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stringlengths 6
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stringlengths 11
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C4Z900 | MKFTKMHGCGNDYVYVNLFEEKLDDPARVSIYVSDRHFGIGSDGLITIGPSDKADFRMRIYNADGSEAEMCGNGIRCVAKYVYDHKLTDKTEISVETGAGIKYLTLYVEENKVSQVRVDMGEPILTPGDIPVVKADGSAYSDDYRVIDEPISAGNREWHMTCVSMGNPHAVVFVDDVAGFELEKYGPLFENHKMFPKRTNTEFVEILSRNEAKMRVWERGSAETWACGTGTCATVMACILNKKTDNKVLVHLRGGDLTIEYIPETNHVFMTGPATEVFSGEIDII | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 31778
Sequence Length: 285
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q21SV0 | MRIPFTKMQGAGNDFVVLDETQGRFGLSTAHYRLLADRHFGVGADQILTVRPSPAPGIDFEYLIHNADGAEVEQCGNGARCFARFVRDQGLTAKDAIRVQTRGGVIEPQLNPDGRVTVNMGAPVFELAEIPFDATGLQPQTSGLWKKWPLALVDSGHATTVYVAVVSMGNPHAVQVVDDVDTAPVRLQGPLIEHHASFPKRVNAGFMQIVDRSHIRLRVYERGTGETLACGSGACAAVVAGIRLGLLDDTVHVQTHGGTLTISWAGAAAPVLMTGPATPVFHGEINLPDNL | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 31084
Sequence Length: 291
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
A6TRX5 | MEIKFKKMHGTGNDFIMIYYEDYPFEQHFNQLAKEVCHRHFGIGADGLMIVKESSVADVQMKYFNSDGSEAGMCGNGIRCFAKFVYDEGLVKKEIFTVETLSGVKELQVATVEEKVSSVRVNMGKMVLDPKQIPVNSEGLQFINEQLMIDGEKYTISTVLLGVPHTIIFMETLDLDRVKRVGKIIENHQLFPENTNVNFAQIINQNTIRVRTWERGAGYTLACGTGVSSVCGIANHLSLVGPNVVVEIEGGKLDIEIAPEGDIYMEGPAKDICKGVYLNSLIK | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 31494
Sequence Length: 283
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
A8MH77 | MDVQFKKMQGTGNDFIVVKYDDFPFEEKLSQLAEKICDRHFGIGADGLLIVNPSSIADIRMDYYNSDGSIAAMCGNGIRCFSKFVFDEGFLRTKQFSVETLDGIKEIAIIEEKGTVKSVEVNMGQVTYDTEKIPVVSEDGYFINKKITVGGQDFIITAVSMGVPHVIIFTEKLDLEQIKFFGPLIEKHAIFPKKTNVNFVHRIDKDNIAVRTWERGAGYTLACGTGSTSAVAVANKLGLVNNNVNVEVEGGNIKIKIKESGNLFMEGPAENICSGRFFFN | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30983
Sequence Length: 280
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q8F9V5 | MASLKFTKMEGIGNDYVYIDSTRNDIRLTPEQIQKISDRNFGIGSDGVIFIRNSKQGDFMMDMYNSDGSSSEMCGNGIRCVAKYIYDHGLTSSKNPKIETGAGILEVDLKIGSGNKVDLVSVDMGKPVLVPSQIPVVWKNEETIIDQPLEIGDKNLKFTAVSMGNPHCVIFVDDSDEFPVRGIGPLIERHSIFPKRVNVEFVTIRGKDHLYQRTWERGAGETLACGTGACAVMVAGNLTRRSGKDVQIDLRGGTLRIQWQESGNILMTGPAREIFSGEIEI | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30966
Sequence Length: 281
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q8Y5N9 | MATIHFTKVHGSQNDFFLVDEEGNQIMDWSDAKRADFAIKLCDREHSLGGADGILYVTKSSEAGPIGQMRVVNSDGSIASMCGNGLRTVARYLLEKHALTEAKVETMKAILDVKKATSLGFDIPTYQVEISPVKFNAESLPMNVGVEKLFNQVVPELDAELAFSAVSVPNPHLITFVDQTVLDSDRQETLASYLNSENPYFPDGVNVSFVKRLSDDAIYVRTFERGVGFTNACGTAMSACSLIKKMLDKDTFETPLNVYNDGGRVQVTAKKDEAGDISLQLIGNATFVSTGSVSYESDTVTELTNEATPEQAQYQELVKEVKEFLKTTE | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 36071
Sequence Length: 329
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
A0LE31 | MGERFIKMHGLGNDFVVLDHLESPRELSPQEARFWADRRRGVGCDQVVQLLPGVEGGDAQMRIYNPDGSRAEMCGNAMRCVGLYLHEQRGMAAALAVETLAGIMRPQVTSALAITVDMGRPQWAGRAIPLDQDGEMIDAPLEVGGQSYRMTALSMGNPHGVVRVADAEGFELAKVGPLVEHHALFPNRINFEVVQVLSRSRIRMRVWERGAGITPACGTGACAAAVACMRQGWVERDCTVVLDGGELQIVWLESDRVMMSGPATEVFRGELVGLPAGF | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30199
Sequence Length: 278
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q0W3B6 | MTKIKFTKMHGNGNDFIVIDEFENPVPEEKKAAFAKKVCHRRFGIGADGVLFLAKPLHTSLHMRIFNEDGSEAEMCGNGIRCFVKYAVDNGHMNPGKDKVETKAGILEVEARIEDGKTLVKVSMGKPLFDPKKIPAAGLNNFINKPLHGYEVTAVNTGVPHAVIFVDDVNAVDLMKVAPEIRYDLKTFPKGINVNFVQREGHNLRVRTYERGVEGETLSCGTGSVASAAVARYLGYTRDETTVYTAGGQLNISFVSDIAYMEGPAETVYEGEIDVDFSAL | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30722
Sequence Length: 280
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q58519 | MEFTKMHALGNDYIVINEFDGEKVKEEEKAEFSRKICRRGFSVGADGVIFIQKPTSDEYDVRFRIFNSDGSEAEMCGNGIRCFSKYVYERIMKKNPLKVETKGGLRVSEMEIEGDEVKKIKVYMGVPKFKLKDIPMVVDGYKEDDEFLNGELKLKNPYLPKVKLSVVNVGNPHAVIFVEDNNIDLDFVREHLDVIGKEIEHHEAFPERINVHFVKVLNPNEIRIVTWERGAGYTTACGTGTTASVIMAHKLGKTNNRVLAHLDGGDLEIEIKDDGVYMIGDAVMVYDAKLINIGW | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 33442
