ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
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
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K3XJZ1 | MTHVISFFSPNPTPTPPPPRVQKQKKKGNRNREPSRKKKARRSPLSHRPRAQIRMTGSMDLPAKGGFSYELCRRNDFLEKKGLKIPGFLKTGTTIVGLVFQDGVVLGADTRATEGPIVADKNCEKIHFMAPNIYCCGAGTAADTEAVTDMVSSQLQLHRYATGRESRVVTALTLLKSHLFKYQGHVSAALVLGGVDCTGPHLHTVYPHGSTDTLPFATMGSGSLAAMSVFESKYKEGLTREEGIQLVTDAIRGGIFNDLGSGSNVDVCVITKGKTEYLRNHELPNPRTYVSSKGYSFTKGQTEVLSTKITQLKQKVEVAE... | 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 ... |
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 me... |
Q6GM46 | MTAKESSNELATPDSDIYIKTFKEHMHLELELPRLSGKRTTTSPKISPRSSPRNSPCFFRKLLVNKSIRQRRRFTVAHTCFDVENGPTPGRSPLDHQASPGSGLVLHTNFTSHNQRRESFLYRSDSDYDLSPKTMSRNSSAASEQHGDDLIVTPFAQVLASLRSVRNNFTVLTNVHGVPNKRSPMTSQPQISRVNHQEDSYQKIAMDTLEELDWCLDQLETIQTYRSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISSTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLKHSSSLNNTSMSRFGVKTDY... | 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 +... |
A0A1S3T8Q3 | MASKLRTCFVCWNLSGFNCVNLSNGNGRIVRVSFPASCKMRHRTTLSSLQHKRQQIKPSTEVGLRQNKDEEEDSEVSSNNDDSVDNTNETKDSVDNTNETEEPLVININGAELAKQLSGKQREDLLGMIRNAEKNILLLNQARVRALEDLEKILAEKDALQGEINALEARLAETDARIKAAAQEKIRVELLEQQLEKLRNELAEKGGTEARYEELRDLQNGDLRDANPLSNKGIIHSLTEELNSLRTENASMKNDLESFKTHISVVKNDDERLVALEKERSSLESALKDLESKLCSQEDVSKLSILTVECKDLSGKVENL... | Pathway: Glycan biosynthesis; starch biosynthesis.
EC: 2.4.1.-
Subcellular Location: Plastid
Sequence Length: 998
Sequence Mass (Da): 112872
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T2D2Z1 | MENLSTRFDTLQEVLLAHYEKDSKKITDHVSFWELLRRESVMLHYARQQGISSLGFFQVPSLQVSEAKAKKAIMMSLMLQQLAKTPFGQEPWSMTETSLEMLEAPPKGKFKKGPRTVEVWFDNNPDNSFPYTSWTCIYIQDAEDTWHKVEGLVDYEGLYYVDCDGEVHYYVKFAADALQYATTGMWRVNYKNQTISASVSSSSSEDQQRQGQQQQQQQQQPSTTTSVEWPQRPSSSGLQHESPFTPRGHGRGCVRGRRSSGSSPHQRGDRGGRGRSQSPSTPTTPGALPPDLSFAGGDRSGGGGGGGGGGRQRGRRGSRG... | 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 transcript... |
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
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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: malony... |
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-enantio... |
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
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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
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R7UTK5 | MSDINDKVKASATTLLIENEASLAELDEADIDIAVVDGTFMTDFKYLVPHRLGVPFVSVSDFFDPWHTGVPWLPSFTPYWLLPYSHEMNFLERMKNTALYFYVRLVGISPKVSPEIVAKYSEFGSFSSPGEISAKSKLWILTSDPVLDYPKPMMPNMIEAGGISTKPAKPLDPMWTEMFQRSAGDIVLVSFGSVVSSFPEETATKLLTAFGQLKQTVIFRFKNKDELTIPANVVISDWLPQNDLLANPNIKVFVTHCGNSGQFEAVYHGVPMIAMPIFGDQFYNAQRVHYRGYGIFVDTFNFQPDDLVSAINRVSHDPSY... | 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
