Datasets:

Synthyra

/

TremblNLP

like 0

Follow

Synthyra 8

D3PHE0

MRGLATLWKGVSRSFSVSSRLSQPLFFSEKHEWVDYDSGSDVATVGITDYAQAALGDIVYVQLPESDTKIKMGEECGALESVKAASELYSPISGIVVDKNVAVEDAPALINTSPEMDGWLFKLKIDATSTGDVKKLMTQDEYKKFLESQEADH

Cofactor: Binds 1 lipoyl cofactor covalently. Function: The H protein shuttles the methylamine group of glycine from the P protein to the T protein. Subcellular Location: Mitochondrion Sequence Length: 153 Sequence Mass (Da): 16773

K3XJZ1

MTHVISFFSPNPTPTPPPPRVQKQKKKGNRNREPSRKKKARRSPLSHRPRAQIRMTGSMDLPAKGGFSYELCRRNDFLEKKGLKIPGFLKTGTTIVGLVFQDGVVLGADTRATEGPIVADKNCEKIHFMAPNIYCCGAGTAADTEAVTDMVSSQLQLHRYATGRESRVVTALTLLKSHLFKYQGHVSAALVLGGVDCTGPHLHTVYPHGSTDTLPFATMGSGSLAAMSVFESKYKEGLTREEGIQLVTDAIRGGIFNDLGSGSNVDVCVITKGKTEYLRNHELPNPRTYVSSKGYSFTKGQTEVLSTKITQLKQKVEVAEGGDAMEE

Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. EC: 3.4.25.1 Catalytic Activity: Cleavage of peptide bonds with very broad specificity. Sequence Length: 327 Sequence Mass (Da): 35613

R7V5B7

MAAGQAVDYSNINNLKDILSTYNRITESCFSRCAYNFNQRQLTDNENDCVMSCASKFINTNQRMMMTFMDIQMKKNEAQAEEQLKAQQLAQTQAQDSAAVQPTTQIPAAEMAAAAFANIEAAKSADDSSSVTGIGVESAAS

Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Subcellular Location: Mitochondrion inner membrane Sequence Length: 141 Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. Sequence Mass (Da): 15296 Location Topology: Peripheral membrane protein

Q6GM46

MTAKESSNELATPDSDIYIKTFKEHMHLELELPRLSGKRTTTSPKISPRSSPRNSPCFFRKLLVNKSIRQRRRFTVAHTCFDVENGPTPGRSPLDHQASPGSGLVLHTNFTSHNQRRESFLYRSDSDYDLSPKTMSRNSSAASEQHGDDLIVTPFAQVLASLRSVRNNFTVLTNVHGVPNKRSPMTSQPQISRVNHQEDSYQKIAMDTLEELDWCLDQLETIQTYRSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISSTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLKHSSSLNNTSMSRFGVKTDYEDMLSKELEDLNKWGLNIFKVASYSCNRPLTCIMYAIFQERDLLKTFKIPVDTLITYTMTLEDHYHSDVAYHNSLHAADVTQSTHVLLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEEHCDIFQNLTKKQRQSLRKMVIDLVLATDMSKHMSLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWGDLVQPDAQDILDTLEDNRNWYQSMIPQSPSPLLDEHDKDCQGLSEKFHFELTLEEEDSDGHDKDGDCLSFYSSTKTLHIVDQGMEDSPDADTELLTDDTSPLDT

Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. Pathway: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. EC: 3.1.4.- Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP + H(+) Sequence Length: 721 Sequence Mass (Da): 82366

A0A1S3T8Q3

MASKLRTCFVCWNLSGFNCVNLSNGNGRIVRVSFPASCKMRHRTTLSSLQHKRQQIKPSTEVGLRQNKDEEEDSEVSSNNDDSVDNTNETKDSVDNTNETEEPLVININGAELAKQLSGKQREDLLGMIRNAEKNILLLNQARVRALEDLEKILAEKDALQGEINALEARLAETDARIKAAAQEKIRVELLEQQLEKLRNELAEKGGTEARYEELRDLQNGDLRDANPLSNKGIIHSLTEELNSLRTENASMKNDLESFKTHISVVKNDDERLVALEKERSSLESALKDLESKLCSQEDVSKLSILTVECKDLSGKVENLQSLLDKATKQADQAVIVLQQNQDLRRKVDELETSLEEANIHKLSSDQLQKYSELMKQKINVLEERLQKSDEELNSYIQLYQKSVKEFQDTLDTLKEQSKRKALEEPVEDMPWEFWSQLLLLIDGWGIEKKISVDDASLLREKVWRRDRRISETYMAYKKQSEPEAISAFLGLLSSETSQGLHVIHIAAEMAPVAKVGGLGDVVSGLGKALQKKGHLVEIVLPKYDCMEYDRVCNLRALSVEIESYFDHQLYKNKIWVGSIEGLPVYFIEPQHPSKFFWRGKFYGEDDDFRRFSFFSRAALEFLLQAGKKPDIIHCHDWQTAFIAPLYWEIFVHKGLNSARICFTCHNFEYQGTAAASELDSCGLVSQNLNKSDKMQDNSARDRVNSVKGGIVFSNIVTTVSPTYAQEVRTAEGGHGLHSTLSSHSRKFVGILNGIDTDAWNPATDAFLPVQYNATDLQGKVENKQALRRKLGLSSADIRRPLVACITRLVPQKGVHLIRHAIYLTFELGGQFVLLGSSPVPHIQKEFEGIANHFQNHDHVRLILKYDESLSHAIYAASDMFIIPSIFEPCGLTQMISMRYGAIPIVRKTGGLNDSVFDVDDDTIPSQFRNGFTFVNPDEQGLNGALVRALNLFKNNPERWKQLVQKDMNIDFSWETSSAEYEDLYLKSVARAKAAKRA

Pathway: Glycan biosynthesis; starch biosynthesis. EC: 2.4.1.- Subcellular Location: Plastid Sequence Length: 998 Sequence Mass (Da): 112872

T2D2Z1

MENLSTRFDTLQEVLLAHYEKDSKKITDHVSFWELLRRESVMLHYARQQGISSLGFFQVPSLQVSEAKAKKAIMMSLMLQQLAKTPFGQEPWSMTETSLEMLEAPPKGKFKKGPRTVEVWFDNNPDNSFPYTSWTCIYIQDAEDTWHKVEGLVDYEGLYYVDCDGEVHYYVKFAADALQYATTGMWRVNYKNQTISASVSSSSSEDQQRQGQQQQQQQQQPSTTTSVEWPQRPSSSGLQHESPFTPRGHGRGCVRGRRSSGSSPHQRGDRGGRGRSQSPSTPTTPGALPPDLSFAGGDRSGGGGGGGGGGRQRGRRGSRGPPRLSPYIPLGQVEQGPGRPEGAALQRPGRPEKNPRLSSTTPVVVLKGPGNALKCWRLRAKAKHGALFCAISTAFSWVEKSSSSRIGRHRILVGFINEEQREDFLRTVRLPRGVECVPGGLDSL

PTM: Phosphorylated. Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex. Subcellular Location: Host nucleus Sequence Length: 444 Sequence Mass (Da): 49110

A0A6P6XRC5

MMETTKDIDNNNNNKTLMATCQVRPNRHIALLNQQDVNGKIELKQISTNPIPIINMIIKLDGFKVGCDANQNISNCLTKTLNNTDNNQSDDDDDEHVAFGMHIHEGSDLSYDCQSVGNHYNPFNMSHGGPNDTIRHLGDLGNIYADQQGSVYMDQLKFFDLSLDPNHQHYIVNRTIVIHNGRDDYGKNSNPASKTTGNSGVRIACCLITLMEQQQQQTNTTVTTTINPLLSNNNESIIATTITENP

Cofactor: Binds 1 copper ion per subunit. Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. EC: 1.15.1.1 Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2 Sequence Length: 246 Sequence Mass (Da): 27388

A0A1T0A708

MTSPNAAIARRFAKARHTYDAAAHVQKVIVRTLMSYAAPHLPTAAKRTLEIGCGTGELSRALLEKVRIDVLILNDLYPEIRQNPANPHGETQYLIGDIEQLPLPDSLDLVVSSSCLQWLKDLPALLERAHGALQDDGVFVFSSFSTENLHQIKHLTNQGLDYYSLKDYENLLTAAGFQILHLSEQQYELNFDSPKAVLKHLQNTGVTATSADFRWTKSTLTQFMQDYQRKFAWQDDAGKWHYPLTYHAVYGVVGKA

Pathway: Cofactor biosynthesis; biotin biosynthesis. Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. EC: 2.1.1.197 Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine Sequence Length: 256 Sequence Mass (Da): 28814

A0A1U8LQU0

MGSSSGSVHKTEEEWRAILSPEQFRILRQKGTELRGTGEYDKFFQEGVYNCAGCGTPLYKSTTKFNSGCGWPAFYEGFPGAINRTPDPDGRRTEITCAACGGHLGHVFKGEGFSVPTDERHCVNSVSIKFVTADATPSL

Cofactor: Binds 1 zinc ion per subunit. Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer. EC: 1.8.4.12 Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein] Sequence Length: 139 Sequence Mass (Da): 15132

R7UEW0

MSSPVLLAICVALLPLLSAGDSCLSPSVKQKVYTTTDSTASIESVVLAEFSITCKNGLKDLSLYAEFEGKTAPASRIPGTNTYQASFSQDHKSLPSGTYTMRIFDEEGYSALRKSEK

Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 117 Sequence Mass (Da): 12563 Location Topology: Single-pass type I membrane protein

A0A251TP97

MIGIQQLPLTGKHSIPFHTPVSVTRCQYKPIIKPEFITKNKDRFWSSSTGPVRAGWFLGLGEKKKVTDLPEIVQAGDPVLNEPARDVRPDEIGSERVQKIIDDMVKVMRGAPGVGLAAPQIGIPLKIIVLEDTEEYIGYAPKEEIKAQDRRSFDLLVIINPNLQKKGNKSALFFEGCLSVDGYRAMVERFLDVEVTGLDRYGQPIKVSASGWQARILQHECDHLAGTLYVDKMVKRTFRTVENLQLPLANGCPKPGVR

Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide] EC: 3.5.1.88 Subcellular Location: Plastid Sequence Length: 258 Sequence Mass (Da): 28787

R7UTK5

MSDINDKVKASATTLLIENEASLAELDEADIDIAVVDGTFMTDFKYLVPHRLGVPFVSVSDFFDPWHTGVPWLPSFTPYWLLPYSHEMNFLERMKNTALYFYVRLVGISPKVSPEIVAKYSEFGSFSSPGEISAKSKLWILTSDPVLDYPKPMMPNMIEAGGISTKPAKPLDPMWTEMFQRSAGDIVLVSFGSVVSSFPEETATKLLTAFGQLKQTVIFRFKNKDELTIPANVVISDWLPQNDLLANPNIKVFVTHCGNSGQFEAVYHGVPMIAMPIFGDQFYNAQRVHYRGYGIFVDTFNFQPDDLVSAINRVSHDPSYKQKIVKASEIFRDRPETPVQRAVSGIEHILKHGGDHLQSHSSKMPLHQFLLLDVLAAALLCFVVGALVSCRIIKCAFGVFFSRLDHNKSKTQ

Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP EC: 2.4.1.17 Subcellular Location: Membrane Sequence Length: 412 Sequence Mass (Da): 46150 Location Topology: Single-pass membrane protein

A0A842X636

MKRTVDSIRGMKAGGERIAVITGYDSRDRELLDSAGVDVILVGDSIGNVRLGYPDTTHVTLEDMMKAAADVTSEKANALVVVDMPIHTYDTFEDAVKNAKRLVDAGGEAVKLEGGSEVADMVKAIVDSGVDVMGHIAHTPQTEKKHRIKGRDEEDAGKLIGDARALEEAGAFAIVIELADPEVAGRVTESVGVPTIGIGAGPRTDGQVLVLDDLVGWTDFSRFPGGRKPRFIGEWDTSSPEKAVGDFINKVKERAFPSEMECYSVYKG

Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Cofactor biosynthesis; coenzyme A biosynthesis. Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. EC: 2.1.2.11 Subcellular Location: Cytoplasm Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate Sequence Length: 268 Sequence Mass (Da): 28717

A0A0J8FEY6

MLKNSKSKLLEGWDYAPNVVTYIRIILSILFIILYLVAGPWGYTSTAIRWSVFVLFVIAASTDKLDGWMARKYNQVTELGKLLDPIADKLLMLSALIIASAFGELYWWITALFVIREIGITILRFYVINKGGKVIAASSAGKFKTLSQSIGIAMLLVPIVPIFCANDIPLWVICYYSIAYGLIGIAIGFATYSGILYVNDALKH

Pathway: Lipid metabolism; phospholipid metabolism. Subcellular Location: Membrane Sequence Length: 204 Sequence Mass (Da): 22655 Location Topology: Multi-pass membrane protein

H9A9I9

MKSMMIISFLFIMISILILMLNLLFSKKSSKDREKMTPFECGFDPLTNSRLPFSIQFFLISLMFLIFDIEIILLLPMIFFMKMKINLNIILMFITFLSILILSTYLEWLESNLNWVI

Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.2 Subcellular Location: Mitochondrion membrane Sequence Length: 117 Sequence Mass (Da): 13920 Location Topology: Multi-pass membrane protein

A0A7R9G9U8

MDIAKKRNVGGNTCVPFLCSMLGSAFWFKYATLIGYNPTMIIVNTMAIVMNSGYLWIYYLFCGRKPLVHRYLMAILALIATTYWYVDYVLEDREDARCKLGLIACCISVLFTASPLVLIGHVIETRSTEALPLLLIASTFLVSVLWLLYGMVLGDTFVTESPTGSFIALQVQNGISVVFGLVQLALFAIYPRRRGSPASPETIRDGEDARRDLTSTTRLQQSGRKVLDSVLRERVAVVDPLQLGRTGRK

Function: Mediates sugar transport across membranes. Subcellular Location: Golgi apparatus membrane Sequence Length: 249 Sequence Mass (Da): 27729 Location Topology: Multi-pass membrane protein

R7UVQ7

MDILNPFGQQASGNKTYDFDDYFDYKDFSEPEIDEQHSLAVIVPFRNAHAELGRFLSHMHTFLRAQNISHVFYIVEQDDSLRFNRGSLINVGFLEAQRDRQSDYFVMHDIDILPLNPRLSYRFDGCAKGPLHLASPSLHPHYSKIDFIGAVLLMTNEQYLKVNGMSNVFWGWGREDEELRIRLRIAGIKIFRPSGVNSTKADSFLHIHNEATRKRDRLIIGDQYKARYRLDTVTGLNTTKYKLLEKVTKELNGVPYAHVRVQLDCNHRATPWCQRQ

Pathway: Protein modification; protein glycosylation. Subcellular Location: Membrane Sequence Length: 276 Sequence Mass (Da): 32103 Location Topology: Single-pass type II membrane protein

R7TEX7

MSLIPRDFSDRIAFFVMLGAIHLITFFELLVILPYIDQDRTKTYWLHFTIGMCFYFDIMSNIGFILTIDTTSGSVIMPSVLKLGWRFCSTCEANAPPRSHHCWMCNKCILKRDHHCTFTGNCIGFSNQRYFLTFILHLTCAAIYCNYLNMDYTWEVLGGFNFKSVITMFVPLVAWMFGFAATYGFFVAFVSALCVIGCLLLSTFSVYHVNNLVHGQTTSEKTHKVHDYDLGLVGNIREVFGVKWYVAWVSPWISSPLPGDGVSFLTKQQHDREGHVIICPMKTAFDPQQNLF

Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 292 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 33429 Location Topology: Multi-pass membrane protein

A0A2D9HD13

MYQFEIEKADEGQRLDRYLALAVPALSRSAIQRLIRDGDVSVDGELTAPKHRVQTGERVSLRIPPPRAAAPEAQPMDLDFLYRDEHFVVINKPAGMTVHPAPGQADQTLVNGLLYEGVGLSGIGGVQRPGIVHRLDRETSGVMVVASHDEAHRKLSKAFAQREVKKTYLCVTAGKPRKPEGLIDTPYGRDPKHRLRFSGKVRSDRRARTRYRVLETMGPCALLEIDLLTGRTHQIRVHLSEAGTPLVGDELYGGGKRWKGVSWPPAKEAMRAMTRQALHAHRLAFQHPMTEQAMDFESPLPADFERLLEGLRSG

Function: Responsible for synthesis of pseudouridine from uracil. EC: 5.4.99.- Catalytic Activity: a uridine in RNA = a pseudouridine in RNA Sequence Length: 314 Sequence Mass (Da): 34996

A0A5E7HWA6

MAISELKLPQGVSAHEFKSPVLLAEGLALKVARQLSDAIDARGTATLVVSGGRSPVAFFQHLAKQTLDWSNVVVTLADERWVPVEHADSNAGLLKRYLLQGPAAKAQFLSLYSATANLEQAAEQADRLLGELPPIDVLILGMGDDGHTASLFPNSPNLADALKVDGSRRCWPMLAPTVPHQRLTMSRALLASATNTVLSISGQSKLTTLSAALAGDDVAAMPIRAFLQPTLEIYWCP

Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. EC: 3.1.1.31 Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Sequence Length: 237 Sequence Mass (Da): 25272

A0A423LWQ7

MKSQRPVNLDLRTIKLPVTAYTSILHRISGVILFVCLAIMLYALDKSLSSEEGFGQVKACLTSPLAKLVIWGILSALLYHLVAGVRHLIMDMGIGETLEGGKLGSKIVIAVSVVVIVLAGVWIW

Cofactor: The heme is bound between the two transmembrane subunits. Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH). Subcellular Location: Membrane Sequence Length: 124 Sequence Mass (Da): 13413 Location Topology: Multi-pass membrane protein

A0A414NGE2

MSRKITKRQQQIYDFIRSYQKEKGYPPSVREMAAAVGLSSPSTVHAHLSALEEHGLIRRDATKPRALEVFNSDGSSYKPEESTASSARGTVKLPLVGRVAAGMPILAEQNIEDSFTVPTEIATDSSSFVLEVHGDSMINAGIFNGDYIIVREQKSAMNGEIVVAMIDGSATVKTFYKERGRVRLQPENDAMEPIYADNPTILGKVVALMRRF

Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. EC: 3.4.21.88 Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA. Sequence Length: 212 Sequence Mass (Da): 23337

A0A2E4X2A9

MLTLKPLSYLRRRKLLKALRTVVKTASKLLSKSLDVKAAHQTELQAAKTHGQSLLEKGETDLDALESAADRLTAAIYDSSFSRHVLPLGLKSFLELLVLLLAALTIRAFLYEPFKIPTGSMKPTLLHGDHVFIRKFHYGPRWPFTTDRIWQGQAPARGDIAVFNFPLDPSVDYIKRIVAVEGDRVKVVDGHLFVNGQPQSRRSLGKHTFLATDERTLQGSPRQADLYQEQSGEAAHYSLLGPQGEAFYNQWPEYYFQQPQKELGALFSDRSRGLACRSDSCEVLPGFVFTMGDNRDGSSDSRLWGGVPVEYLRGKATLIWFSHDWTEPVLPLGPLTIGRLRWKRMFRYVDDLGSDLSAPSERL

Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins. EC: 3.4.21.89 Subcellular Location: Membrane Sequence Length: 363 Sequence Mass (Da): 40932 Location Topology: Single-pass type II membrane protein

A0A397EZF7

MVGWEWGHLIVSVTRTIWSVDSLGSGARDAGYPSVAHGMFPRGPIELVEYFMDDLQHKVQDKLAAETIDLPVTDRLKRGIRFRLELLAPYISVWPQAMALGALPQNAPTTVKKLAEMVDDIWVYAGDRSTDVSWYTKRAVLTGVYTATELFMLTDQSPNHEDTWRFLDRRIEEAIALGDIPNNAQDVAGMLSIGIQSLLSTAAALAGPLTTQVVQQVGQHVPNPLTAFPSTAFPFQTPSSSTPVAPTAAPVDTPASTSETPTSAPLDTTPPKPPQL

Pathway: Cofactor biosynthesis; ubiquinone biosynthesis. Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Subcellular Location: Mitochondrion Sequence Length: 276 Sequence Mass (Da): 29946

A0A7C7G4J6

MTDAQPVTGVILAGGRGQRMGGVDKGLVEYKGTPLIEHVIAVLSPQVDELLINANRNIKIYEQYGYPIIADELPEYPGPLAGMLTCLGNATHDHVVFVPCDTPALPDDLVERLLHDMEQSGNRACFAHDGERAQPVIAMLRSSVQIPLAQYMACGQSKVMDWMQQIAATPVDFCDSRTAFANVNSPDDLQ

Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide EC: 2.7.7.77 Subcellular Location: Cytoplasm Sequence Length: 190 Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein. Sequence Mass (Da): 20678

A0A1U8JYU3

MHSNKPLFNSRKCRLWIQHQEGRHLANLNLDEVYFQRTTSIPPASNSRLSSLPPKPTGFSYEREATINIPLDIASRGSRNQDLKKKEKELQSKEADLRRREQEVRRKEEAVARAGVVLEEKNWPPFFLSFIMILLMKF

Function: Probably involved in membrane trafficking. Subcellular Location: Cytoplasmic vesicle Sequence Length: 138 Sequence Mass (Da): 16178 Location Topology: Multi-pass membrane protein

D0QKR3

AFPRMNNMSFWLLPPSLMLLLSSNFLNPSPGTGWTVYPPLSSYLFHSSPSVDLAIFSLHISGLSSIMGSLNFIVTIIMMKNISLKHIQLPLFPWSVFITTILLLFSLPVLAGAITMLLFDRNFNTSFFDPTGGGDPILYQHL

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 142 Sequence Mass (Da): 15794 Location Topology: Multi-pass membrane protein