Sequence Length: 295
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q8TY71 | MQFWKVHGARNDFVLVDETEEEVVPESDKPDFARWACDRRSGVGADGVVFIRSDPPSVEMRIFNRDGSEAEFCGNAARCVVKYVTEVRGENVKILRTLSGAHRVEVQGGWIAVEVPEAEIKKVVELGYEVDAGVPHFVRLTERDPIHDFGGLTDEAKTIFSEYEPKGGVNVTYAAPSVDELRVRTFERGVGWTPACGSGVVAASLVYSEIFGPFEEVSVRTAGGCLRVSLSDGPLLIGRAEIVYKGELRGDWRENTDHQRRRHSLSRSPSGRPRLQECR | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30994
Sequence Length: 279
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q8E9H5 | MIQFTKMHGLGNDFMVVDGITQNVFFSPEQIRRLADRNFGVGFDQLLLVEPPYDPDLDFHYRIFNADGGEVENCGNGARCFARFVRNKGLTNKNKIRVSTSAGKMTLRLERDGTVTVNMGVPVLEPSQIPFKAKKAEKTYLLQTPQQTFLCGAASMGNPHCVLDVEDVANANVAEIGALLTKHERFPRGVNVGFMQVVNAGHIKLRVYERGAAETLACGTGACAAVVVGQIQGKLDQQVQVDLPGGSLTINWEGEGKPLWMTGPAQHVYDGQIQL | Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 30063
Sequence Length: 275
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Subcellular Location: Cytoplasm
EC: 5.1.1.7
|
Q9UN19 | MGRAELLEGKMSTQDPSDLWSRSDGEAELLQDLGWYHGNLTRHAAEALLLSNGCDGSYLLRDSNETTGLYSLSVRAKDSVKHFHVEYTGYSFKFGFNEFSSLKDFVKHFANQPLIGSETGTLMVLKHPYPRKVEEPSIYESVRVHTAMQTGRTEDDLVPTAPSLGTKEGYLTKQGGLVKTWKTRWFTLHRNELKYFKDQMSPEPIRILDLTECSAVQFDYSQERVNCFCLVFPFRTFYLCAKTGVEADEWIKILRWKLSQIRKQLNQGEGTIRSRSFIFK | Function: May act as a B-cell-associated adapter that regulates B-cell antigen receptor (BCR)-signaling downstream of PI3K.
PTM: Phosphorylated on tyrosine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32194
Sequence Length: 280
Subcellular Location: Cytoplasm
|
P16524 | MEHLLNPKAREIEISGIRKFSNLVAQHEDVISLTIGQPDFFTPHHVKAAAKKAIDENVTSYTPNAGYLELRQAVQLYMKKKADFNYDAESEIIITTGASQAIDAAFRTILSPGDEVIMPGPIYPGYEPIINLCGAKPVIVDTTSHGFKLTARLIEDALTPNTKCVVLPYPSNPTGVTLSEEELKSIAALLKGRNVFVLSDEIYSELTYDRPHYSIATYLRDQTIVINGLSKSHSMTGWRIGFLFAPKDIAKHILKVHQYNVSCASSISQKAALEAVTNGFDDALIMREQYKKRLDYVYDRLVSMGLDVVKPSGAFYIFPSIKSFGMTSFDFSMALLEDAGVALVPGSSFSTYGEGYVRLSFACSMDTLREGLDRLELFVLKKREAMQTINNGV | Function: Essential for murein biosynthesis . Probably catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL-2,6-diaminopimelate (Probable).
Catalytic Activity: 2-oxoglutarate + N-acetyl-(2S,6S)-2,6-diaminoheptanedioate = L-2-acetamido-6-oxoheptanedioate + L-glutamate
Sequence Mass (Da): 43536
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (acetylase route): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.6.1.-
|
Q7ZXQ9 | MSVNLSKNGAALQGAYKDVLDEKTKTDWALYTYEGNSNDIRLAETGDGGLEELVEELSSGKVMYAFCRVKDPNSGLPKFVLVNWTGEGVKDARKGACANHVSTMANFLKGAHVTINARAEEDVEPESIMEKVAKASGANYNFHKESKRGNEGPQGPVGSVYQKTNAMSEIKRVGKENFWAKAEKDEEERRMEENRRANSEKDRLERERKEREQREAETREQRFRERAKEIDAQRKEQEETEKQQTVPASQRSVNPRETFLQKERSLPESGPVSAQPGRLRSPFLQKSACQPESSPPPSPVHRVQEPPSPPVYPAHQTPPESPVPPVSHPPESTVHVKEQCTASQQEEENIYQDATEDQNIYEDTTENQNIYEDTPQEEPVYEIEVEEEKGVCARALYDYQAADDTEISFDPDDLITQIQFIDEGWWRGFSPAGHFGMFPANYVELLE | Function: Adapter protein that binds F-actin and dynamin, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation. Does not bind G-actin and promote actin polymerization by itself, but excerts its functions by interaction with other proteins. Required for the formation of organized podosome rosettes (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50612
Sequence Length: 447
Subcellular Location: Cytoplasm
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Q557J6 | MASLDISDPDITKYIKLVQDGNPANRWIVFSYVPKSNNKIKFCDSGSGDLKELREELDDSSIRFAYIRFVINNMPKFVYIPWCGDGVNGPIKGAFSGHAIEFSKSFKPIHHQVNARSEEDIDEKAITAALNKATGASYDSGSKVQGATKGTFIPQSVSQGREAATKSNAEVKNVINKNDYNKIQESAEYWKQNQANKSEPAKPTRPEYNLSTERDDYWKQQQAEKQKQQQQQQQQQASRVNAPPPSRTVGNKFQEQVSKPTETAPPQPRPAPSKGSVLNRFPAATQQQQEPPAPSRPAAPVPSRVNKPAAPVQPVYQEPVHEEPQYEEPQYEEEQQQQYEEQPTEEQQYYQEEPQQQYEEQPTEEQQYYQEEQQQYEEQPTEEQQYYQEEQQQYEQPTEDQQYYQEEQQQYEQPAEEQYDQSGYLQAKALYDYNGENDGDLSFREGDIITILDQSDPDGWWQGSLPTGEQGFFPSNFVQQL | Function: Actin-binding adapter protein. Binds to F-actin but is not involved in actin polymerization, capping or bundling. Does not bind G-actin. Controls pseudopodium number and motility in early stages of chemotactic aggregation.
