. Increases mitochondrial respiration and levels of CPT1A and cytokines IL1B, IL6, IL8, IL10 and TNF in senescent cells. Increases activity of the serine/threonine protein kinase complex mTORC2 and reduces activity of the PTEN phosphatase, thus promoting phosphorylation of AKT. This promotes AKT-mediated phosphorylation of transcription factor FOXO1 which reduces FOXO1 activity, leading to reduced levels of MSTN and promotion of skeletal muscle growth. Promotes osteogenic differentiation of bone marrow mesenchymal stem cells via the TGFB/SMAD pathway. Promotes osteoblast proliferation and osteoblast synthesis of type I collagens COL1A1 and COL1A2 via the TGFB/SMAD pathway. |
A0A0C5CJR8 | APRA_PSEMA | Metallopeptidase AprA (EC 3.4.24.-) (Heat-resistant peptidase) | MSKAKDKAIVSAAQASTAYSQIDSFSHLYDRGGNLTINGKPSYTVDQAATQLLRDGAAYRDFDGNGKIDLTYTFLTSASSSTMNKHGISGFSQFNAQQKAQAALAMQSWSDVANVTFTEKASGGDGHMTFGNYSSGQDGAAAFAYLPGTGAGYDGTSWYLTNNSYTPNKTPDLNNYGRQTLTHEIGHTLGLAHPGDYNAGEGAPTYNDATYGQDTRGYSLMSYWSESNTNQNFSKGGVEAYASGPLIDDIAAIQKLYGANYNTRAGDTTYGFNSNTGRDFLSATSNADKLVFSVWDGGGNDTLDFSGFTQNQKINLNEASFSDVGGLVGNVSIAKGVTIENAFGGAGNDLIIGNNAANVIKGGAGNDLIYGAGGADQLWGGAGNDTFVFGASSDSKPGAADKIFDFTSGSDKIDLSGITKGAGLTFVNAFTGHAGDAVLTYAAGTNLGTLAVDFSGHGVADFLVTTVGQAAVSDIVA | Peptidase able to cleave azocasein and the milk substrates beta-casein and Na-caseinate. Can withstand UHT processing of milk, and is able to spoil UHT milk over the storage period. {ECO:0000269|Ref.1}. |
A0A0C5PHQ7 | ELOV5_TACFU | Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) | MEILNQRLNQQFDSWMGPRDPRVRGWLLLDNYLPTLSFTIIYLLIVWMGPKYMRNRQPVSCRGILVVYNMALTLLSLYMFYELVTAVWQGGYNFFCQDTHSGGEADNRVINVLWWYYFSKLIEFMDTFFFILRKNNHQITFLHIYHHFTMLNIWWFVMNWVPCGHSYFGATFNSFIHVLMYSYYGLSAIPAIQPYLWWKKYITQGQLVQFVLTMIQTSCAVVWPCGFPKGWLYFQISYMITLIILFSNFYIQTYKKKGTAAKKDPRHNGIKSVNGHSNGASHTNAVKNRKARTD | Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (By similarity). In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid (By similarity). |
A0A0C5Q4Y6 | C76H2_ROSOF | Ferruginol synthase 1 (RoFS1) (EC 1.14.14.175) (11-oxomiltiradiene synthase) (EC 1.14.14.-) (Cytochrome P450 76AH22) (Ferruginol monooxygenase) (11-hydroxyferruginol synthase) (EC 1.14.14.60) (Miltiradiene oxidase) | MDSFPLLAALFFILAATWFISFRRPRNLPPGPFPYPIVGNMLQLGTQPHETFAKLSKKYGPLMSIHLGSLYTVIVSSPEMAKEIMHKYGQVFSGRTVAQAVHACGHDKISMGFLPVGGEWRDMRKICKEQMFSHQSMEDSQWLRKQKLQQLLEYAQKCSERGRAIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLAIIEGFLNERVESRRTNPNAPKKDDFLETLVDTLQTNDNKLKTDHLTHLMLDLFVGGSETSTTEIEWIMWELLANPEKMAKMKAELKSVMGEEKVVDESQMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAIGRDHSIWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHRGVLFGFAVRRAVPLKIVPFKV | Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products. Catalyzes the oxidation of abietatriene to produce ferruginol. Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol. Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant. May also convert miltiradiene into 11-oxomiltiradiene (By similarity). |