A0A922L1U3

MNSNEHQSNSSQQTKKFKHQPCSGVFRSEEMLLCQLFLRSNVSFETTCRLGELGIVEFRDLNADLNAYQRKYVDEIKHIGEVQRKLIYLSQQLQKSDLPIVKPIGDPAIPKYKEIIALENQIEKLDNDLREINEHLYTLRLERSELVEMSMILAKTNQLLETTRRQQRASFNGQYPITDSGNQNQALDLDPEQSSIGVPKQPQKQGFECNKIYTITGLLRAEKALAFRKVIWRVCGQNALVQFFDIDNPIDDAKAEEFVQKKVFLVMCQGDKLYGKIEKICNGFHASKYPLPDDEDHYRLLCLKVEQDLKDIQLVIEKTSQQHLKILTAVAQPKNFPTWMVQVTKLRAIFTTMNLYQKTEKGFLAEGWCARSDYYLLNGIIQEINDRAGILGQAVVEKVSTTSTPPTYFRLNRFTQGFQNIVDSYGMATYREMNPAPYTIITFPFLFAMMFADAGHGLIMMLFGLWMVLYERKLNGKSNNEIWLTFFDGRYIILLMGAFSIYTGSIYNDIFAKGYNLFGTCFDSHATEIKLYDDLIIANNGSHNSNDTVFNKKLEIYIPKGDRSYPYGIDPAWQISSNKIIFLNSFKMKLSVIVGVLQMLFGVMISLCNHINAKSWTSIVFEFIPQLIFLLSLFGYMIILIFVKWLRTWSPPSNAPSILIDFINMFLMKYPNENEPQTIYLNPWYPHKQEIQTILLILALLQVPIMLLVKPIIKVFFSNRQKRQPANIEESTSNNQQQQQQQGDSNNHEESTGDIFTHQAIHTIEYCLGSISHTASYLRLWALSLAHSQLSEVLWQRVMHAGFATENSNLIIRVIMTYLTFGLWAVLTIAILIVMEGLSAFLHALRLHWVEFQSKFYTGAGYAFRPFYLKRILTETNILIE

Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase. Subcellular Location: Membrane Sequence Length: 881 Sequence Mass (Da): 101561 Location Topology: Multi-pass membrane protein

R7V7X5

RLGNYLVILFMVSKVFYIANAIGQLFVLSEILSISYSNYGFDVMSGMVADHDWTESAHVAFPRVTFCDFDVRRLGNVHRYTVQCVLPLNLYNEKIYMFIWFWLIFVAAVSMLSFFVWLIRFLFRSDRRMFINNHLKMGDKVFDKNDKKLCNKFLNNYLKQDGAFLLRLIAHNTNSITTTEVTCAMWDLW

Function: Structural component of the gap junctions. Subcellular Location: Cell membrane Sequence Length: 189 Sequence Mass (Da): 22321 Location Topology: Multi-pass membrane protein

K3YV05

MEMASHTVLSLLLLLPFLFAAAADVAPGPSPPGELNLTGILENGGQYSTLLRLLQTTRIAQQLTEQLKNSYDGLTFFAPNDDAFTKLKTGTLNGLSDQQKIQLLLYHVLPRYYSVTTFQTASNPLPTEGSGPGGMYTVNVTTTTSSHLVNMSTGVVDVPISSTLVARFPLAVYSIDAVLLPEQLFGASRKAVAPAPAGQAAGAAAGKAAARKKGGVPKSDVAAEPSAAGKETEDSTKAAAACRGMSAGWTTIAAFALMAVVNLVGA

Function: May be a cell surface adhesion protein. Subcellular Location: Cell membrane Sequence Length: 266 Sequence Mass (Da): 27482 Location Topology: Lipid-anchor

W4HCH6

MGQPDNASSSPTTPPSGDIAPILVIGAGPHALALVLALLEEDASSEFTERDTIHMGFWRQKLGRKKNQKGPRNQSKNLPTSSSSSSSCLRRQIRVLDPSGTWCSTWNGNFATFGISHLRSPVNVHLDPLRPEGLRDYATSTNQLKSQVSEPPPSIRFSRRNRAFTTNTSMFSENDRQFLGCPSRELFAEFQEHLIHQYGIASMVEKAAAVAIEPLDTSSSPLFKVTCAGGNVIVAKHVVVAIGTQNIPRIPAWATPLWQQTPTNLIVHSSDAALHAVAYAKRMRHKRVLIVGGGLTSVHLAREVVSTWGAKHVTLVTRKPTLLVQPYDVPLEWISPLLRAKMLADFFDEDTLELKVQRIRDARRGGSVTRSALAQLHAVATPHNYHHRGNTVVTNVERIGACDDTQLRVTLSDGSSADEIVVDHIILATGSDIDVTKERLFDGMRHLGAPPVGGLPALDDELRWESDLNLFVMGGYAALQLGPTAGNLMGARSGANKLAELILEGVATKAAKTRHHHLRALCGKENLYDFLT

Pathway: Siderophore biosynthesis. EC: 1.14.13.196 Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+) Sequence Length: 532 Sequence Mass (Da): 58086

A0A7R9BN75

MLVKHSRRFLKRSLDHVLRIGWRLETTRRPVTGDTVEYLRLVTLDPDGVTNDYSVFYSESYSVPVLYLSRYSDSGELVAPSGCEDCLTPTDHPISGAPVLFFHPCRTSEWAVLTPKSDAGLKYIPSWMSWPFARFLGIQEPASTLFSMLNGIAHVFGLSALLRQVKSEAPFRGWWIANGLIMILCWVFSTIFHTRDTPFTEKLDYAGGMIANVAALTAVTVRLVGIERLTRTGTMIMLGAGCSFVYRHLKFLFGVSFDYGYNMKVHLAIGGFHVIGWLCWAFLNRSTCPYAWKGAAVNFLMAATMALELLDFPPFLWTLDAHALWHLSTIPLIPLWYS

Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Subcellular Location: Golgi apparatus membrane Sequence Length: 338 Sequence Mass (Da): 38122 Location Topology: Multi-pass membrane protein

K4B3F9

MEEDKQNQVARIQDFDPPKKPKTNKYAIACTFLASLSSILLGYDIGVMSGAILYIKKDLHITDVQVEILVGILNVYSLFGSAAAGRTSDWIGRRYTMVVAAGIFFAGALLMGFATTYAFLMFGRFVAGVGVGYALMVAPVYTAEVSPASSRGFLTSFPEVFINFGILMGYVSNVVFSKLSTHLSWRFMLGIGAIPSVFLAVSVLAMPESPRWLVMQGRLGDARRVLNKTSDSLQEAQFRLADIKQAAGIPENCNDDIVEVPKRPTGDNVWKELVFSPTPAVRHILITGVGIHFFQQASGIDAVVLYSPKIFEKAGIKSDHDKLLCTVAVGVVKTLFILVATFMLDRSGRRRLLLTSVGGMVASLVLLATGLTIIEHSEQKLIWAIALCIAMVLAYVALFSIGMGPITWVYSSEIFPLRLRATGCSIGVAVNRVTSGVVSMTFLSLEKAITIGAAFFLYAALAAVALVFFYTLMPETQGKTLEEMETLFGTFWNWRARARELKELKKTEKNSNDNGHIPMGTSNALAMQNVMMVTTQTNIVV

Catalytic Activity: NH4(+)(in) = NH4(+)(out) Subcellular Location: Membrane Sequence Length: 541 Sequence Mass (Da): 59047 Location Topology: Multi-pass membrane protein

A0A174LBR9

MQCFQGKSVYKGIAMGPIVVLKKNDYQVKRTRIEDTEAEVKRVDEALKASQEQLQKLYDKAVREVGEASAAIFEVHQMMLEDEDYLEAIQNMIRTEQVNAEYAVAVTGDNFAEMFASMDDDYMKARSADIKDISERLVRNLSGQGDVDLSEIEPSVIVADDLSPSETVQMDKDKILAFVTVHGSTNSHTAILARMMNIPALIGVKMDLEALQSGVTAVVDGFQGMVTFDPDEETKAQTETKIQEEAEKLKLLQELKGKENITLDGRKINIYANIGSVGDIGYVMENDAGGIGLFRSEFLYLGRNDFPTEEEQFQAYKQAVQMMAGKKVIIRTLDIGADKQVDYFNLGNEDNPAMGYRAIRICLRQPEIFKTQLRALLRAAVYGNLSIMYPMITSTEEVKKIYEIVAEVEEELKAQEIQYKIPEQGIMIETPAAAIISDKLAEMVDFFSIGTNDLTQYTLAIDRQNEKLDEFYNPHHEAILRMIQMVVDNAHKCGKWAGICGELGADATLTEQFVRMGLDELSVAPSMVLKLRKIVREMKVEE

Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate EC: 2.7.3.9 Subcellular Location: Cytoplasm Sequence Length: 542 Sequence Mass (Da): 60851

A0A1S3VUZ2

MAVATRGTRGGSTFRGLFSFRIFISAMFSLLFIATLSVLFTNNPSTSQDVSDLPTTGNAYVHRTFLALKSDPLRTRVDLIHQQAKDHIALVNAYGAYARKLKLDISKQLKTFDELAHNFSDIAMKPVYQKSLFETDGPIDEDALKQFEKEVKERVKIARMIIVEAKENYDNQLKIQKLKDTIFAVHESLAKAKKNGAMASLISARSIPKSLHCLAMRLMGEKISNPEKYRDEGPKPEFEDPTLYHYVIFSDNVIAVSVVVRSVVKNAMEPWKHVFHVVANRMNVGAMKVWFKMRPIEGGAFLEVKAVEEFAFLNSSYVPILRQLESAKMNQPENATNDSNMKNAKSLSMMDHLRFYLPEMYPKLYKILLLDEDVVVQKDLTGLWNIDMEGKVNGAVEICFGSFHRYAHYMNFSHPLIKEKFNPKACAWAYGMNIFNLDAWRREKCTDTYQYWQNLNEDQSLWKAGILPPGLITFYSTTKSLDKSWHVLGLGYNPSISMDEINKAAVIHYNGNMKPWLDIALNQYKNLWTKYVDNDMEFVQMCNFGL

Pathway: Glycan metabolism; pectin biosynthesis. EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 546 Sequence Mass (Da): 62556 Location Topology: Single-pass type II membrane protein

A0A7J4M0K6

MKIKVLKDESKELTIEFETKDTTIPDLIVSELLDNDDVDFAGVAKDHPETGNAVLTLKSKKKAKDVLLKAIESLDEQFASLKTQVSKKGK

Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) EC: 2.7.7.6 Subcellular Location: Cytoplasm Sequence Length: 90 Sequence Mass (Da): 9973

A8IXB2

MPLAKLRNVVLEYAAIAIYVSAIYTSVVLLPSALALFYLFGATSPSAWLLLAAFLALTFTPLQLTTGALSERFVQFSVARAAAYFPTRVVVTDPEAFRTDRGYLFGFCPHSALPIALPIAFATTSPLLPKELRGRTHGLASSVCFSAPIVRQLYWWLGVRPATRQSISGLLRARKVAVLVPGGVQEVLNMEHGKEVAYLSSRTGFVRLAVQHGAPLVPVWAFGQTRAYSWFRPGPPLVPTWLVERISRAAGAVPIGMFGQYGTPMPHREPLTIVVGRPIPVPELAPGQLEPEPEVLAALLKRFTDDLQALYDKHKAQFGKGEELVIM