Sequence Mass (Da): 55338
Sequence Length: 481
Domain: The SH3 domain mediates the control of pseudopodium number.
Subcellular Location: Cytoplasm
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Q9UJU6 | MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACASHVSTMASFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESGRFQDVGPQAPVGSVYQKTNAVSEIKRVGKDSFWAKAEKEEENRRLEEKRRAEEAQRQLEQERRERELREAARREQRYQEQGGEASPQRTWEQQQEVVSRNRNEQESAVHPREIFKQKERAMSTTSISSPQPGKLRSPFLQKQLTQPETHFGREPAAAISRPRADLPAEEPAPSTPPCLVQAEEEAVYEEPPEQETFYEQPPLVQQQGAGSEHIDHHIQGQGLSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE | Function: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes (By similarity). May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes.
PTM: Degraded by caspases during apoptosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 48207
Sequence Length: 430
Domain: The SH3 domain mediates interaction with SHANK2, SHANK3 and PRAM1.
Subcellular Location: Cytoplasm
|
Q13409 | MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREAEALLQSMGLTPESPIVFSEYWVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRTLHWDTDPSVLQLHSDSDLGRGPIKLGMAKITQVDFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNADYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA | Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function . Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules . The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (By similarity). Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (By similarity).
PTM: The phosphorylation status of Ser-90 appears to be involved in dynactin-dependent target binding.
Sequence Mass (Da): 71457
Sequence Length: 638
Subcellular Location: Cytoplasm
|
Q9Y6G9 | MAAVGRVGSFGSSPPGLSSTYTGGPLGNEIASGNGGAAAGDDEDGQNLWSCILSEVSTRSRSKLPAGKNVLLLGEDGAGKTSLIRKIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDAVSLKDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKQMEQKLIRDFQEYVEPGEDFPASPQRRNTASQEDKDDSVVLPLGADTLTHNLGIPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKAEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVSGGSPAGGAGGGSSGLPPSTKKSGQKPVLDVHAELDRITRKPVTVSPTTPTSPTEGEAS | Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores.
PTM: Phosphorylated during mitosis but not in interphase.
Sequence Mass (Da): 56579
Sequence Length: 523
Subcellular Location: Cytoplasm
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Q9QXU8 | MAAVGRVGSFGSSPPGLASTYASGPLANELASGSGGPAAGDDEDGQNLWSRILREVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGEDFPASPQRRATAAQEDRDDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKIEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVGGSPGGGAAGASTSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSPTTPPSPTEGEAS | Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By similarity).
PTM: Phosphorylated during mitosis but not in interphase.
Sequence Mass (Da): 56792
Sequence Length: 523
Subcellular Location: Cytoplasm
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P16453 | MMEPSEYHEYQARGKEMVDYICQYLSTVRERQVTPNVKPGYLRAQIPSSAPEEPDSWDSIFGDIEQIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNIMDWLAKMLGLPDFFLHHHPSSQGGGVLQRTVSESTLIALLAARKNKILEMKAHEPNADESSLNARLVAYASDQAHSSVEKAGLISLVKIKFLPVDDNFSLRGEALQKAIEEDKQQGLVPVFVCATLGTTGVCAFDKLSELGPICAREGLWLHVDAAYAGTAFLRPELRGFLKGIEYADSFTFNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSIKLWFVIRSFGVKNLQAHVRHGTDMAKYFESLVRSDPVFEIPAERHLGLVVFRLKGPNCLTESVLKEIAKTGQVFLIPATIQDKLIIRFTVTSQFTTKDDILRDWNLIREAANLVLSQHCTSQPSPRAKNLIPPPVTRDSKDLTNGLSLESVNEGGDDPVQVRKIFRLPGDSLETTMDPFDDCFSEEASDTTKHKLSSFLFSYLSVQNKKKTMRSLSCNSMPMSAQKSPPPDASVKHGGFFRARIFSGFPEEMMMMKKGGFKKLIKFYSVPSFPECSSQCGTLQLPCCPLQAMV | Function: Catalyzes the biosynthesis of histamine from histidine.
PTM: May be post-translationally processed.
Catalytic Activity: H(+) + L-histidine = CO2 + histamine
Sequence Mass (Da): 73636
Sequence Length: 656
Pathway: Amine and polyamine biosynthesis; histamine biosynthesis; histamine from L-histidine: step 1/1.