A0A0C5QRZ2 | C76H2_SALFT | Ferruginol synthase (SfFS) (EC 1.14.14.175) (11-oxomiltiradiene synthase) (EC 1.14.14.-) (Cytochrome P450 76AH24) (Ferruginol monooxygenase) (11-hydroxyferruginol synthase) (EC 1.14.14.60) (Miltiradiene oxidase) | MDPFPLVAAALFIAATWFITFKRRRNLPPGPFPYPIVGNMLQLGSQPHETFAKLSKKYGPLMSIHLGSLYTVIISSPEMAKEIMHKYGQVFSGRTIAQAVHACDHDKISMGFLPVGAEWRDMRKICKEQMFSHQSMEDSQNLRKQKLQQLLEYAQKCSEEGRGIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLGLIEGYLNERIEFRKANPNAPKKDDFLETLVDALDAKDYKLKTEHLTHLMLDLFVGGSETSTTEIEWIMWELLASPEKMAKVKAELKSVMGGEKVVDESMMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGAQVLINAWAMGRDPSLWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEASDAHKGVLFGFAVRRAVPLKIVPIKA | Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products. Catalyzes the oxidation of abietatriene to produce ferruginol. Catalyzes the oxidation of ferruginol at C-12 to produce 11-hydroxyferruginol. Ferruginol and 11-hydroxyferruginol are intermediates in the biosynthesis of carnosate, a potent antioxidant. May also convert miltiradiene into 11-oxomiltiradiene (By similarity). |
A0A0C5XL88 | PART_SPHYB | Prs ADP-ribosylating toxin (EC 2.4.2.-) (Mono-ADP-ribosyltransferase) (mART) | MTTSFWRIATDARTYEADDLSGAGAKITGGRWNEVGVAIVYAASSRALACLETVVHLNSGGLPLNRYLVEIEVPDEVLASAEVATPGNLPVGWDAEPAGRVSISFGSQWAQSQRTALLLVPSVIVPEETNLLINPAHPDAKGIKARKVRKWLYDPRMIRKA | Toxic component of a type II toxin-antitoxin (TA) system. Expression in E.coli inhibits cell growth bacteriostasis is neutralized by expression of cognate antitoxin ParS. ADP-ribosylates E.coli ribose-phosphate pyrophosphokinase (RPPK, prs) using NAD(+) in vitro ADP-ribosylates RPPK on 'Lys-182' and 'Ser-202'. Cannot use NADP(+). Also auto-ADP-ribosylates in vitro in the presence of RPPK auto-ADP-ribosylation decreases. |
A0A0C6DRW4 | DSZC1_RHOER | Dibenzothiophene monooxygenase (DBT monooxygenase) (DBT-MO) (EC 1.14.14.21) | MTLSPEKQHVRPRDAADNDPVAVARGLAEKWRATAVERDRAGGSATAEREDLRASGLLSLLVPREYGGWGADWPTAIEVVREIAAADGSLGHLFGYHLTNAPMIELIGSQEQEEHLYTQIAQNNWWTGNASSENNSHVLDWKVRATPTEDGGYVLNGTKHFCSGAKGSDLLFVFGVVQDDSPQQGAIIAAAIPTSRAGVTPNDDWAAIGMRQTDSGSTDFHNVKVEPDEVLGAPNAFVLAFIQSERGSLFAPIAQLIFANVYLGIAHGALDAAREYTRTQARPWTPAGIQQATEDPYTIRSYGEFTIALQGADAAAREAAHLLQTVWDKGDALTPEDRGELMVKVSGVKALATNAALNISSGVFEVIGARGTHPRYGFDRFWRNVRTHSLHDPVSYKIADVGKHTLNGQYPIPGFTS | Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner (Ref.2, PubMed:11229908). Also acts on thioxanthen-9-one and 4,6-dimethyl DBT and 2,8-dimethyl DBT (Ref.2). |
A0A0D1DWQ2 | CMU1_USTMA | Secreted chorismate mutase (EC 5.4.99.5) | MKLSVSIFVLLAVSAFGGGSAAAVSGKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQAYLIPITTQIEAAAILDHANKCT | Secreted chorismate mutase that is one component of a cocktail of effectors shaping the host metabolome and acting as virulence factors. The enzyme is taken up by plant cells, can spread to neighboring cells where it affects the biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway. Interfers with the activity of host cytosolic chorismate mutase CM2 through heterodimerization. |