EC: 2.3.1.- Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 327 Sequence Mass (Da): 35730 Location Topology: Multi-pass membrane protein

A0A838H6F6

MAKNLVIVESPTKAKTLERYLGSDFRVLASYGHVRDLPRSDFAIEVAGGDGVSLRYEIPKSSSKHVNAIRKEARGADRVFLATDLDREGEAIAWHVAEVAGIDTDDENRVVFAEITRDAILSAFERPRRIDAHLVDAQQARRAVDRIVGYRLSPTLWRNVASGISAGRVQSVALRLICDREDEIRRFVAQDYWSLHGNFARDGASVATQLHTVDGARVTDPKKLQEQAGKGREGRYLVIADAQSAEALAERSRAVRRWTVTDVKRREAKRNPQPPFTTSTLQQEAERKLGFSPSRTMRLAQQLYEGINVGDETVGLITYMRTDSLNISDTALGEIAELVRGDFGARYALDKPRRYKGKAKGAQEAHEAIRPTSVARRPEALARRLDADQRALYDLIYKRTVASQMAPAVFDTLRADIVGGEGGDEPEGGDQPGDGRRSRRPEGGDQAELRYRASGQVLRFDGYLAVYEEGRDEDDADEQTAVGDRLPDLEDGQLLTLTSVRGEQHTTSPPPRYTGASLVKVLESEGIGRPSTYASIIGVLLNREYVRTESRRFFPTPLGEVVVAYLKQHFAEVVDVSFTARMEDELDEIAEGHETWGKLVADFLGEVDDWIAERKPERPRIPIEDATCPECGEAMEKVFSGKSRQWFASCHRWPDCKGTLPLDTYGNVTTVEQLRPDPDVECPECGKPMIRRDGRFGPFYGCQDYPACKGIVNVEQRIGFACPTCGKGHMTQRMSRYGKPFYGCNRYPECDFAMWTQPLARPCPSCGGPLKPPRRNAKNPVAVCANCEQRVPVEADPPRAEPEEFVPARARVTSGQ

Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. EC: 5.6.2.1 Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. Sequence Length: 816 Sequence Mass (Da): 90861

Q5FWL1

MESREAYFNILLATDSYKVTHYKQYPPNTSRVYSYFECREKKTKNSRIRKVKYEETVFYGLQYILKKYLEGKVVTKQKIQEAKEVYREHFQDDVFNETGWNYILEKYDGHLPIEIKAVPEGSVIPRGNVLFTVENTDPECYWLTNWIETILVQTWYPITVATNSREQKKILAKYLFETSGSLTGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGIALIKRYYGTKDPVPGFSIPAAEHSTITAWGKDHERDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRSLIESRSDKAPLIIRPDSGNPLDTVIKVLEILEKKFPVEENSRGYKVLPPYIRVIQGDGVDINTLQEIVEGMKQHKWSIENISFGSGGALLQKLTRDLLNCSFKCSYVVTNGLGVNVFKDPVADPNKRSKKGRLSLHSTRKKEYVTLEEGKGDLEEYGPDLLRTVFQNGKIISCYSFDDVRRNAGLINTELEEEIQ

Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide: step 1/1. Catalytic Activity: beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + H(+) + nicotinamide EC: 2.4.2.12 Subcellular Location: Nucleus Sequence Length: 491 Sequence Mass (Da): 56041

R7TEH1

MKCFNWLFFVCFSLTEGHASRLEAYKHECEYYDPVKCKSEPEACNKTVEQCPDPDPSARSHCYASWKNDTGKFELVKKGCWLDQPECYDKFECVEERLEEGKPYFCCCEGHMCNANFTVSPNAKKPTTTPSTGHSHQAMLFSLLPIIGIAIVIIIVFYLWKLNHRQDPYHTQLPTHDPSPMTPPSPDLGQRPINLLEVKARGRFGCVYKAQMGERVIAVKVFPLQDKQSWATEKDIYSLPQLNCHANILHYIGAEKRGENLNMDLWLITQFHEQGSLYDYLKGNLVSWQQLLAICESMAKGLAYLHEDLPATRTQQAKPAIAHRDFKSKNVLIKSDLTACIADFGLALKFEGGVSVGETHGQVGTRRYMAPEVLEGAINFSRDSFLRIDMYACGLVLWELISRCSAADGPVEEYRLPLEEDVGTHPSLEEMQDAVVSKKSRPGFKDVWRKHPGLCTMCDTIEECWDHDPEARLSAGCVQERLSQLTLLQNTAGLPQPPCKQLPSYSLQPPRYSVSQRTQSSPPPSYSDGYQIPIV

Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein] EC: 2.7.11.30 Subcellular Location: Membrane Sequence Length: 535 Sequence Mass (Da): 60454 Location Topology: Single-pass type I membrane protein

R7UJA8

MAVEHMRLSSGIDMPILGLGTWKSKPGEVENAVKAAIDAGYRHLDCAWIYGNEQEVGAALKSKIDEGVVKREDLFITSKIWNTKHRFEDALTNIKQSLSNLGISYLDLSLIHWPTSMKHDGNCDKFPRDDQGNVQHTNVSYLETWKALEKAMDDGLVKAIGLSNFNSRQIGEIISNARIQPSVLQVEIHPYFTQEKLVHFCKERNIVVTAYSPLGSPDRPWAAPGEPLLLEDPKLIEIAKKYSKSPAQVIIRWLMQRGIAVIPKSVTPSRIIENFNVRDFKLTADDMNVVSGFNRNHRLVCPSITVNGVRQFRDRAAPNFPFNDEF

Catalytic Activity: a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH EC: 1.1.1.2 Subcellular Location: Apical cell membrane Sequence Length: 326 Sequence Mass (Da): 36796

A0A1I2JDI3

MKDNKLKKILIIIVIVLVVGAVGFKFYYNRLVNHPFKLTVDSVELEVKEGQSLNDVLKKLSKQNIIGNTYLIKYYVKSNDLDTNIKKGRYLIEKNMTLDTFLSNLSLGKVTAGLNKVTIPEGYNIEEIAASLEKSQVISKEEFLKAVKEYNAPSYIKKNSERKYQLEGFLFPDTYEFEKDISGEEIIERMLLRFEEVISEIEQATGKKIDKNNLDDIVTMASIVEKEAERDDERGKVASVFYNRIEQHTKFQSCATVLYALGYHKAEVSNEDIKVNSPYNTYKVDGLPIGPIACPGKASLNAAINPEKTNYLFFISNDDGTHTFTDNDKEFMRLKEIRDNKNKK

Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. EC: 4.2.2.- Subcellular Location: Cell membrane Sequence Length: 344 Sequence Mass (Da): 39320 Location Topology: Single-pass membrane protein

A0A3B8T2P7

MHVEHAIVGAGLIGGYLAAHLADVTLQLQSDARLLVVGRDYAKCQFGPRMTISDFATPVQTRDTQNIEFVTNTSSWASTKRYPNVVWLTIKCTGIKQVVPDIRPLIGPQTIVVCCQNGIGSDAVIRQAFPDNPVIRCMFPFNVVKLNKGHFHRGSSGTVMLERLPLGQYPVFDDFHQRFSPVIDALNEQYGEVFPCAWCSNMDALLWAKCQVNLTNSVNALSNLSLKETLLDKGYRKIIALMMQEHLAVCAAQGIALPKITKVAAKFIPTVLRLPNWLFSRVAKSMVDIDPHAKLSMWWDLDQGRATEIDFINGATMIAGQRLGIDTPMNNIVYAAIKKMEKAPTRYALSAQDLLK

Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2. EC: 1.1.1.169 Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH Sequence Length: 356 Sequence Mass (Da): 39530

A0A378YUR7

MIVVVMGVSGSGKSTVGQRLADRLGCGFSDADSFHSPANIEKMRRGEALNDNDRAPWLAAIREAIVARRLAGRHHVFACSALRSRYRDVLGEHDGDVVFVYLKGAPEVIGERLASRSGHFFDPALLQSQFDTLEEPRDALIIDIRESPDAIVETLLHKLAACPGGAPLMSAGAARVQ

Pathway: Carbohydrate acid metabolism. EC: 2.7.1.12 Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+) Sequence Length: 177 Sequence Mass (Da): 19118

R7UWP5

MSAAARITSYCANHSRFARFFATNAKQKPIKVGDPLPNVRLYEGTPDQTVMTHDIFRGKKGVLFAVPGAFIPGCSRSHIPEYLGHCESYRKEGYEEVVCLSVNDPFVMDAWGHFVKSSDRIRMLSDMKCEFTNATNMQLDSASLLGNIRSRRYFLLINDNVVEYVSHEPEDTGLSCLLCIKRMKPKDMDEINQSMDKKDSS

Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. EC: 1.11.1.24 Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O Sequence Length: 201 Sequence Mass (Da): 22758

A0A7R9BHN3

MRIVPASVDFNEKDSTTFRNYGTGDTPSEIRVRETYEKLHTYQTVDFVKGRIAKWGKFDHFKASVMDTLERLSTFLDETDPDMDLPNIIHAFQTAERIREKHPDMDWFHLTGLIHDLEIAKWGKFDHFKASVMDTLERLSTFLDETDPDMDLPNIIHAFQTAERIREKHPDMDWFHLTGLIHDLGKIMAFYGEPQWAVAGDTHPVGCEFAKSIVYRERTFDANPDLHDSRYNSKYGVYQPNCGLRNVTMTWGHDEYMFRILEHNKCSLPPEALFHSFYPWHTGGDYMHLCDEYDLKMLPMVQAFQ

Cofactor: Binds 2 iron ions per subunit. Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1. Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O EC: 1.13.99.1 Subcellular Location: Cytoplasm Sequence Length: 305 Sequence Mass (Da): 35780

K3Z4A4

MAALEAARAWAASVIPPELAAAAGGDPLAALAATAAALVAGLLILAVWFRSGNGAPAKPAPTPVRPPPVKIDADADVDDGRKRVTIFFGTQTGTAEGFAKSMAEEARARYEKAVFKVVDLDDYAQEDEEYEEKLKKETVVLFFLATYGDGEPTDNAARFYKWFTEGKEKEVWLKDLKFGVFGLGNRQYEHFNKVAKVVDELLQEQGGKRLVPVGLGDDDQCIEDDFTAWKELVWPELDQLLRDEDDTTGASTPYTAAIPEYRVVFIDRSDLSFQDRSWTLANGTGVIDIHHPCRSNVAVRKELHKPASDRSCIHLEFDISGTGVVYETGDHVGVYSENSVETVEEAEKLLDLSPDTVFTIHADAEDGSPRRGGGSLAPPFPSPCTLRTALLRYADLLNPPKKAALLALASHASDPAEAERLRFLASPAGKDEYSQWITASQRSLLEVMAAFPSAKPPLGVFFAAIAPRLQPRYYSISSSPKMAPSRIHVTCALVYGPSPTGRIHQGVCSTWMKNTIPLEYSEECSWAPIFVRQSNFKLPADPSTPIIMIGPGTGLAPFRGFLQERLALKQSGVELGTSILFFGCRNCNVDYIYEDELQNFLQEGALSELIVAFSREGPTKEYVQHKMVEKATEIWNIISQGGYLYVCGDAKGMARDVHRVLHTIVQEQGSLDSSKTESYVKSLQMEGRYLRDVW