EC: 4.1.1.22
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O87873 | MSEASSPLKVWLERDGSLLRLRLARPKANIVDAAMIAAMRQALGEHLQAPALRAVLLDAEGPHFSFGASVDEHMPDQCAQMLKSLHGLVREMLDSPVPILVALRGQCLGGGLEVAAAGNLLFAAPDAKFGQPEIRLGVFAPAASCLLPPRVGQACAEDLLWSGRSIDGAEGHRIGLIDVLAEDPEAAALRWFDEHIARLSASSLRFAVRAARCDSVPRIKQKLDTVEALYLEELMASHDAVEGLKAFLEKRSANWENR | Function: Catalyzes the hydration of cyclohexa-1,5-diene-1-carboxyl-CoA.
Catalytic Activity: cyclohexa-1,5-diene-1-carbonyl-CoA + H2O = 6-hydroxycyclohex-1-ene-1-carbonyl-CoA
Sequence Mass (Da): 27882
Sequence Length: 258
Pathway: Aromatic compound metabolism; benzoyl-CoA degradation.
EC: 4.2.1.100
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Q9FHR8 | MTMESYKTLEIIRKNTDSSVFHLIINRPSHLNALSLDFFIEFPKALSSLDQNPDVSVIILSGAGKHFCSGIDLNSLSSISTQSSSGNDRGRSSEQLRRKIKSMQAAITAIEQCRKPVIAAIHGACIGGGVDLITACDIRYCSEDAFFSIKEVDLAIVADLGTLQRLPSIVGYANAMELALTARRFSGSEAKDLGLVSKVFGSKSELDNGVTTIAEGIGGKSPLAVTGTKAVLLRSREVSVEQGLDYVATWNSAMLISDDLNEAVSAQMMKRKPRFAKL | Function: Converts 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in degradation of unsaturated fatty acids.
Catalytic Activity: a (3E,5Z)-dienoyl-CoA = a (2E,4E)-(5,6-saturated)-dienoyl-CoA
Sequence Mass (Da): 29920
Sequence Length: 278
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Peroxisome
EC: 5.3.3.21
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Q08558 | MSSRVCYHINGPFFIIKLIDPKHLNSLTFEDFVYIALLLHKANDIDSVLFTVLQSSGKYFSSGGKFSAVNKLNDGDVTSEVEKVSKLVSAISSPNIFVANAFAIHKKVLVCCLNGPAIGLSASLVALCDIVYSQNDSVFLLFPFSNLGFVAEVGTSVTLTQKLGINSANEHMIFSTPVLFKELIGTIITKNYQLTNTETFNEKVLQDIKQNLEGLYPKSVLGMKELLHSEMKQKLIKAQAMETNGTLPFWASGEPFKRFKQLQEGNRRHKL | Function: Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs . Required for ECI1 to be locazed to the peroxisome .
Catalytic Activity: a (3E,5Z)-dienoyl-CoA = a (2E,4E)-(5,6-saturated)-dienoyl-CoA
Sequence Mass (Da): 30058
Sequence Length: 271
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Peroxisome
EC: 5.3.3.21
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P51852 | MKLAEALLRALKDRGAQAMFGIPGDFALPFFKVAEETQILPLHTLSHEPAVGFAADAAARYSSTLGVAAVTYGAGAFNMVNAVAGAYAEKSPVVVISGAPGTTEGNAGLLLHHQGRTLDTQFQVFKEITVAQARLDDPAKAPAEIARVLGAARALSRPVYLEIPRNMVNAEVEPVGDDPAWPVDRDALAACADEVLAAMRSATSPVLMVCVEVRRYGLEAKVAELAQRLGVPVVTTFMGRGLLADAPTPPLGTYIGVAGDAEITRLVEESDGLFLLGAILSDTNFAVSQRKIDLRKTIHAFDRAVTLGYHTYADIPLAGLVDALLEGLPPSDRTTRGKEPHAYPTGLQADGEPIAPMDIARAVNDRVRAGQEPLLIAADMGDCLFTAMDMIDAGLMAPGYYAGMGFGVPAGIGAQCVSGGKRILTVVGDGAFQMTGWELGNCRRLGIDPIVILFNNASWEMLRTFQPESAFNDLDDWRFADMAAGMGGDGVRVRTRAELKAALDKAFATRGRFQLIEAMIPRGVLSDTLARFVQGQKRLHAAPRE | Cofactor: Binds 1 metal ion per subunit.
Catalytic Activity: H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde
Sequence Mass (Da): 57981
Sequence Length: 545
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 4.1.1.74
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P23234 | MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTAAQQRGELLHHTLGDGEFRHFYHMSEPITVAQAVLTEQNACYEIDRVLTTMLRERRPGYLMLPADVAKKAATPPVNALTHKQAHADSACLKAFRDAAENKLAMSKRTALLADFLVLRHGLKHALQKWVKEVPMAHATMLMGKGIFDERQAGFYGTYSGSASTGAVKEAIEGADTVLCVGTRFTDTLTAGFTHQLTPAQTIEVQPHAARVGDVWFTGIPMNQAIETLVELCKQHVHAGLMSSSSGAIPFPQPDGSLTQENFWRTLQTFIRPGDIILADQGTSAFGAIDLRLPADVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYTVERAIHGAEQRYNDIALWNWTHIPQALSLDPQSECWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGALTKALEACNNA | Cofactor: Binds 1 metal ion per subunit.
Catalytic Activity: H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde
Sequence Mass (Da): 60024
Sequence Length: 552
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 4.1.1.74
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Q5ZJM7 | MSAPAKRRCRGPAADLDSSFQKRLRKISIEGNIAAGKSTLVRLLEKHSDEWEVIPEPIAKWCNIQTSEDECKELSTSQKSGGNLLQMLYDKPTRWAYTFQTYACLSRVRAQLKPISAKLHEAEHPVQFFERSVYSDRYVFASNLFESGNINETEWAIYQDWHSWLLNQFQSEIELDGIIYLRTTPQKCMERLQKRGRKEEEGIDLEYLENLHYKHETWLYEKTMRVDFENLKEIPILVLDVNEDFKNDKIKQEYLIDEIKSFLTS | Function: Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine . Shows highest activity against deoxyguanosine followed by deoxycytidine and then deoxyadenosine . Shows only very minor activity against deoxyuridine and deoxythymidine .