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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
Cat... |
A0A0J8FEY6 | MLKNSKSKLLEGWDYAPNVVTYIRIILSILFIILYLVAGPWGYTSTAIRWSVFVLFVIAASTDKLDGWMARKYNQVTELGKLLDPIADKLLMLSALIIASAFGELYWWITALFVIREIGITILRFYVINKGGKVIAASSAGKFKTLSQSIGIAMLLVPIVPIFCANDIPLWVICYYSIAYGLIGIAIGFATYSGILYVNDALKH | Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 204
Sequence Mass (Da): 22655
Location Topology: Multi-pass membrane protein
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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) + NA... |
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
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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
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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
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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
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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(+)
Sequen... |
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
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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 ... |
A0A2E4X2A9 | MLTLKPLSYLRRRKLLKALRTVVKTASKLLSKSLDVKAAHQTELQAAKTHGQSLLEKGETDLDALESAADRLTAAIYDSSFSRHVLPLGLKSFLELLVLLLAALTIRAFLYEPFKIPTGSMKPTLLHGDHVFIRKFHYGPRWPFTTDRIWQGQAPARGDIAVFNFPLDPSVDYIKRIVAVEGDRVKVVDGHLFVNGQPQSRRSLGKHTFLATDERTLQGSPRQADLYQEQSGEAAHYSLLGPQGEAFYNQWPEYYFQQPQKELGALFSDRSRGLACRSDSCEVLPGFVFTMGDNRDGSSDSRLWGGVPVEYLRGKATLIW... | 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
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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: Cytopl... |
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
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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-cytoc... |
A0A922L1U3 | MNSNEHQSNSSQQTKKFKHQPCSGVFRSEEMLLCQLFLRSNVSFETTCRLGELGIVEFRDLNADLNAYQRKYVDEIKHIGEVQRKLIYLSQQLQKSDLPIVKPIGDPAIPKYKEIIALENQIEKLDNDLREINEHLYTLRLERSELVEMSMILAKTNQLLETTRRQQRASFNGQYPITDSGNQNQALDLDPEQSSIGVPKQPQKQGFECNKIYTITGLLRAEKALAFRKVIWRVCGQNALVQFFDIDNPIDDAKAEEFVQKKVFLVMCQGDKLYGKIEKICNGFHASKYPLPDDEDHYRLLCLKVEQDLKDIQLVIEKTS... | 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 mem... |
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
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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