Cofactor: Binds 1 FAD per monomer. Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. EC: 1.6.2.4 Catalytic Activity: NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450] Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 694 Sequence Mass (Da): 76358 Location Topology: Single-pass membrane protein

A0A0U2VZT1

MGTVLDSSLIEGELVLDLKNVSKDMIEVVGGKAANLGELLSLGIRVPPGFVITSNAFRYFLKYNGLYDVIKNIFENDKDEKKVSEKVKSLILNAEIPPDLKKAISDAYEQLEKISNKEVLVAVRSSATVEDIEEASFAGQQDTFLNVSKNDLFSYIKKVWASLHNERAISYRNAKGIDHLSAHMAVVVQKMVNAKAAGVMFTLHPSTGDTNYVIIESNWGLGESVVGGKVTPDEIVIDKSTLKIVQKRISHKTIKVTYDKQMKKNVELKLDENEANSISITEEEAKELAKLALKVEQHYERPMDIEWAIDSDIKFPENIFLLQARPETYWSSKQVKPKEEVLVKASVGKILTKGLPASPGIAYGKARVILDIKDAGSFNQGEILVTRMTDPDWVPLMKIASGIVTDEGGMTSHAAIVSRELGIPAVVGTGNATNSIKDGQQITIDAFRGIVYEGKIEFEEEVKEKQTVSGISGISKETILSLYPVTATKIYMNLGQPDVINKYLDLPFDGIGLMRIEFIVSEWIKYHPLYLIKNGKPEVFVDKLAEGISIVASAIYPRPVVVRFSDFKTNEYKRLYGGDEFEPDERNPMLGWRGVSRYISKQYEPAFRLEVKAIRKVREEMGLKNVWVMFPFVRTSWELKKAIEIMEDEGLRRNQEFKVWIMAEVPSVVILADEFSKIVDGYSIGSNDLAQLTLGVDRDSDLLARMGYYDERDPAVLKGIKTLISVAHKYGKTVSICGQAPSVYPEVVEFLVRAGIDSISVNPDAVISVRRQVASVEQKILLEGLSKNKRKS

Pathway: Carbohydrate biosynthesis; gluconeogenesis. Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. EC: 2.7.9.2 Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate Sequence Length: 792 Sequence Mass (Da): 88390

A0A8J8BQ57

MNDQELMEAARKAAETSYSPYSRVQVGAALTTKNNQVFIGCNIENASYSLSMCAERVAIFTAVLHGMKPGELSKIAVAGKTVGDQWQSCPPCGACRQVILEFAESNKTPVIYQVREQVKSVPIGELLRDGFTIPSPTYL

Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. EC: 3.5.4.5 Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine Sequence Length: 139 Sequence Mass (Da): 15132

A8J1T4

MVQALCSAGAARRGGRQAYSFLASLLSQQRGFAAAAEKDVVVVGGGPGGYVAAIKAAQLGLSVACVEGRGALGGTCLNVGCIPSKALLNSSHMYMEAKQHFGSYGIKMDGLSYDFAAVQAQKDGVVSGLTKGIEGLFKKNKVEYVKGWGKLVSPHEVEVAAADGSSSRLRAKNILLATGSEVTPLPGVPIDEEKIVSSTGALALKSVPGEMVVIGGGYIGLEMGSVYQRLGAKVTVVEFLDNIVPSMDAEVRRSFMRTLEKQGLKFKMGTKVTKGEVVGGRVHLTLEPAKGGAAEKMECDVCLVSIGRRPYSKGLGLEAVGVNTDNRGRVIVDAHFRTNVPSVYAIGDLVPGPMLAHKAEEDGVAAVEIMAGKHGHVNYATVPSICYTHPEVASVGLTEEEAKAKGHEVKTGKFSFMANSRARAVGDTDGMVKIVADKKSDKLLGMTIMGPNAGEMIHEGVLALEYGASSEDIARTCHGHPTLSEAVKEAALATAFGKPIHM

Cofactor: Binds 1 FAD per subunit. EC: 1.8.1.4 Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH Sequence Length: 502 Sequence Mass (Da): 52483

A0A396ZT60

MGQLTWTIVTLCLIVFQMRFVLDSICKGLVWLFFPASLVVCNDCFAYFCGKLVGRRVFTTPFLKLSPNKTWEGFLGAFVCTLVFAFWSSALLAQSPWMICPLESIEVQ

Pathway: Lipid metabolism. EC: 2.7.7.41 Subcellular Location: Membrane Sequence Length: 108 Sequence Mass (Da): 12259 Location Topology: Multi-pass membrane protein

A0A945QDZ0

MSKTRLYLITPSTFNLNKFAGSLTEALEGGDVASVQLRMKESNDEDIIEAAKVLMPICHAKDVAFIINDNADIAKIVGADGVHIGQEDPTLEEVRSIIGVNKVIGVTCKDSKHISMTAGEQGADYVAFGAFFPTKTKSMATTAYPEILQWWQDIFEIPCVAIGGINSSNASSIAKAGADFVAVCSGVWDHPDGPKIAVTEINEAINT

Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). EC: 2.5.1.3 Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate Sequence Length: 207 Sequence Mass (Da): 22090

F5L8E4

MKQYTFFKGIHLKFIVILLLVIILAIQVFGAYFNRALESHLVNNFTRMLDQQAHLLAYSIQHELDKPYNEEEGLGAYEHIQFLIDKMFAAIPHAEIQVLDRNGVVISTNSDNRSIIGQRNTQIEVKRALLGTRDEAIRLHPKTGHRMKIMSIPIKVNQEVVGAVYLMASLEETYQSIAEINSLLVKGTLIALCLTAVIGVALARTISAPIKEMTKQTQAMAAGDFSKQVKVYSEDEIGQLAQGINHLSQRLSQALGEIEEEKNKLASILFYMSDGLIATDRKGRIILLNQQAEMMLNKQAKEVLGQKLSDVLDFPDEVQQDTLLFREGRFQVDIGADGQPLILEITVSPLHLDGEGQGLIAVLQDVTEREQLERDRKAFVANVSHELRTPLTTMKSYVETLISGAMDDPAVAKRFLQVIANETERMIRLVNKLLQLSKLDSKRFKLRLKKLDLHALIQETIQRFSFQLQERELTVKLDIEADLPPIEADKDMLTQVLDNILSNAIKYSLAGGQIKVTARQEGDQLKLVIEDEGVGIPKQELKHIFKRFYRVDKARSRDKGGVGLGLSITREMILAHQGSIEIDSDVGEGTAVTIRLPLQLSAREGAS

Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. EC: 2.7.13.3 Subcellular Location: Membrane Sequence Length: 607 Sequence Mass (Da): 68042 Location Topology: Multi-pass membrane protein

A0A7R9GKE7

MTNYSRFAFPVKIVSSDNSRANNDGFFQDDHASLDDEFSPGVFELLKVMSSNIMKSLPGSFLIWRPIAYLTNARDFNDATAVKVSQLKDVDSMGSHDLDSVLGAVFGNRTLAVKMQAMNVSFGLPEDGFFFGTNYTVWNLVVGLGLPPKDNFSPLIISAIIVVVTAPIAIGISGVVCLAVKRISGRMRPETSVIRS

Function: Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization. Subcellular Location: Lysosome membrane Sequence Length: 196 Sequence Mass (Da): 21315 Location Topology: Single-pass type I membrane protein

A0A922L5B2

MSFIYRSVIRKIDPLVPIKLRPIWEHDAGPKTVFFWSPVIKWGLVIAGISDLSRPVENLSARQTASLAATGLIWSRYSLVIIPKNWGLFSVNFFVAATNIAQLGRIYFHNDRKSIKDSQL

Function: Mediates the uptake of pyruvate into mitochondria. Subcellular Location: Membrane Sequence Length: 120 Sequence Mass (Da): 13642 Location Topology: Multi-pass membrane protein

R7U0W3

MAATPVPEIIALKRDGKELSKEQIGTFLRGVVDETVQDSQLGAFLMATFLRGMSDKETVELTNAMTTSGEVLHWPAEWKAITVDKHSTGGVGDKISLPLVPALAACGLKVPMISGRGLGHTGGTLDKLESIPGFNVMQTSVEMTNIINDVGCFIVGQTATLVPADRIMYAHRDVTGTVSSIPLICGSIISKKAAETLGALILDVKVGKGAVMKSSQEAEDLARNLVNVSNGMGINTKAIMSRMDHPIGLAIGNALEVIESLQCLQGKGPKSLRTLVSTLGGHLLHSTHKCKSPEEGIEIISEVLSNGKALEKFRQMLKAQGVEENVANRLCSSDMTDLPKAKHTTDDIAIFIPIAGYVSDIDSYACAVICNKLGAGRTKAGEAVDHAVGMVLCVAYGDRIEKGMTWSCC

Pathway: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2. Function: Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. EC: 2.4.2.4 Catalytic Activity: phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine Sequence Length: 409 Sequence Mass (Da): 43329

Q66KN3

MFGQTVRRFATSAIRRSHYEEGPGKNLPFSVENKWRLLGMMTLFFGSGFAFPFIIVRHQLLKK

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Subcellular Location: Membrane Sequence Length: 63 Sequence Mass (Da): 7349 Location Topology: Single-pass membrane protein

A0A935J058

MNLSKRKDIVFIILAGFFITNAIVAELIGGKLVQFFGLFTQSIGIILWPVVFLLTDIINEYYGKSGVRKLTYITVGLIIYTYILITIGINMQATNFSPVPDDAFKTVFGQSQWIIIGSIVAFLFSQLIDVYFFWVFRRLTKGKMIWLRATASTVISQFFDTFIVQFIAFVLPGNWAFEEYLKNASMGYVFKLLVALALIPVIYFLHGVIHKYIKTAEEEGVKN

Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage. Subcellular Location: Cell membrane Sequence Length: 223 Sequence Mass (Da): 25404 Location Topology: Multi-pass membrane protein

R7VK14

MVVRTRVDVGVNCLVIAAVQSGVCSDHVCLRNEEGRDRILAAAFSHTGRFFAACDDFKQMVIWAIEAGQWKTLGTRSLHRRCTSVSFSRDESSVVVADKSGDVFQYTVKTVEGDGRLLLGHVSMILDACLCADDQLLVTADRDEKLRVSRFPNSYNIHGFCLGHKEFVSCSRWLDEEKLLLSGSGDGTLKLWDLESCDLKSSVDCRSQQTDDLEVSSIAVCSEYKIVVAGFNGKSLLMVYAIQSTPNPRLEFVQTLTLSGVLWDMTFHGGCLLVLQESESKPLLGFDIQGNKLMPTDDDVSGRRRGSAFSRLSDVVNERAAFFKECASYESIFASLHKARIDNMKEYIEKKKERMSAAQKRSKNSPDQTAAPVAKQAKS

Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. Subcellular Location: Nucleus Sequence Length: 379 Sequence Mass (Da): 42026

A0A6V8PR21

MGLKATVVLSSFVVMAAHLDNQFEEGFQEEILQVHKMREGRAIILIKDLRLFGHHGVYEREKREGQPFIIDLEIEADMADATRSDHLKDTVDYGQVVSQVSRIVEEESFDLIEALAEKIAAELLKEEKIKKVAVTVKKPEAPLSRSLEYVGVRLVRGKDSDHSDS

Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4. Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. EC: 4.1.2.25 Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde Sequence Length: 165 Sequence Mass (Da): 18644

A0A2T3KIS1

MTTEVKDTFNLNVPAQSNDGHDLDDHDHHDYAGDTIFGFWIYILSDCLLFGTLFAVYAVYSNSFAGLIEPKELFNLSFVLAETALLLFSSFTFGMAMLKANHEDMKGMFKWLGITFMLGFSFLIMELYEFYHFSSEGATFHSSAYWSAFYGLVATHGLHVFAGLVWMIVLFFHFKRDGFSAENKTRLACLSLFWHFLDIIWICVFSVVYLMGVL

Function: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. Subcellular Location: Cell membrane Sequence Length: 214 Sequence Mass (Da): 24537 Location Topology: Multi-pass membrane protein

A0A6A7ZCW0

MKAWIVLLLALTLPMTALAEEAAEGAAKVSYITMSPPFVGNYGLDGSAKLKVYKADISLRVSSDEAAKAVKANDALIRNQLVGLFTQQTSESLGSVEAKEKVRQEALKQVQQVMTDETGKPMVEDLLFNNLIVQ

Function: Controls the rotational direction of flagella during chemotaxis. Subcellular Location: Cell inner membrane Sequence Length: 134 Sequence Mass (Da): 14513 Location Topology: Single-pass membrane protein

A0A5E4APS9

MLRGVLGKTFRLVGYTIQYGCIAHCAFEYVGGVVMCSGPSMEPTIQNSDIVFAENVSRHFYGIQRGDIVIAKSPSDPKSNICKRVIGLEGDKILTTSPSDFFKSHIYVSNISIMLFIGIRVD

Function: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO. EC: 3.4.21.- Subcellular Location: Mitochondrion inner membrane Sequence Length: 122 Sequence Mass (Da): 13439

A0A1C5XG09

MKEIRILIGGMGNAARPMVDLLTSERERMENVYGLHFRIVGAVDSRGGVIAPNGISSVTLSEAKNRGTLADIPGLGIQGLTALEMIEQCSADVYLDGLPPYLPTGEPGTSNIRRALERGMHVVTANKAPLALHWKELFSLAAQQGLQIRYGTAASAGLPTLEMGKLLGRCGELLEFGGIFNASCMYVFDAMGQGQSFDMAVQGAKAGGFLEPDPSMDLDGWDTAMKTVIQANTYWDQAYTLADVAIQGICGLTQADMIDAKSRGEVWCMVGRAVQNPDGSLKLTAGPERLPADHPLARAHWSDKVLWMQTRTQGGQVHHCIGASASSTPGNMYLDLVTIAREL

Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3. EC: 1.1.1.3 Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH Sequence Length: 343 Sequence Mass (Da): 36763

A0A0K2UBJ8

MGLLSEGQPLSWSETKKLADHVHEHGITQFINSYEKLKHRHGDDLKWGDEVEYFIIKFKHSSQEARVCLKAMELLSILQKPKIRGDKDLNSIWVPEYAAYMVEGTPGVPYGGGSISQFNRIEANMKMRRNEVRALLEDDESILSITNFPRLGCSKFTYPEIFPLPESEITRSLFWPDAAIYPSHPRFKTLSRNIRERRGEKVAIDLPIFKDKYTEEVLKNDPGYIDGKEGHVHCDAMGFGMGMCCLQVTFQATNVDEARILYDQLAPLCPILLALTAATPTCRGYLVDRDCRWDTISASVDCRTQEERGLLPLSTDKFVIPKSRYDSISTYLSKESLKFNYNDINLVYDKDIYEKLIDNQIDTLLAKHISHLFIRDPISVFSEKVHQDDNKETDHFENIQSTNWQTMRFKIPPVDPKIGWRVEFRPCEIQFTDFENSSIVCFVVLLTRTILSYNFNFLIPISLVDINMKRAQETDAIMKQRFYFRINIADSDAPPEIEELTIHEIFNGTSEFEFPGLISLIKSYLSNQNVETDTMCTLCNYLHFIERRASTELITNAKFIREFILDHPDYKQDSVISERINYDLLIEIDKITDGVLKNERLLGNFKT

Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. EC: 6.3.2.2 Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate Sequence Length: 607 Sequence Mass (Da): 70241

A0A0R3SFU1

MPFAQLDSFIPMLTCSDIARGLIIFAKGLPLGETGLRWLKIHLANLTGKVKRSSNDEREAYTDSILDEVIDSAEKPFDGRGWWREQEEPWQTLACCRELTAALRHPTGSADYINYFPVHQDGSCNGLQHYAAMGRDERGAASVSLEDCERPRDVYTDVTEVVEAHRKEDAEAGVEIASILEGAVQRKVIKQSVMTTVYGVTLYGAMAQIKRQLRELPAFRARAGADADKQLGPASAYLARLTLTSIGKIFTSSATTQAWFAKFQFLQ

Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. EC: 2.7.7.6 Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1) Sequence Length: 267 Sequence Mass (Da): 29636

A0A397E022

MKISTISVAVILLFYFVSMQKITIAQLDSVSRKATAENFRGLVTGDNQPGWSYKNSTCHRILKGFVVQCGSYDTRGGTSIYGKDFEDEATGLTLKHSKRGILQMANAGPNTNGAQFCFMLGPAAHLNGHHVVFGEIVQGLDVLDLMEAAGVASDDDELGRSVVLVDGGEIFD

Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. EC: 5.2.1.8 Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Sequence Length: 172 Sequence Mass (Da): 18504

A0A6B9V211

ELGQPGTLIGNDQIYNVMVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIAGGLIESGAGTGWTVYPPLAANIAHAGASVDLTIFSLHLAGASSILGAVNFITTIINMRSPGMSWDQTPLFVWSVFLTAILLLLSLPVLAGAITMLLTDRNLNTTFFDPAGGGDPILYQHLF

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 196 Sequence Mass (Da): 20997 Location Topology: Multi-pass membrane protein

B5KV22

LPGDYGFDPLGLXDPEGTGGFIEPKWLAYGEVINGRFAMLGAAGAIAPEIFGKLGLIPAETALPWFKTGVIPPAGTYDYWADPFTLFVFEMALMGFAEHRRLQDWYNPGSMGKQYFLGLEKGFAGSGD

Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Subcellular Location: Membrane Sequence Length: 128 Sequence Mass (Da): 13884 Location Topology: Multi-pass membrane protein

A0A2E4WZL4

MNLLVRIASALVLLPIALYCIHKGGWAMIGLIAVAISIALGEAFRMVFDDALEQRVLSLLGMVMLAGLGAGILDSRQLPMSLGLMAMVVIAQAVLLILRPRTIETIPARWSAACFLPLYVGLPLLLAMSMRVHSGPDLIYLCLAVTFTNDTFAYFVGKNLGKHKLHPRVSPKKTWEGLAGGVIGSLIASFIIWHWLDLKAPWTALLAYGLTMGVLTPMGDLAESLLKRAADVKDSGRIIPGHGGVLDRIDALLFGFPITYMFALLVLR

Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate EC: 2.7.7.41 Subcellular Location: Membrane Sequence Length: 268 Sequence Mass (Da): 29015 Location Topology: Multi-pass membrane protein

A0A0R3SN21

MIRFWLSVTLVTVAASAASMEESTTLALPIGALNDQDKQHFKEIFSSFKKDSIKEAHYAHIGGSVFDFNSLEGVSCDTLKTYFDSSDLEMQYYALSAARGVKSCIVGD

Pathway: Protein modification; protein glycosylation. Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 108 Sequence Mass (Da): 11854 Location Topology: Multi-pass membrane protein

A0A1X9ZWU5

TLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLILLLASSMVENGAGTGWTVYPPLSSSIAHSGASVDLAIFSLHLAGVSSILGAVNFITTIINMRSNGITFDRMPLFVWSIGITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 219 Sequence Mass (Da): 23577 Location Topology: Multi-pass membrane protein

A0A6V8PG33

WRTGKDVALEFLVSSMVIVALALGIYSVASGTIDSLHEVSRGWQWTGYNLVHHQDSVYGNIAVTQSDGQSNFYVSGLLMFTAPDPDIAFIEEVTHFPLLYHPSPQRVLLIGGGVGGVLNEILKHPVTKVVYVELDPIIIQVAREHSLTRALDDPRLRIELTDGRLFVSHTQEKYDVIIVNLSPPSTLQLNRAYTQEFFRKVHNILSPGGILSFGLPWSETYVSQEMISHNRCIYETVKKVFPGVSIIPGERSIFLASADPAALTNALETIYYRFQDRDLATRLLTVPYIQYKLSPERIERLLAPLRAGEPVETNQDLRPIGTYHNLALWNVMFYPGSRGFFNWISRMQLWWFLIPVGLLLTVPISINWRRVSSRPMLLPVVLAIMTTGFAGMTFSLISFLAFQTLHGYLYQKIGILVAAFMLGLAFGGLSMNHIMNKLRRDILALGKIELAISGYAFLLPLILILLFAHLDKLPPFIPAEVPLSLLNWGAGFLVGLEFPLANKIYLGSKSGVGRVAGTLYASDLCGAIVGAVLTSVFLIPILGISKTCLVIAMFKIASLVVLITATACPRKQTKGA

Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1. Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine Subcellular Location: Cell membrane Sequence Length: 576 Sequence Mass (Da): 63824 Location Topology: Multi-pass membrane protein

K3XXM8

MRAVAAAASPPLVARAVLLLLSPRFPPPIPRPQSIMNSSPSSSPPVGYHSRAAANTQPRGGGGRRGGRRGGGGGRWVARGGGDGGDRIDALGSSSSSSSGGYHSMPAAAASPQPRGGGDGNERTDALRSSPPSSAGYHSRTTAFASPQPRGGGDRGGRGGGNGRDRIAALGRIMSRVLRHMAVELGLDMRTDGYVRVSDLLSLNLRTYAEVPLKNHTVDEVREAVRRDNKQRFSLLEEDGELLIRANQGHTVTTVTSESLLTPILSADEVSVCVHGTYRTKLSSILQSGLKRMARLHVHFSSGLPSSGEVISGMRSNINILIHLDVKKALNDGMKLYISENKVILTEGFDGVVPVKYFEKIETWPGRAPVPLQR

Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate. EC: 2.7.1.160 Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide Sequence Length: 374 Sequence Mass (Da): 39688

A0A5E4BDT9

MQPRRLLFLKPRWPLLRREFLDPRERFLESQPPLGDANVGQFWPVEPTRDKHLRNGLRLGSDFTQAVFQAAPTGSSRGLGAFELLWRAGTRSPPLLRVGPAISMATATSGPCAGGSRDILWRVLGWRIVASVVWSVLLLPICATVFIVFSSIDLFHPIQWLSDSFNDLYSSYVIFYLLLLSVVIIIISIFNVEFYAVMPSIPCSRLALIGKIFHPQQLMHSFVHAALGMVMAWCAAVITKGRYSFLVVPCSDTESLDSSAARNCLNEYHLFFLLAGAFMGYSYSLLYFVNNMNYLPFPIIQVRHHLSIILC

Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane. Subcellular Location: Membrane Sequence Length: 311 Sequence Mass (Da): 35061 Location Topology: Multi-pass membrane protein

A0A922IC51

MLRLRPKLIRKFLSSQSQLTGTRHLSSQGSSKLKASFLLGTGAVAVTTLTLAYAKYDKQFADQLTSYAPFIKNLLEDNPTLKAKDDGISEFQIMKTYKPIETVKSISNVQQKSNGEEKAVTEKKEEPTKMPEPQKITNSKSENQPKITEKDLKNEVENLQLKAHNPNVLEDEFRGQLKRLLYAFNEFYEEKRILYETENKRKQEVEMKNYLIQERASMSEEYEKSMKKLKQMEKLLQIRDQLDKQEKASKKLWLLSQTLSKLLEHNRTLSKESTPIDIQEKIDCIRKIVDENFANETLIQVALKTLPEDAIKSGVYSEEDLVRRFYNVHKICNHVALVDKEYTNIFGYLKSYAYSYVRPLFQIEFEISPNPIKIKEIPSEELEGKMEIDPNEWDSYDILQRVKLCVEHRNLEMAIRYANLLNGEPYVVAKDWIKDAREHLEVKQVLELVQTKIASINLHQLSFSA

Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Subcellular Location: Mitochondrion inner membrane Sequence Length: 465 Sequence Mass (Da): 54152 Location Topology: Single-pass membrane protein

A6MHM4

MISHIISQESGKKETFGSLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQISYSPSLLWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAILAGFIQWFPLFTGFSLNVNLLKIQFFIMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTSWNIISSIGSTISLIGVIMFIYIIWEAMISNRTPIFSNNLSTSIEWFHQMPPSE

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 250 Sequence Mass (Da): 27976 Location Topology: Multi-pass membrane protein

A0A251TRZ8

MVSETSSRSRIIERENRQVKGQLMMNRASGSRWYHPFTARQWQELEDQALFYKYMISGMPIPPHLIYTIRASLDSSTHPPPNVGRKVDGEEAGGRCRRTDGKKWRCSKEACPDSKYCQKHMHRGRNRSRKSVELNTPIPYRKSNGMKDGEMDESFKTSLGGASWQLAINNNTSSSNPSENAYSFQQQDDEIERKEKVMHHFLI

Function: Transcription activator. Subcellular Location: Nucleus Sequence Length: 203 Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively. Sequence Mass (Da): 23471

Q6NTM7

MFILAYTFIFLMCMIGNMLVCFIVLKNRQMRTVTNMFILNLAISDLLVGIFCMPTTLVDNLITGCKNELCKERNQGQSCLQAQHQPPCCYQQYGDYCANLTS

Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Subcellular Location: Cell membrane Sequence Length: 102 Sequence Mass (Da): 11634 Location Topology: Multi-pass membrane protein

Q599J7

MKSVFYTRFFILLPWVLIVVIIIDSDTRRSPGSGPAARYYPLWNRRVGRAALTRPRPSDPSTEHNSAPHNRGKNETVLPVIFAITPTYSRPVQKAELTRLANTFRQVPRLHWILVEDSVHPTELVSRFLAGAGVKSSHLYVPTPRRYKRTGLPRATEQRNAGLDWLRLQYQQRPGIHSAQPHDLSGVVFFADDDNTYSLELFHEMRTTQKVSVWPVGLVGGRRYERPVVENGKVVSWYTGWRADRPFAIDMAGFAVSLQVILSSPKAVFKRRGSQPGMQESDFLKQITKVDELEPKANNSTKVLVWHTRTEKVNLANEPKHPQDTIKIEV

Pathway: Protein modification; protein glycosylation. Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP EC: 2.4.1.135 Subcellular Location: Golgi apparatus membrane Sequence Length: 330 Sequence Mass (Da): 37637 Location Topology: Single-pass type II membrane protein

K4A2Q6

MATMDVDNSPELRRLLEQEKEQLMAKQMVSKLTSVCWDKCITSTPGSKFSTGETTCLSNCARRFLDMSMILAKRFQLK

Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Subcellular Location: Mitochondrion inner membrane Sequence Length: 78 Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. Sequence Mass (Da): 8909 Location Topology: Peripheral membrane protein

A0A0A8TLW9

MSSVFVSNTVHEENQPAHLKLTDPTIPVNVNLPKWDEPAQRYCPAGVYEIMENDDGSKRFQINAANCVHCKTCDIKDPSQNITWVTPEGGGGPNYPNM

Cofactor: Binds 1 [4Fe-4S] cluster. Function: Accepts electrons from ETF and reduces ubiquinone. EC: 1.5.5.1 Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein] Sequence Length: 98 Sequence Mass (Da): 10873

Q7YGE0

LLPPSLTLLLMSSMVENGSGTGWTVYPPLSANIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSNGISYDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLIYTPAMMWSLGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNMKWLKTQFLIMFIGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGIIMFMIIIWKSLIKQ

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Membrane Sequence Length: 376 Sequence Mass (Da): 41445 Location Topology: Multi-pass membrane protein

A0A251VLX5

MYFLGFATDFAMLVFKNFSIFCYQFLCRLNLLTDFATILIKPHSGFKTFDDSYYRLVTKRRGLLQSDAALLNDPETRAYLVQSTSHGSTFFTDFGVSMVKMGRIGVLTGSQGEVRKVCSKRN

Cofactor: Binds 2 calcium ions per subunit. EC: 1.11.1.7 Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O Sequence Length: 122 Sequence Mass (Da): 13881

U9TZ27

MEDATYALPTSGTGTLRRGKTLTRPERYQPASPLLTGKKERKPLDPWVLFTRAVTFWAPSALLSKFFGLRDKQSQQAWREKFALCFIAAIMGGIVAFLTVGLRPTLCPSSQSNNAEQFLHYGAVDGVLGVLGWQFNVSQALINEVNFFDIIDNNGPGFDITNKFKRDVNEIPSCLAPGIQKFAAVTTPLCTSGPECPLPKLTQSAIDQYRLVNTTKKVGFDFDQVGRIKNYFVIDGAVLNMDSYIEAHPNPIENDLIDNIIRDVLNTNHPEGGKDATRLFYNREDTKQVIVCIMQKYYAGNIDKQTIGCFTSDLFNLILLVVILGIVMCRFFMACIFDWFISHRLAHKPKMEKKTTVSSPVKRKFNMNDVGNDLFTVLLVTCYSEGEVGLRITCESMAATDYPDDRKLLFLICDGIITGSGNDKSTPDICVEMMEVVEEFKNPRPMSYIAIAAGNKQHNMAKVYAGHYLYKERRVPMILVVKCGAQEEQGKPKPGNRGKRDSQLILMNFFSRITYNDRMTALDYDLFRKIHHLMGVTPDFFEIVLMVDADTKVYPNSLRLLINCMCNDPLIMGLCGETKIANKRDSWVTAIQVFEYYISHHLGKGFESVFGGVTCLPGCFCMYRLKARKGDDDWVPIITKPEIVQEYSQNEVGTLHQKNLLLLGEDRFLTTLMLRNFPRRKMTFCPQAVCKTVVPDEFKVLLSQRRRWINSTIHNLMELVLVRNLCGTFCFSMQFVVFMDLMGTVVLPVAIMLTFLLIVKSILNPPRNFSETIPLLMLVAVLGLPAILIFITTRKLVYVLWMLIYLLALPVWNFVLPSYAYWHFDDFSWGETRKVEGEGKGDDHGKKEGSFDSSKVPLKRWEDWERTRLRRMKRKERQRQQIASGAVHLTHQVIPDDESQYELLSPQTDDNYAETSSNNSQSQQYYNYLDDDYGSRQHGRI

Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP EC: 2.4.1.16 Subcellular Location: Membrane Sequence Length: 941 Sequence Mass (Da): 107305 Location Topology: Multi-pass membrane protein

A0A8S3HRB5

MWNEEFWLPRNTTWTNFTVLEQQGIRLPQLHDLIYVYPLALLLYVTRLLLEYCIAQPVGRLVGIRQVHLRNSRVSLLGKFSESCWRFIFYLCIFLYGNQVNSFLFPLKKSWTWDTKDCWLNYPNHRLTDDIFWYYMIELAFYWSLIFSQFIDVKRKDFWQMFLHHIATISLLSFSYTVNFVRIGALVLVIHDCGDFWLEVG

Pathway: Lipid metabolism; sphingolipid metabolism. Subcellular Location: Membrane Sequence Length: 201 Sequence Mass (Da): 24304 Location Topology: Multi-pass membrane protein

A0A816RKV7

MGVRFRAICGSLLFIFFIVWILLLTNEVDQSSYPRIYVASPVAQNFDYILEPGDDICSAAEPLLLIVYVHSAIENRHRRESIRSTWASRAMFGKHIRVLFMVGSSQNRDLMKQVQFEFDIYRDIVQQTFIDAYRNLTYKGIMALNWISRHCNRASYVLKTDDDMLINMFSILNHLYTLTYVYPMEAWHSTIACLVWTRMRVTRDPTSKWFVSSTEYPYEHFAPYCSGSAYFITQDLIRPLFQASRSMPFFWIDDYYITGLLPQAIRSSVYVNYLYINSLFVINVDLVEQRFLSPFGLSSLVFGHMPASVNRLLHIWQHLVTNSHSAYKYLNRTSL

EC: 2.4.1.- Subcellular Location: Golgi apparatus membrane Sequence Length: 335 Sequence Mass (Da): 39268 Location Topology: Single-pass type II membrane protein

A0A150IQG8

MNFIELIIVGAIQGFLEFLPVSSSGNVSLILMNFLKLSPSESFSLSLFLHLGTLLAVLVYFRKDIFSILKNIKTDKTSHFLIVSTLITGIVGVPIYIGLKSIFENIQIEVGNIIIGLFLIGTGIFLRYKPKSGFKKVQGSNMWDMILAGVAQGISIIPGISRSGSTLAVLLGREFDKEEALRISFLMSIPAILGGIVLEAEDTTFFMNTFPAIIGAFITSIIVIKGLLEFAKRLNFSYFCIAFGAITVIISLLIL

Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate EC: 3.6.1.27 Subcellular Location: Cell membrane Sequence Length: 255 Sequence Mass (Da): 27851 Location Topology: Multi-pass membrane protein

A0A0R3SMA2

MLDEDHFITADMEGNIQLMGRYQTVSLEEPVVPTIRTVLPIPPKPSSPPPPSLETAASSSAFTVPRSQTPASLFEPDVEQAPLHNSLELTTKCMALTEKWNMTTLSAEHWNSIGTTHTLYASTTGCLGMMVNISPILFIFLKEVEERMRRLIRPFGGLSQEVYRACRDCLSNFVTSKNIIDGELIETFLELNKEDKEKVVRGLQIPTTVDAFGRFDDTSYDSMVATKDCTVGDLTRVVEELAGLH

Pathway: Protein modification; protein ubiquitination. Function: Component of complexes involved in DNA repair and protein ubiquitination. May play a role in the regulation of the circadian clock. Subcellular Location: Nucleus Sequence Length: 245 Domain: The core of the protein consists of three WD40 beta-propeller domains. Sequence Mass (Da): 27241

A0A3B9Y2H1

MKVKITRGKFEGMNACSDKHGVIAALAIDHRGNLLQEIAMSRGANGTASAADMLVFKTAVTKTLTPYASAILLDPEYGLEAISSRSPATGVMLAYEKSGYDFSTKGRLPDLLPEWSVRRLIGIGAQAIKILLYYNPLDEEQINMVKHVYIERIGAECTALDVPFFLEPLVYDDALGDEKGLAFARRKPEYVARTMQEFSKPQYGVDVLKVEVPVNPAFMAGSRAFSGEGVAYSRQEASEHFRTIASTTTMPFIFLSAGVSNEVFCEMLELAAEAGVKFSGVLCGRATWQGGISVYANEGSPALDRWLAQQGVQNIQTINTVLVHCALPWWDVYEGKDNIEVIEQGNVSQ

Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 2/2. EC: 4.1.2.40 Catalytic Activity: D-tagatofuranose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Length: 349 Sequence Mass (Da): 38193

K4ABY9

MVAVAWPLSAVAGLIPASLTLTLLIATLVSILVLGAAAFFFEHIRRIGCMHSLERSAVSDAFFEDPNSLNKVPCPSIFDPPEKYISLIVPAYNEEHRLPEALTETLNYLKRRAAADKSFSYEVLIVDDGSTDRTSKVGFKFVKEHKIDNVRVLLLGRNHGKGEAVRKGMLHSRGELLLMLDADGATKVTDLEKLEAQVHALAQKVNSSPGTSTGSPQKVSDVEIAVFGSRAHLEKQALATRKWYRNFLMKGFHLVVLLTAGPGIRDTQCGFKMFTRAAARKLFTNIRLKRWCFDVELVYLCKHLRIPMVEVSVNWTEIPGSKVRMTSIMHMVFELLLIRVGYGLGIWKIYT

Catalytic Activity: a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-D-glucosyl phosphate + UDP EC: 2.4.1.117 Subcellular Location: Golgi apparatus membrane Sequence Length: 351 Sequence Mass (Da): 39212 Location Topology: Multi-pass membrane protein

A0A0G3Y7H2

MISHIISQESGKKETFGSLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNNSPSLLWALGFVFLFTVGGLTGVILANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYSLFTGLTMNEKWLKSQFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISTIGSTISLFGILFFLFIIWESMISKRMPIFSVQLNSSIEWYQ

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 244 Sequence Mass (Da): 27457 Location Topology: Multi-pass membrane protein

K3YVL9

MVLWVFGYGSLIWNPGFDFDDKILGFIKGYKRTFNLACIDHRGTPEHPARTCTLETDEEAICWGIAYCVKGDTDKEQKAMQYLERRECEYDQKISVDFFKEGDSLKPAVTGVLVFVSTPDPIGNKYYLGPAPLQDMARQIATANGPTGYNRDYLFSMEKALASIIHEDDSIIELANEVRKVLNRTKEAKITGSDVSLQSHVPLVHLSALPEGTVVDSR

Cofactor: Binds 2 Mn(2+) ions per subunit. Function: Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and plays a significant role in glutathione (GSH) homeostasis. EC: 4.3.2.9 Catalytic Activity: an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid Sequence Length: 218 Sequence Mass (Da): 24428

A0A1I8I9R3

SAEVASSAAADRPPIEVAVLLSDEKERKLRLFERCRQNPPSGVRFHRLDLDELLQSGSRYRVVLHKIHSELTSNKPESIDRVRRFKAWIEARGSELVLLDPLRGLESMLLARPCPGNPGDPVADSNGALRFPLLCKPHLASGAEAHSMSLVFNAGQLADLRPPLVAQEFVNHGARIIKVYVLGSRIHACIRPSVRDFQADHAGPAIQFSSHAVSKAGCQSELSDAAASAQNGDDGEMLLSRYSGLLEPLCRACRSVLGLDLLNLDLVPDTRSGRLGLVDINQFPGFESMPNYVDALVELIKLKVNY

Cofactor: Binds 2 magnesium ions per subunit. Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. EC: 2.7.1.134 Catalytic Activity: 1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+) Sequence Length: 306 Sequence Mass (Da): 33469

A0A0R3SL61

MEFDTLVRMSTILLFSIAPGVKTSSKFIDEVWLESVLVVKLNSWLNQEMNNSPPSLILMNLREYQLCYDGLKTRYAKNITSFWCESTNPDKFIHEDLGIAAYLLCLWRNDTIRKPRFVDIGCGNGLLVHILTSEGFKGKGVDIRKRKIWDLYPDNVKRNLIEMTVDPQTHPGFPEADWLIGNHSDELTPWMPILGARSNPHCRIFVIPCCPFSLFQKFDLGKHKMFTDSAIEAGSIWQGRFRGYVSYLKEHFKSCGFIPDLDILRIPSTKRLCIVGRNFTSDGWETRIANVNSVIQSENALHSAFKPRKGDPDEVMASLSIEQRVEIGAKVFSKILELGSTKEKILTVDGRQWNSGGCLSIKEACQLLDPEVMAELKFVRGGLQTVLRNQHQTFMVAKILKLLLGLVTGEGIRLRYEPERQQEMKATNNEDKPRKTKVCWMEANHPDGCPYPASLCRFAHRGEQIGIS

Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase. Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine EC: 2.1.1.211 Subcellular Location: Cytoplasm Sequence Length: 468 Sequence Mass (Da): 53258

A0A267FW43

MGQALVPDRLKHMHDMYLNPDAAPDLIKGSRFDPLLGFPNGRKERPMPPITEDEMIMAGLPEQQRDYCAHWYLAFFKCRYQYKARSFWKCADVLHGVEQCQYDDRVLRMKEHERERRLMLRQAKGQLELE

Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Subcellular Location: Membrane Sequence Length: 130 Sequence Mass (Da): 15513 Location Topology: Peripheral membrane protein

A0A251UBS3

MSPNILTPAFTFLLLCIVYALLWISLCFNHTLPPLGIDVGNPVKDVTPRTFNILHEGSKGVLSCERVPISGVSRLKLQHYASVYNVTLTPSVSIPKKWHSRIQVCFHRNSSLGLCQCENDDWRSLHNGLWVSTMSPYDQKFVDVKFGGTVTGSVTVSLEEVEQRWRYVLLVVGVVLLFFAPVVSEWVPFYYASSMVIGIITVVLIILYQARILLPTGRRNTFYLTIMCSVIGAGSFVVHHLSAFLNSFLINFGMSPEIQNLVCYFVGLGIFLLGAALGYWLLRKFFISEDGEVYVGVAQFVKWAMFIVAVTCIFLSSKDNPLAMVAVGSCLALYHITAKIKWCYYETRSYSGNQNLWARSKHTTPNHGRAEFLSCSKKTSPLNGLINSFKWSNSPVKGKLSPLTKPGSTRDVYSTYHKTPNRKNFSKEEWEEFTEESTRQSVAELASSPEFADWVVKNSGRIKLLREDSLDGLDENESSSSNGYVTQNRNGLGFFDWFLR

Catalytic Activity: NH4(+)(in) = NH4(+)(out) Subcellular Location: Nucleus inner membrane Sequence Length: 500 Sequence Mass (Da): 56278 Location Topology: Multi-pass membrane protein

A0A2C5X6U2

MRPNRYWTAGGSFWRLPSEAPELFDDLKGAELVIFKGDLNYRKLTCDAHWAPTTPFQEALGPMGKGSGVNVLSLRTCKADVVVGLPPGKDEELRKTPGGGGDSGARRWAWHGKWAVVSLSEGGEN

Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism. EC: 3.1.3.- Catalytic Activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate Sequence Length: 125 Domain: Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine. Sequence Mass (Da): 13583

E1UI20

MTNIRKTHPLLKIIILSFIDLPAPSNISSWWNFGSLLGICLMIQILTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGMYYGSYTFMETWNIGVILLFAVMATAFMGYVLPWVQMSF

Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. Subcellular Location: Membrane Sequence Length: 140 Sequence Mass (Da): 16030 Location Topology: Multi-pass membrane protein

A0A816TSH7

MYSVIFKDIILEIDDDDAKSINTLVNFCRQQNIPEIQINSLQFTYHQKSPVWWYTKPMFLYSMLNRALRMLDMEVMIKLGFFIRSLHLQLKQLHQEQSSNFQQAFTVYRGQGLSQQDFQNLCDSKGGLLSFNNFLSTSKEKEVAMNFVQDSPHESTDNVGVIFIMTIDPSKISTSNTPFAMIDKHSAVRGEKEILFTMHTVFRVVEIKQTAKNNRLCEVQLTITDDNDPQLSTLTNQIKEEVQGTTGWRKMGKLMLQVGHFDQAEELYDELLKGASDDRERAHIYHMLAMMKNSQGKYQEAIKLYEQSLKISRKTLPEDDASLAPTYSNIGLAYNNMGEYSKALEYYEKANKIYGISLPPIHPDLACSYSNIGGVYKNMGEYSKALEYYEKANQIWKISLPPTHPDLATSYNNIGQVYNNMGEYSKALEYYEKSLKIREKALPPTHPDFATSYNNIGQVYYNMGEYSKALKFHKKSLKIREKALPPTHPCFGGSYLCLAACFEKMGDYTAALNALENGYKIQEKTFEEGNQAFDSTFSWYGRVYRSLKEYSKALSYFEKCLAIERKILPEKHPNLAITYSNIGDVHRLMGDYERALAFHQKALNIQENVKCNPLDCATTYMNLGGTYREMNDYTTALTYYQKGLKICEEKLVKTHPDLAVIYHNMSKLYFLTQKYSMAMKYVQQAVEIGQEKLSSTHPHLLEYRETFEKIRKKQ

Function: Kinesin is a microtubule-associated force-producing protein that play a role in organelle transport. Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide Subcellular Location: Cytoplasm Sequence Length: 714 Sequence Mass (Da): 82451