Catalytic Activity: 2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a ribonucleoside 5'-diphosphate + dCMP + H(+)
Sequence Mass (Da): 31240
Sequence Length: 265
Subcellular Location: Nucleus
EC: 2.7.1.74
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Q12517 | MTGAATAAENSATQLEFYRKALNFNVIGRYDPKIKQLLFHTPHASLYKWDFKKDEWNKLEYQGVLAIYLRDVSQNTNLLPVSPQEVDIFDSQNGSNNIQVNNGSDNSNRNSSGNGNSYKSNDSLTYNCGKTLSGKDIYNYGLIILNRINPDNFSMGIVPNSVVNKRKVFNAEEDTLNPLECMGVEVKDELVIIKNLKHEVYGIWIHTVSDRQNIYELIKYLLENEPKDSFA | Function: Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body. DCP1 is activated by the DEAD-box helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the mRNA.
PTM: Phosphorylated.
Sequence Mass (Da): 26266
Sequence Length: 231
Subcellular Location: Cytoplasm
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Q8GW31 | MSGLHRSSSSSKNIGNCLPSKELLDDLCSRFVLNVPEEDQQSFERILFLVEYAYWYYEDNAVENDPKLKSLSLKEFTSLLFNSCDVLRPYVTHIDDIFKDFTSYKCRVPVTGAIILDETYERCLLVKGWKGSSWSFPRGKKSKDEEDHACAIREVLEETGFDVSKLLKREEYIEFVFRQQRVRLYIVAGVTEDTVFAPLTKKEISEITWHRLDHLQPASNEVITHGVSGLKLYMVAPFLSSLKSWILKHPSPVARRPNKPLKALCVWNARTSVGGNGTATVESQNRKSELRTTTMESNSRKPELKRTTMESHSTKPELRKGTMESHNTTATVESHNTKPVVDHSQDIKPGGSFINFKFNQSVILQALESGNSA | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Essential for postembryonic development, especially during the formation of the shoot apical meristem (SAM).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP
Sequence Mass (Da): 42387
Sequence Length: 373
Subcellular Location: Cytoplasm
EC: 3.6.1.62
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Q75BK1 | MSLPLRNPLDSVSLERALEDLIVRFIINVPPEDLATVERELFHFEEAQWFYTDFVKLTNPHLPNMKFKTFASYVISLCPLVWKWQDVNPEEALQKFSKYKKSIPVRGAAIFNETLNKILLVKGTESDSWSFPRGKISKDEDDVDCCIREVMEEIGFDLTNYVLEDQYIERNIGGKNYKIYLVKGVPQDFAFKPQVRNEIEKIEWRDFWKLSRSIHKSNNKFYLVSSMVKPLSLWVKKQKQIQGEEQLKQYAEEQLKLLLGIGTQEEAADPGRDLLNMLQSSVGQKKPLVFSDDESQASISTSAPTTVPPAPSTANSQSVQPIAAGAYAGYPFPFPQYPIPGMQTINPFQFVQSSHQGVFATHSTFTTSHQYPQAQAPQTQQPVPGAVVYPVQSQLQQAYQPPHTPVVKPSVIEDRAPHSKQLLELLKNPRKPEVEDESTAKTLLKLLKNPTKENRTSANTVPSSKGAVSGPSGGRSISGQSIDTANLPSGMASSMGAKSTAIPLYSPRSSLSEMTLPDEPLGGYEEFESSSEEEQGEELAYMNLQEPTSSVMESNAKVENNTLDNISHVDTSGNLSTRSLQSEKTEKSKPTAKPKIKLLKRGETLTPLTPSISSQTATSESSAAGPTVPSEKDVSSRIQNSQGNELLDVLKSKAQPEPSVASTSPAKELLNTLNKPQGSVYQNLLFGANHRKSDDESSPRHSPVSQQARTHEFLNLLKRPQAKAENEELQSVLLTPPANSGMVQNSSTLPNIPYGNLHQDQAAALLFPQQPPQFQQPYAATNTNSKELLAILRKPASNQQKQLHEQTPANPVDQPTTLASEQQNLVKQQISNPSQSLQQGTPLQQPQPQHTQSPSNLHVTGNTAAAQELLGMLRKSRVVP | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body (By similarity).
Sequence Mass (Da): 97262
Sequence Length: 880
Subcellular Location: Cytoplasm
EC: 3.-.-.-
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O62255 | MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPSSSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASLNEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSPNHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPSTEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINREETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP | Function: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs . Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP . RNA-decapping enzyme although it does not bind the RNA cap . May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs . In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia . Required for the developmental axon guidance and regrowth of PLM touch receptor neurons . Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons . Promotes survival at high temperatures .
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP
Sequence Mass (Da): 87369
Sequence Length: 786
Subcellular Location: Cytoplasmic granule
EC: 3.6.1.62
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Q8IU60 | METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKPYNNHSEMSDLLKGKNQSMRGNGRKQYQDSPNQKKRTNGLQPAKQQNSLMKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAEGQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL | Cofactor: Mn(2+) ion is required for highest activity. Can also utilize magnesium ions.
Function: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs . Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP . Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay . Plays a role in replication-dependent histone mRNA degradation . Has higher activity towards mRNAs that lack a poly(A) tail . Has no activity towards a cap structure lacking an RNA moiety . The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping . Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts .
PTM: Phosphorylated at ser-249 in a MTOR-dependent manner .