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W4HCH6 | MGQPDNASSSPTTPPSGDIAPILVIGAGPHALALVLALLEEDASSEFTERDTIHMGFWRQKLGRKKNQKGPRNQSKNLPTSSSSSSSCLRRQIRVLDPSGTWCSTWNGNFATFGISHLRSPVNVHLDPLRPEGLRDYATSTNQLKSQVSEPPPSIRFSRRNRAFTTNTSMFSENDRQFLGCPSRELFAEFQEHLIHQYGIASMVEKAAAVAIEPLDTSSSPLFKVTCAGGNVIVAKHVVVAIGTQNIPRIPAWATPLWQQTPTNLIVHSSDAALHAVAYAKRMRHKRVLIVGGGLTSVHLAREVVSTWGAKHVTLVTRKP... | 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
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A0A7R9BN75 | MLVKHSRRFLKRSLDHVLRIGWRLETTRRPVTGDTVEYLRLVTLDPDGVTNDYSVFYSESYSVPVLYLSRYSDSGELVAPSGCEDCLTPTDHPISGAPVLFFHPCRTSEWAVLTPKSDAGLKYIPSWMSWPFARFLGIQEPASTLFSMLNGIAHVFGLSALLRQVKSEAPFRGWWIANGLIMILCWVFSTIFHTRDTPFTEKLDYAGGMIANVAALTAVTVRLVGIERLTRTGTMIMLGAGCSFVYRHLKFLFGVSFDYGYNMKVHLAIGGFHVIGWLCWAFLNRSTCPYAWKGAAVNFLMAATMALELLDFPPFLWTLD... | 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
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K4B3F9 | MEEDKQNQVARIQDFDPPKKPKTNKYAIACTFLASLSSILLGYDIGVMSGAILYIKKDLHITDVQVEILVGILNVYSLFGSAAAGRTSDWIGRRYTMVVAAGIFFAGALLMGFATTYAFLMFGRFVAGVGVGYALMVAPVYTAEVSPASSRGFLTSFPEVFINFGILMGYVSNVVFSKLSTHLSWRFMLGIGAIPSVFLAVSVLAMPESPRWLVMQGRLGDARRVLNKTSDSLQEAQFRLADIKQAAGIPENCNDDIVEVPKRPTGDNVWKELVFSPTPAVRHILITGVGIHFFQQASGIDAVVLYSPKIFEKAGIKSDH... | Catalytic Activity: NH4(+)(in) = NH4(+)(out)
Subcellular Location: Membrane
Sequence Length: 541
Sequence Mass (Da): 59047
Location Topology: Multi-pass membrane protein
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A0A174LBR9 | MQCFQGKSVYKGIAMGPIVVLKKNDYQVKRTRIEDTEAEVKRVDEALKASQEQLQKLYDKAVREVGEASAAIFEVHQMMLEDEDYLEAIQNMIRTEQVNAEYAVAVTGDNFAEMFASMDDDYMKARSADIKDISERLVRNLSGQGDVDLSEIEPSVIVADDLSPSETVQMDKDKILAFVTVHGSTNSHTAILARMMNIPALIGVKMDLEALQSGVTAVVDGFQGMVTFDPDEETKAQTETKIQEEAEKLKLLQELKGKENITLDGRKINIYANIGSVGDIGYVMENDAGGIGLFRSEFLYLGRNDFPTEEEQFQAYKQAV... | 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 transfer... |
A0A1S3VUZ2 | MAVATRGTRGGSTFRGLFSFRIFISAMFSLLFIATLSVLFTNNPSTSQDVSDLPTTGNAYVHRTFLALKSDPLRTRVDLIHQQAKDHIALVNAYGAYARKLKLDISKQLKTFDELAHNFSDIAMKPVYQKSLFETDGPIDEDALKQFEKEVKERVKIARMIIVEAKENYDNQLKIQKLKDTIFAVHESLAKAKKNGAMASLISARSIPKSLHCLAMRLMGEKISNPEKYRDEGPKPEFEDPTLYHYVIFSDNVIAVSVVVRSVVKNAMEPWKHVFHVVANRMNVGAMKVWFKMRPIEGGAFLEVKAVEEFAFLNSSYVPI... | 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
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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): ... |
A8IXB2 | MPLAKLRNVVLEYAAIAIYVSAIYTSVVLLPSALALFYLFGATSPSAWLLLAAFLALTFTPLQLTTGALSERFVQFSVARAAAYFPTRVVVTDPEAFRTDRGYLFGFCPHSALPIALPIAFATTSPLLPKELRGRTHGLASSVCFSAPIVRQLYWWLGVRPATRQSISGLLRARKVAVLVPGGVQEVLNMEHGKEVAYLSSRTGFVRLAVQHGAPLVPVWAFGQTRAYSWFRPGPPLVPTWLVERISRAAGAVPIGMFGQYGTPMPHREPLTIVVGRPIPVPELAPGQLEPEPEVLAALLKRFTDDLQALYDKHKAQFGK... | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 327