A0A0D1DWZ5 | RRM4_USTMA | RNA-binding protein RRM4 | MSDSIYAPHNKHKLEAARAADAAADDAATVSALVEPTDSTAQASHAAEQTIDAHQQAGDVEPERCHPHLTRPLLYLSGVDATMTDKELAGLVFDQVLPVRLKIDRTVGEGQTASGTVEFQTLDKAEKAYATVRPPIQLRINQDASIREPHPSAKPRLVKQLPPTSDDAFVYDLFRPFGPLRRAQCLLTNPAGIHTGFKGMAVLEFYSEQDAQRAESEMHCSEVGGKSISVAIDTATRKVSAAAAEFRPSAAAFVPAGSMSPSAPSFDPYPAGSRSVSTGSAASIYATSGAAPTHDTRNGAQKGARVPLQYSSQASTYVDPCNLFIKNLDPNMESNDLFDTFKRFGHIVSARVMRDDNGKSREFGFVSFTTPDEAQQALQAMDNAKLGTKKIIVRLHEPKTMRQEKLAARYNAANADNSDMSSNSPPTEARKADKRQSRSYFKAGVPSDASGLVDEEQLRSLSTVVRNELLSGEFTRRIPKVSSVTEAQLDDVVGELLSLKLADAVEALNNPISLIQRISDAREQLAQKSASTLTAPSPAPLSAEHPAMLGIQAQRSVSSASSTGEGGASVKERERLLKAVISVTESGAPVEDITDMIASLPKKDRALALFNPEFLKQKVDEAKDILDITDESGEDLSPPRASSGSAPVPLSVQTPASAIFKDASNGQSSISPGAAEAYTLSTLAALPAAEIVRLANSQSSSGLPLPKADPATVKATDDFIDSLQGKAAHDQKQKLGDQLFKKIRTFGVKGAPKLTIHLLDSEDLRALAHLMNSYEDVLKEKVQHKVAAGLNK | Key RNA-binding protein involved in the formation of polar-growing hyphae which is essential for infection by the plant pathogen. During filamentation, assembles into particles that shuttle bidirectionally along microtubules to both poles. The RRM4 transport particles are part of the endosomal mRNP transport that regulates polarity of the infectious hyphae by transporting distinct mRNAs encoding, for example, the ubiquitin fusion protein UBI1, the small G protein RHO3, or the septin CDC3, from the nucleus to cell poles. Recognizes a broad spectrum of cargo mRNAs and precisely binds at stop codons, which constitute landmark sites of translation, suggesting an intimate connection of mRNA transport and translation. Binds also to the specific binding motif UAUG of cargo mRNAs via its third RRM. Plus-end-directed KIN3, a kinesin-3 type motor, mediates anterograde transport of RRM4-containing mRNPs whereas split dynein DYM1-DYN2 functions in retrograde movement of mRNPs. |
A0A0D1E015 | UPA1_USTMA | FYVE zinc finger domain protein UPA1 (PAM2 domain-containing protein UPA1) | MTIPDPANIIHNDAGTASPHHIWADVGDSTSSSQHEATRSRSDDANGGASASMHAPQHVKANRAAQPTYDSSDLPSFGLSARLTRDSSSFGSKPSSSASDSRRPKFAPYEAENLWATSSTTSHPSKASQSTLSPNASVFKPSRSLQPNHFEPHAVANVHDFDDPLNSAYSSDTVSPRPDHAPLDHEQPQQPSALDPVAVSKVEEQRGDHSIPHQNGLVSAQAQTASDAVSTSKYTTEAADQEEDQDDFVYPGADSPSSGQAAVQDEQQAVTDSQTTKSLTKQESDPEASSTSLSAPAEAEHIVVGSAAEQSLTSSAPAETAVHIDYDTLAQLCSRGPLSDLQSFFHTAQESGLSMFSLSNDPNPGNGLVPLHFAAKDGKTDIVRWLITQAGAIVEMEDREGETALHKAAMAGKLSVASLLLSHGADANAQDADGWTALHNACSRGYLDLVRLLVDRGHAQIDVQGGRGAWTPLMNAASKGHLPVVRHLTAKYHADPFVRNAAGETAFDVAAATFEVYICEILERYEAERWNASKFTTSSPSRSGAIVPGRGPYEPLALHTTIPVILHENQRLDTRLQTLALNGGKPRWSSSSAARAHKPDRRSPSSMPPGPLAPSRTRHVPMRQDDVGLPTRSLPYKLRLRSRVGPAAARRRAAALAAQHTPNPQDCHDDDLASTPTPESVLQARRGTSSVNGASAQHADAESSHFWLCEWQLDTTHPLVDVEHGWQYAQSFDALDDKWSSQPPPPLERLLEGRGLSASVTRAITGGAGFANAQAEQEISSSSWVRRRRWIRVLRRRLDIEFGDDLEACEGATGAGAEHLVLSSESQSNGDGSHGLSTAAIMAAQEAAKSECSQLGPDADYVSRAKALAGPSAASGATPADAMGADRDELARRIARLVMANTELRAAFEDDDVERRSRAEELRKEYALQLGQLREAAGLDEDEDEDAADDDDDEFIYPNSYKDDGASVFTRLVNGETSGTLSRPSLSQRQSSAASMLRNSVAPSEAGTSLAAARSADLAANREFRVPTNEAPNKVVLRHGPTMREQNLQPQWQRDEEAKDCIGCGRHFTFFLRKHHCRRCGRIFCDACSSKRAQLRMAELVVDPSLPSMAASEVLAPTRVCNGCHAELQLPPQLQNMRGADAMMAASRSRGADEVSGRSILETQLEDGAFRSTLAPPSDVSSRASELTECPVCSTTLSALGGSEEQEAHVRNCLENGGGGSMQGGRYLVYKLPEDSPIVGKECSICMEDFVANSTIARLPCLCYFHRGCIDSWFKRGRECPVHARDW | FYVE zinc finger domain protein that functions in endosomal targeting and transport of mRNAs, as well as associated ribosomes. The endosomal mRNA transport regulates polarity of the infectious hyphae by transporting a broad spectrum of cargo mRNAs from the nucleus to cell poles. Involved in chitinase CTS1 secretion. Dispensable for general endosomal functions but crucial for endosomal recruitment of RRM4. |