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP
Sequence Mass (Da): 48423
Sequence Length: 420
Subcellular Location: Cytoplasm
EC: 3.6.1.62
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O13828 | MSFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRAQNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGAIMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFDCSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNLMDLPTFKKNKPQTMKNKFYMVIPFLAPLKKWIKKRNIANNTTKEKNISVDVDADASSQLLSLLKSSTAPSDLATPQPSTFPQPPVESHSSFDIKQKILHLLNEGNEPKSPIQLPPVSNLPLNPPIQSSNSRLSHDNNSFDPFAYLGLDPKNPSASFPRVVSQNNMLTNKPVLNNHFQQSMYSNLLKDQNSVQHLFAASDMPSPMELPSPSTVYHQVFYPPTSTSVSSYGLGKTPQPAYGSSSPYVNGHQTQQISSLPPFQSQTQFLARNSDNSGQSYNSEGDSNSKRLLSMLSQQDTTPSSSTLSKEANVQLANLFLTPNSLETKKFSDNSQGEEISDNLHGESCNNPNANSVHSAQLLQALLHPSATETKEETPKKTSDSLSLLTLLKSGLPTPANDLQNKSQNNERKASSQVKELEVKNYSKSTDLLKKTLRIPRNDEPLEAANQFDLLKVSPQQKSEVPPKRNELSQSKLKNRKKKENSETNKNHVDMSPGFVKILKRSPLADQKKEDTQESDFKGSDDHFLSYLQSVVSSNSNGLH | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.
Sequence Mass (Da): 83234
Sequence Length: 741
Subcellular Location: Cytoplasm
EC: 3.-.-.-
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P53550 | MSLPLRHALENVTSVDRILEDLLVRFIINCPNEDLSSVERELFHFEEASWFYTDFIKLMNPTLPSLKIKSFAQLIIKLCPLVWKWDIRVDEALQQFSKYKKSIPVRGAAIFNENLSKILLVQGTESDSWSFPRGKISKDENDIDCCIREVKEEIGFDLTDYIDDNQFIERNIQGKNYKIFLISGVSEVFNFKPQVRNEIDKIEWFDFKKISKTMYKSNIKYYLINSMMRPLSMWLRHQRQIKNEDQLKSYAEEQLKLLLGITKEEQIDPGRELLNMLHTAVQANSNNNAVSNGQVPSSQELQHLKEQSGEHNQQKDQQSSFSSQQQPSIFPSLSEPFANNKNVIPPTMPMANVFMSNPQLFATMNGQPFAPFPFMLPLTNNSNSANPIPTPVPPNFNAPPNPMAFGVPNMHNLSGPAVSQPFSLPPAPLPRDSGYSSSSPGQLLDILNSKKPDSNVQSSKKPKLKILQRGTDLNSIKQNNNDETAHSNSQALLDLLKKPTSSQKIHASKPDTSFLPNDSVSGIQDAEYEDFESSSDEEVETARDERNSLNVDIGVNVMPSEKDSRRSQKEKPRNDASKTNLNASAESNSVEWGPGKSSPSTQSKQNSSVGMQNKYRQEIHIGDSDAYEVFESSSDEEDGKKLEELEQTQDNSKLISQDILKENNFQDGEVPHRDMPTESNKSINETVGLSSTTNTVKKVPKVKILKRGETFASLANDKKAFDSSSNVSSSKDLLQMLRNPISSTVSSNQQSPKSQHLSGDEEIMMMLKRNSVSKPQNSEENASTSSINDANASELLGMLKQKEKDITAPKQPYNVDSYSQKNSAKGLLNILKKNDSTGYPRTEGGPSSEMSTSMKRNDATNNQELDKNSTELLNYLKPKPLNDGYENISNKDSSHELLNILHGNKNSSAFNNNVYATDGYSLASDNNENSSNKLLNMLQNRSSAINEPNFDVRSNGTSGSNELLSILHRK | Function: Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay . Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP . Decapping is the major pathway of mRNA degradation in yeast and occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body . Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts .
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP
Sequence Mass (Da): 108667
Sequence Length: 970
Subcellular Location: Cytoplasm
EC: 3.6.1.62
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D3K0N9 | MVDEVDANSTGDNSLVNMKGFSFKEVLGSDSARKSAFILLDSSNGENAILLADKNAFPVDKTSWSAILTGSTLKPIMKNDIYSSYTLCMPNEFSDVKSTLIYPCNEKHIAKYRDQKRFIINETPEDYRTITLPYIQRNQMSLEWVYNILDHKAEVDRIIYEETDPHDGFILAPDLKWSGEQLECLYVQALVRRKGIKSIRDLTANDLPLLEGIRDKGLNAIKEKYGLDKHQIRAYFHYQPSFYHLHVHFIHVSYEAPASGVAKAVLLDDVINNLKLIPDFYQRSTLTFTAKEQDPIYRREN | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs of the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 2 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to m(7)GMP and m3(2,2,7)GMP, respectively . May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by dcs-1 to m7GMP. Binds to m7GpppG and strongly to m7GDP.
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 34565
Sequence Length: 301
Subcellular Location: Nucleus
EC: 3.6.1.59
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Q8MJJ7 | MAELAHQQSKRKRELDAEEAEASSTEGEEAGVGNGTSAPVRLPFSGFRVKKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVDQVAQLLKGSPELQLQFSNDVYSTYHLFPPRQLSDVKTTVVYPATEKHLQKYLRQDLHLVRETGSDYRNVTLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIKSLRDLTAEHLPLLRNILREGQEAILRRYQVAADRLRVYLHYLPSYYHLHVHFTALGFEAPGAGVERAHLLAEVIDNLEQDPEHYQRRTLTFALRADDPLLALLQEAQRS | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP. Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death.
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 38402
Sequence Length: 337
Domain: The C-terminal histidine triad (HIT) motif and the N-terminal domain are required for the decapping activity. The N-terminus is necessary but not sufficient for binding cap structures.