Sequence Mass (Da): 35730
Location Topology: Multi-pass membrane protein
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A0A838H6F6 | MAKNLVIVESPTKAKTLERYLGSDFRVLASYGHVRDLPRSDFAIEVAGGDGVSLRYEIPKSSSKHVNAIRKEARGADRVFLATDLDREGEAIAWHVAEVAGIDTDDENRVVFAEITRDAILSAFERPRRIDAHLVDAQQARRAVDRIVGYRLSPTLWRNVASGISAGRVQSVALRLICDREDEIRRFVAQDYWSLHGNFARDGASVATQLHTVDGARVTDPKKLQEQAGKGREGRYLVIADAQSAEALAERSRAVRRWTVTDVKRREAKRNPQPPFTTSTLQQEAERKLGFSPSRTMRLAQQLYEGINVGDETVGLITYM... | 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 ... |
Q5FWL1 | MESREAYFNILLATDSYKVTHYKQYPPNTSRVYSYFECREKKTKNSRIRKVKYEETVFYGLQYILKKYLEGKVVTKQKIQEAKEVYREHFQDDVFNETGWNYILEKYDGHLPIEIKAVPEGSVIPRGNVLFTVENTDPECYWLTNWIETILVQTWYPITVATNSREQKKILAKYLFETSGSLTGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGIALIKRYYGTKDPVPGFSIPAAEHSTITAWGKDHERDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRSLIESRSDKAPLIIRPDSGNPLDTV... | 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... |
R7TEH1 | MKCFNWLFFVCFSLTEGHASRLEAYKHECEYYDPVKCKSEPEACNKTVEQCPDPDPSARSHCYASWKNDTGKFELVKKGCWLDQPECYDKFECVEERLEEGKPYFCCCEGHMCNANFTVSPNAKKPTTTPSTGHSHQAMLFSLLPIIGIAIVIIIVFYLWKLNHRQDPYHTQLPTHDPSPMTPPSPDLGQRPINLLEVKARGRFGCVYKAQMGERVIAVKVFPLQDKQSWATEKDIYSLPQLNCHANILHYIGAEKRGENLNMDLWLITQFHEQGSLYDYLKGNLVSWQQLLAICESMAKGLAYLHEDLPATRTQQAKPA... | 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
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R7UJA8 | MAVEHMRLSSGIDMPILGLGTWKSKPGEVENAVKAAIDAGYRHLDCAWIYGNEQEVGAALKSKIDEGVVKREDLFITSKIWNTKHRFEDALTNIKQSLSNLGISYLDLSLIHWPTSMKHDGNCDKFPRDDQGNVQHTNVSYLETWKALEKAMDDGLVKAIGLSNFNSRQIGEIISNARIQPSVLQVEIHPYFTQEKLVHFCKERNIVVTAYSPLGSPDRPWAAPGEPLLLEDPKLIEIAKKYSKSPAQVIIRWLMQRGIAVIPKSVTPSRIIENFNVRDFKLTADDMNVVSGFNRNHRLVCPSITVNGVRQFRDRAAPNF... | 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
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A0A1I2JDI3 | MKDNKLKKILIIIVIVLVVGAVGFKFYYNRLVNHPFKLTVDSVELEVKEGQSLNDVLKKLSKQNIIGNTYLIKYYVKSNDLDTNIKKGRYLIEKNMTLDTFLSNLSLGKVTAGLNKVTIPEGYNIEEIAASLEKSQVISKEEFLKAVKEYNAPSYIKKNSERKYQLEGFLFPDTYEFEKDISGEEIIERMLLRFEEVISEIEQATGKKIDKNNLDDIVTMASIVEKEAERDDERGKVASVFYNRIEQHTKFQSCATVLYALGYHKAEVSNEDIKVNSPYNTYKVDGLPIGPIACPGKASLNAAINPEKTNYLFFISNDDG... | 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
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A0A3B8T2P7 | MHVEHAIVGAGLIGGYLAAHLADVTLQLQSDARLLVVGRDYAKCQFGPRMTISDFATPVQTRDTQNIEFVTNTSSWASTKRYPNVVWLTIKCTGIKQVVPDIRPLIGPQTIVVCCQNGIGSDAVIRQAFPDNPVIRCMFPFNVVKLNKGHFHRGSSGTVMLERLPLGQYPVFDDFHQRFSPVIDALNEQYGEVFPCAWCSNMDALLWAKCQVNLTNSVNALSNLSLKETLLDKGYRKIIALMMQEHLAVCAAQGIALPKITKVAAKFIPTVLRLPNWLFSRVAKSMVDIDPHAKLSMWWDLDQGRATEIDFINGATMIAG... | 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
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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
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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 = [thioredoxi... |
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
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K3Z4A4 | MAALEAARAWAASVIPPELAAAAGGDPLAALAATAAALVAGLLILAVWFRSGNGAPAKPAPTPVRPPPVKIDADADVDDGRKRVTIFFGTQTGTAEGFAKSMAEEARARYEKAVFKVVDLDDYAQEDEEYEEKLKKETVVLFFLATYGDGEPTDNAARFYKWFTEGKEKEVWLKDLKFGVFGLGNRQYEHFNKVAKVVDELLQEQGGKRLVPVGLGDDDQCIEDDFTAWKELVWPELDQLLRDEDDTTGASTPYTAAIPEYRVVFIDRSDLSFQDRSWTLANGTGVIDIHHPCRSNVAVRKELHKPASDRSCIHLEFDIS... | 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 ... |
A0A0U2VZT1 | MGTVLDSSLIEGELVLDLKNVSKDMIEVVGGKAANLGELLSLGIRVPPGFVITSNAFRYFLKYNGLYDVIKNIFENDKDEKKVSEKVKSLILNAEIPPDLKKAISDAYEQLEKISNKEVLVAVRSSATVEDIEEASFAGQQDTFLNVSKNDLFSYIKKVWASLHNERAISYRNAKGIDHLSAHMAVVVQKMVNAKAAGVMFTLHPSTGDTNYVIIESNWGLGESVVGGKVTPDEIVIDKSTLKIVQKRISHKTIKVTYDKQMKKNVELKLDENEANSISITEEEAKELAKLALKVEQHYERPMDIEWAIDSDIKFPENIF... | 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
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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
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A8J1T4 | MVQALCSAGAARRGGRQAYSFLASLLSQQRGFAAAAEKDVVVVGGGPGGYVAAIKAAQLGLSVACVEGRGALGGTCLNVGCIPSKALLNSSHMYMEAKQHFGSYGIKMDGLSYDFAAVQAQKDGVVSGLTKGIEGLFKKNKVEYVKGWGKLVSPHEVEVAAADGSSSRLRAKNILLATGSEVTPLPGVPIDEEKIVSSTGALALKSVPGEMVVIGGGYIGLEMGSVYQRLGAKVTVVEFLDNIVPSMDAEVRRSFMRTLEKQGLKFKMGTKVTKGEVVGGRVHLTLEPAKGGAAEKMECDVCLVSIGRRPYSKGLGLEAV... | 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
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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
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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-met... |
F5L8E4 | MKQYTFFKGIHLKFIVILLLVIILAIQVFGAYFNRALESHLVNNFTRMLDQQAHLLAYSIQHELDKPYNEEEGLGAYEHIQFLIDKMFAAIPHAEIQVLDRNGVVISTNSDNRSIIGQRNTQIEVKRALLGTRDEAIRLHPKTGHRMKIMSIPIKVNQEVVGAVYLMASLEETYQSIAEINSLLVKGTLIALCLTAVIGVALARTISAPIKEMTKQTQAMAAGDFSKQVKVYSEDEIGQLAQGINHLSQRLSQALGEIEEEKNKLASILFYMSDGLIATDRKGRIILLNQQAEMMLNKQAKEVLGQKLSDVLDFPDEVQQ... | 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
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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
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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