Subcellular Location: Cytoplasm
EC: 3.6.1.59
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G5EFS4 | MKRIADEELVREERAEESTQKWLQDAKFQEILGADSSHKSLFVLLSHPDGSQGILLANKSPFSEEKSDIEKLLATAQLQEISRNDIFGSYNIEIDPKLNLLKSQLIYPINDRLIAKYRQEEKFVIRETPELYETVTRPYIEKYQLNLNWVYNCLEKRSEVDKIVFEDPDNENGFVLLQDIKWDGKTLENLYVLAICHRHGLKSVRDLTGDDLEMLYNMRDKSLEAINQKYGLKTDQIKCYFHYQPSFYHLHVHFINLKYDAPASTTMSAILLDDVINNLELNPEHYKKSTLTFTRKNGDKLMEMFREALKN | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs of the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 2 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to m(7)GMP and m3(2,2,7)GMP, respectively . May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by dcs-1 to m7GMP. Binds to m7GpppG and strongly to m7GDP.
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 36477
Sequence Length: 311
Subcellular Location: Nucleus
EC: 3.6.1.59
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Q96C86 | MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS | Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP . May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP . Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death.
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 38609
Sequence Length: 337
Domain: The C-terminal histidine triad (HIT) motif and the N-terminal domain are required for the decapping activity. The N-terminus is necessary but not sufficient for binding cap structures.
Subcellular Location: Cytoplasm
EC: 3.6.1.59
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Q99KJ8 | MADPKYADLPGIARNEPDVYETSDLPEDDQAEFDAEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGKTKRTGYESGDYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTPVVLAKQLAALKQQLVASHLEKLLGPDAAINLADPDGALAKRLLLQLEATKSSKGSSGGKATAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQGACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQNKVHQLYETIQRWSPVASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQVQTTMRENLATVEGNFASIDARMKRLGK | Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. In the dynactin soulder domain, binds the ACTR1A filament and acts as a molecular ruler to determine the length (By similarity). Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44117
Sequence Length: 402
Subcellular Location: Cytoplasm
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Q9Z716 | MSAFFDLLKSQTASHPPIWLLRQVGRYMPPYQELKGSQSLKTFFHNTEAIVEATLLGPSLLHVDAAILFADILSILDGFAVTYDFAPGPRIQFSPEQPFTFTSDPQTIFSYLLDAIRTLKQKLPVPLIVFAASPFTLACYLIDGGASKDFSKTMSFLYVYPEKFDQLISTIIEGTAIYLKTQMDAGAAAVQLFESSSLRLPSALFTRYVTEPNRRLIAKLKEQAIPVSLFCRCFEENFYTLQATQADTLHPDYHVDLHRIQKNLMLSLQGNLDPAIFLLPQEKLLHYVEAFLVPLRTYPNFIFNSGHGILPETPLENVQLVVSYVQRQL | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37166
Sequence Length: 329
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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Q8KAW2 | MLKNDLFIRALKRQATPRTPIWVMRQAGRYLPEYRAVREKTDFLTLCKTPELACEVTIQPVDLMGVDAAIIFSDILVVNEAMGMNVEIIETKGIKLTPPIRSQADIDKLIDPDIDEKLGYVLDAIRLAKKELNDRVPLIGFSGAAWTLFTYAVEGGGSKNYTWAKKMMYREPKMAHQLLQKISDCISAYLVKQVEAGADAIQIFDSWASALSEDDYREFALPYIKQNVAAVKAAYPEIPVIAFAKDMNTILSDIADCGADAVGLGWNIDIAKARKELNDRVCLQGNMDPTVLYGTPEKIKSEAAKVLKQFGQHNDHSGHVFNLGHGILPDVDPANLKCLVEFVKEESAKYH | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39104
Sequence Length: 351
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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A0M6C4 | MIKNDLLLKALKGESVERPPVWMMRQAGRYLPDFMKLKEKYDFFTRCRTPELATEITVMPIRQIGPDAAILFSDILVVPQAMNIEVEMKPGVGPWLPNPIDSPKKVEQVIVPDVNEELGYVFEAIKMTKQELNDEVPLIGFAGSPWTILCYCVQGQGSKTFDKAKRFCFMNPIAAHTLLQKITDTTIAYLKEKVKAGVDAVQLFDSWGGLLEPKDYQEFSWKYMQQIIEALKDEVPVIAYGKGCWFALDKMAKSGAAALGVDWTCEARNARYLSGGEITLQGNFDPARLYSKPIEIKYMVNDMIKAFGKDRYIANLGHGILPNIPVDNAKAFVDAVKEYKE | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 38434
Sequence Length: 341
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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Q6KZ54 | MNSFISMIRNGYSDTIPVWFMRQAGRYLKEYNEKKGRMTIKEICMDPELIAGISYDPVRILNVDAAIIFSDITIPLEALGYKIEFLPGGPRIINGYIKNHDMKDIIYFEESNFKYKIYDAIKIFKEKYHFPLIGFSGGLITVLSYIIAGGPDSNLNLTKRSMLSDDKFNDYINIIKDMIIKYIRLQVRAGVDAIQIFDSWLGYLSPQTYENYIKGHIEEILSEINVPVIYFSTGTSSIIEKLSRLNVDYISVDWRLDMKLARSMVNKKGLQGNLDPLIAAYNLRYALKETSDIINAAGRSSYIFNLGHGVIPETPVENLKHIVNFVHNFNQ | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37932
Sequence Length: 331