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R7U0W3 | MAATPVPEIIALKRDGKELSKEQIGTFLRGVVDETVQDSQLGAFLMATFLRGMSDKETVELTNAMTTSGEVLHWPAEWKAITVDKHSTGGVGDKISLPLVPALAACGLKVPMISGRGLGHTGGTLDKLESIPGFNVMQTSVEMTNIINDVGCFIVGQTATLVPADRIMYAHRDVTGTVSSIPLICGSIISKKAAETLGALILDVKVGKGAVMKSSQEAEDLARNLVNVSNGMGINTKAIMSRMDHPIGLAIGNALEVIESLQCLQGKGPKSLRTLVSTLGGHLLHSTHKCKSPEEGIEIISEVLSNGKALEKFRQMLKAQ... | 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 A... |
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-cytoc... |
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
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R7VK14 | MVVRTRVDVGVNCLVIAAVQSGVCSDHVCLRNEEGRDRILAAAFSHTGRFFAACDDFKQMVIWAIEAGQWKTLGTRSLHRRCTSVSFSRDESSVVVADKSGDVFQYTVKTVEGDGRLLLGHVSMILDACLCADDQLLVTADRDEKLRVSRFPNSYNIHGFCLGHKEFVSCSRWLDEEKLLLSGSGDGTLKLWDLESCDLKSSVDCRSQQTDDLEVSSIAVCSEYKIVVAGFNGKSLLMVYAIQSTPNPRLEFVQTLTLSGVLWDMTFHGGCLLVLQESESKPLLGFDIQGNKLMPTDDDVSGRRRGSAFSRLSDVVNERA... | 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... |
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-dihydr... |
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
Sequen... |
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
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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
Se... |
A0A1C5XG09 | MKEIRILIGGMGNAARPMVDLLTSERERMENVYGLHFRIVGAVDSRGGVIAPNGISSVTLSEAKNRGTLADIPGLGIQGLTALEMIEQCSADVYLDGLPPYLPTGEPGTSNIRRALERGMHVVTANKAPLALHWKELFSLAAQQGLQIRYGTAASAGLPTLEMGKLLGRCGELLEFGGIFNASCMYVFDAMGQGQSFDMAVQGAKAGGFLEPDPSMDLDGWDTAMKTVIQANTYWDQAYTLADVAIQGICGLTQADMIDAKSRGEVWCMVGRAVQNPDGSLKLTAGPERLPADHPLARAHWSDKVLWMQTRTQGGQVHHC... | 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
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A0A0K2UBJ8 | MGLLSEGQPLSWSETKKLADHVHEHGITQFINSYEKLKHRHGDDLKWGDEVEYFIIKFKHSSQEARVCLKAMELLSILQKPKIRGDKDLNSIWVPEYAAYMVEGTPGVPYGGGSISQFNRIEANMKMRRNEVRALLEDDESILSITNFPRLGCSKFTYPEIFPLPESEITRSLFWPDAAIYPSHPRFKTLSRNIRERRGEKVAIDLPIFKDKYTEEVLKNDPGYIDGKEGHVHCDAMGFGMGMCCLQVTFQATNVDEARILYDQLAPLCPILLALTAATPTCRGYLVDRDCRWDTISASVDCRTQEERGLLPLSTDKFVI... | 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
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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
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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
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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-cytoc... |
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
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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 (... |
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 m... |
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-cytoc... |
A0A6V8PG33 | WRTGKDVALEFLVSSMVIVALALGIYSVASGTIDSLHEVSRGWQWTGYNLVHHQDSVYGNIAVTQSDGQSNFYVSGLLMFTAPDPDIAFIEEVTHFPLLYHPSPQRVLLIGGGVGGVLNEILKHPVTKVVYVELDPIIIQVAREHSLTRALDDPRLRIELTDGRLFVSHTQEKYDVIIVNLSPPSTLQLNRAYTQEFFRKVHNILSPGGILSFGLPWSETYVSQEMISHNRCIYETVKKVFPGVSIIPGERSIFLASADPAALTNALETIYYRFQDRDLATRLLTVPYIQYKLSPERIERLLAPLRAGEPVETNQDLRPI... | 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: putre... |
K3XXM8 | MRAVAAAASPPLVARAVLLLLSPRFPPPIPRPQSIMNSSPSSSPPVGYHSRAAANTQPRGGGGRRGGRRGGGGGRWVARGGGDGGDRIDALGSSSSSSSGGYHSMPAAAASPQPRGGGDGNERTDALRSSPPSSAGYHSRTTAFASPQPRGGGDRGGRGGGNGRDRIAALGRIMSRVLRHMAVELGLDMRTDGYVRVSDLLSLNLRTYAEVPLKNHTVDEVREAVRRDNKQRFSLLEEDGELLIRANQGHTVTTVTSESLLTPILSADEVSVCVHGTYRTKLSSILQSGLKRMARLHVHFSSGLPSSGEVISGMRSNINI... | 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
Se... |
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 memb... |
A0A922IC51 | MLRLRPKLIRKFLSSQSQLTGTRHLSSQGSSKLKASFLLGTGAVAVTTLTLAYAKYDKQFADQLTSYAPFIKNLLEDNPTLKAKDDGISEFQIMKTYKPIETVKSISNVQQKSNGEEKAVTEKKEEPTKMPEPQKITNSKSENQPKITEKDLKNEVENLQLKAHNPNVLEDEFRGQLKRLLYAFNEFYEEKRILYETENKRKQEVEMKNYLIQERASMSEEYEKSMKKLKQMEKLLQIRDQLDKQEKASKKLWLLSQTLSKLLEHNRTLSKESTPIDIQEKIDCIRKIVDENFANETLIQVALKTLPEDAIKSGVYSEED... | 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: 46... |
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-cytoc... |
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 phosphatidylinosit... |
Q599J7 | MKSVFYTRFFILLPWVLIVVIIIDSDTRRSPGSGPAARYYPLWNRRVGRAALTRPRPSDPSTEHNSAPHNRGKNETVLPVIFAITPTYSRPVQKAELTRLANTFRQVPRLHWILVEDSVHPTELVSRFLAGAGVKSSHLYVPTPRRYKRTGLPRATEQRNAGLDWLRLQYQQRPGIHSAQPHDLSGVVFFADDDNTYSLELFHEMRTTQKVSVWPVGLVGGRRYERPVVENGKVVSWYTGWRADRPFAIDMAGFAVSLQVILSSPKAVFKRRGSQPGMQESDFLKQITKVDELEPKANNSTKVLVWHTRTEKVNLANEPK... | 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 ... |
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 me... |
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 | LLPPSLTLLLMSSMVENGSGTGWTVYPPLSANIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSNGISYDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLIYTPAMMWSLGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNMKWLKTQFLIMFIGVNI... | 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-cytoc... |
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 | MEDATYALPTSGTGTLRRGKTLTRPERYQPASPLLTGKKERKPLDPWVLFTRAVTFWAPSALLSKFFGLRDKQSQQAWREKFALCFIAAIMGGIVAFLTVGLRPTLCPSSQSNNAEQFLHYGAVDGVLGVLGWQFNVSQALINEVNFFDIIDNNGPGFDITNKFKRDVNEIPSCLAPGIQKFAAVTTPLCTSGPECPLPKLTQSAIDQYRLVNTTKKVGFDFDQVGRIKNYFVIDGAVLNMDSYIEAHPNPIENDLIDNIIRDVLNTNHPEGGKDATRLFYNREDTKQVIVCIMQKYYAGNIDKQTIGCFTSDLFNLILL... | 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 | MGVRFRAICGSLLFIFFIVWILLLTNEVDQSSYPRIYVASPVAQNFDYILEPGDDICSAAEPLLLIVYVHSAIENRHRRESIRSTWASRAMFGKHIRVLFMVGSSQNRDLMKQVQFEFDIYRDIVQQTFIDAYRNLTYKGIMALNWISRHCNRASYVLKTDDDMLINMFSILNHLYTLTYVYPMEAWHSTIACLVWTRMRVTRDPTSKWFVSSTEYPYEHFAPYCSGSAYFITQDLIRPLFQASRSMPFFWIDDYYITGLLPQAIRSSVYVNYLYINSLFVINVDLVEQRFLSPFGLSSLVFGHMPASVNRLLHIWQHLV... | 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 Topolog... |
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 do... |
A0A3B9Y2H1 | MKVKITRGKFEGMNACSDKHGVIAALAIDHRGNLLQEIAMSRGANGTASAADMLVFKTAVTKTLTPYASAILLDPEYGLEAISSRSPATGVMLAYEKSGYDFSTKGRLPDLLPEWSVRRLIGIGAQAIKILLYYNPLDEEQINMVKHVYIERIGAECTALDVPFFLEPLVYDDALGDEKGLAFARRKPEYVARTMQEFSKPQYGVDVLKVEVPVNPAFMAGSRAFSGEGVAYSRQEASEHFRTIASTTTMPFIFLSAGVSNEVFCEMLELAAEAGVKFSGVLCGRATWQGGISVYANEGSPALDRWLAQQGVQNIQTINT... | 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 M... |
K4ABY9 | MVAVAWPLSAVAGLIPASLTLTLLIATLVSILVLGAAAFFFEHIRRIGCMHSLERSAVSDAFFEDPNSLNKVPCPSIFDPPEKYISLIVPAYNEEHRLPEALTETLNYLKRRAAADKSFSYEVLIVDDGSTDRTSKVGFKFVKEHKIDNVRVLLLGRNHGKGEAVRKGMLHSRGELLLMLDADGATKVTDLEKLEAQVHALAQKVNSSPGTSTGSPQKVSDVEIAVFGSRAHLEKQALATRKWYRNFLMKGFHLVVLLTAGPGIRDTQCGFKMFTRAAARKLFTNIRLKRWCFDVELVYLCKHLRIPMVEVSVNWTEIPG... | 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-cytoc... |
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: 2... |
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
S... |
A0A0R3SL61 | MEFDTLVRMSTILLFSIAPGVKTSSKFIDEVWLESVLVVKLNSWLNQEMNNSPPSLILMNLREYQLCYDGLKTRYAKNITSFWCESTNPDKFIHEDLGIAAYLLCLWRNDTIRKPRFVDIGCGNGLLVHILTSEGFKGKGVDIRKRKIWDLYPDNVKRNLIEMTVDPQTHPGFPEADWLIGNHSDELTPWMPILGARSNPHCRIFVIPCCPFSLFQKFDLGKHKMFTDSAIEAGSIWQGRFRGYVSYLKEHFKSCGFIPDLDILRIPSTKRLCIVGRNFTSDGWETRIANVNSVIQSENALHSAFKPRKGDPDEVMASLS... | 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):... |
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.
... |
A0A251UBS3 | MSPNILTPAFTFLLLCIVYALLWISLCFNHTLPPLGIDVGNPVKDVTPRTFNILHEGSKGVLSCERVPISGVSRLKLQHYASVYNVTLTPSVSIPKKWHSRIQVCFHRNSSLGLCQCENDDWRSLHNGLWVSTMSPYDQKFVDVKFGGTVTGSVTVSLEEVEQRWRYVLLVVGVVLLFFAPVVSEWVPFYYASSMVIGIITVVLIILYQARILLPTGRRNTFYLTIMCSVIGAGSFVVHHLSAFLNSFLINFGMSPEIQNLVCYFVGLGIFLLGAALGYWLLRKFFISEDGEVYVGVAQFVKWAMFIVAVTCIFLSSKDN... | 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... |
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 membra... |
A0A816TSH7 | MYSVIFKDIILEIDDDDAKSINTLVNFCRQQNIPEIQINSLQFTYHQKSPVWWYTKPMFLYSMLNRALRMLDMEVMIKLGFFIRSLHLQLKQLHQEQSSNFQQAFTVYRGQGLSQQDFQNLCDSKGGLLSFNNFLSTSKEKEVAMNFVQDSPHESTDNVGVIFIMTIDPSKISTSNTPFAMIDKHSAVRGEKEILFTMHTVFRVVEIKQTAKNNRLCEVQLTITDDNDPQLSTLTNQIKEEVQGTTGWRKMGKLMLQVGHFDQAEELYDELLKGASDDRERAHIYHMLAMMKNSQGKYQEAIKLYEQSLKISRKTLPEDD... | 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
|
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