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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A1VJ58 | MFAPLQNDTFLRACLRQATDHTPVWLMRQAGRYLPEYKATRAKAGSFMGLATNTDYATEVTLQPLERYPLDAAILFSDILTVPDAMGLGLSFALGEGPRFATPVRDEAAVNKLEVPDMNKLRYVFDAVTSIRKALGGRVPLIGFSGSPWTLACYMVEGSGSDDYRLVKTMLYQRPDLMHKMLAINADAVALYLNAQIEAGAQAVMIFDSWGGVLADAAFHTFSLAYTARVLSQLKREHKGVTIPRLVFTKGGGQWLESMKQLDCEVLGLDWTVNLAKARALVGENGPNAKALQGNLDPNVLFANPAQIEAEVAAVLNSFGAPHTDLTQTGPTQIFNLGHGISQHTPPESVEVLVRAVHAHSRSLRKQQG | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 40223
Sequence Length: 369
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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Q5RDK5 | MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCEPTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLECLRDPEVVASELDYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVAAGAQALQLFESHAGHLGPQLFSKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN | Function: Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway. Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme. In vitro also decarboxylates pentacarboxylate porphyrinogen I.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 40721
Sequence Length: 367
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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A5F3N0 | MTELKNDRYLRALLKQPVDYTPVWMMRQAGRYLPEYRATRAQAGDFMALCKNAELASEVTLQPLRRFPLDAAILFSDILTIPDAMGLGLRFAAGEGPVFERPITCKADVDKIGIPDPEGELQYVMNAVRQIRKDLQGEVPLIGFSGSPWTLATYMVEGGSSKAFTKIKKMMYSEPTVLHALLDKLADSVISYLNAQIKAGAQAVMVFDTWGGVLTPRDYQQFSLQYMHKIVDGLIRENEGRRVPVTLFTKNGGMWLEQIAATGCDAVGLDWTINIADAKARVGDKVALQGNMDPSILYAPAPRIREEVASILAGFGQGGTGHVFNLGHGIHLDVPPENAGVFVEAVHELSKPYHP | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39048
Sequence Length: 355
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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Q8CWI5 | MQFFENDSYLRSALRKSVKRTPIWIMRQSGRYLKEYQSIKKQAKDFLSLCKTPDLSSKAALIPIKKFSLDAAIIFSDILILPYAMGMDVNFYENLGPSFLNPISSISDMKNLNVPDPEKNLKYVLDSIKIICKELDKKIPLIGFSGSPWTLACYMIEGKCNKIFSKIKKMIYQNSKELHFLLKKITNSIILYLNSQIIYGVNAIIIFDTWGGILTEEKYCEYSLHYMSLIIKNLFCKYKGNKIPVTIFTKNGGQWIKKIAKSGCDVIALDWSVDIEYARKQVNGKIAIQGNMDPFELYGSFSSIEEETNKILSKFGYNSGHIFSLGHGIYKDTPPENVNFLIESVHNLSKKYHKKNRFKK | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 41359
Sequence Length: 360
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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B3CM33 | MESNKPAIVRIIKQNKPNEKVPIWLMRQAGRSLPEYRKAVEKTSNFMEICYSIDLVVELTLQPIKRFDMDAAIIFSDILIIADVLGCDVNFVRGVGPIIKPVKSSEELKNSQEFETKTFPILNAIRKVRSQLSEEKSLIGFAGGPWTVASYIIEGGSSKTFSKVLHFCSLELEEVIKKITEATIIYLIKQIEFGADVIQLFDSNAGILQGELFERYVIKPTKEIVSAIKNKFPDFPIIGFPRSAGNLYKDYYEKTGVSAVSIDYNVPIEWAKANLKIPLQGNLNPSLLAYNKAEAIEEAKRIIDCFRGLPFIFNLGHGVLPDTPVENIAALVDLVRNY | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 37935
Sequence Length: 338
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.1.37
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Q15SS1 | MFAAQYIGNKSFNVVEGHAIAPQAGEVRLDVGYVGICGTDMHIYHGVMDQRVSIPQTIGHEISGVVAQIGEGVEGFTVGEKVVVRPLDWCGECPTCEAGLTHICQNLKFMGIDTPGAFQSSWTVKARTLHKLPAGVDLKQGALVEPLSVACHDVRRSRLKAGEKAVILGGGPIGQLVAAVAKSVGAEVLVSEPNDSRREFADELGVKSVNPMDTDLAAYVDQWTGTKGADVVFEVSGVLPAIQSMTQIAGRRGRIVMVAIHSTAPPIDLFQFFWKELELLGARVYEAADFDWAIELIASGQIDLKPFISSVSPLADIGSAFANMDGNPQGMKALVECNAEQ | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in the degradation of 3,6-anhydro-L-galactose, which is the major monomeric sugar of red macroalgae. Catalyzes the third step of the pathway, the NAD(+)-dependent oxidation of 2-dehydro-3-deoxy-L-galactonate (L-KDGal) to 3-deoxy-D-glycero-2,5-hexodiulosonate (L-DDGal).
Catalytic Activity: 2-dehydro-3-deoxy-L-galactonate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH
Sequence Mass (Da): 36373
Sequence Length: 341
EC: 1.1.1.389
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Q15SS0 | MLEKFSLEGKVALVTGCKRGIGKGIALGLAEAGADIIGVSASLALEGSDVENEVKALGRNFKGYQCDFSDRDALYAFIKEVKADFPKIDILVNNAGTILRAPAAEHGDDLWDKVIDVNLNSQFILSREIGKEMVARQSGKIIFTASLLTFQGGITVPGYAASKGAIGQLVMALSNEWAGKGVNVNAIAPGYIDTDNTQALREDSERSAAILGRIPQGRWGNPDDFKGPAVFLASDAASYVNGAILLVDGGWMGR | Function: Involved in the degradation of 3,6-anhydro-L-galactose, which is the major monomeric sugar of red macroalgae. Catalyzes the fourth step of the pathway, the reduction of 3-deoxy-D-glycero-2,5-hexodiulosonate (L-DDGal) to 2-dehydro-3-deoxy-D-gluconate (KDG).
Catalytic Activity: 2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-2,5-hexodiulosonate + H(+) + NADH
Sequence Mass (Da): 26864
Sequence Length: 254
EC: 1.1.1.127
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B2J6X9 | MSNVQASFEATEAEFRVEGYEKIEFSLVYVNGAFDISNREIADSYEKFGRCLTVIDANVNRLYGKQIKSYFRHYGIDLTVVPIVITEPTKTLATFEKIVDAFSDFGLIRKEPVLVVGGGLTTDVAGFACAAYRRKSNYIRVPTTLIGLIDAGVAIKVAVNHRKLKNRLGAYHAPLKVILDFSFLQTLPTAQVRNGMAELVKIAVVANSEVFELLYEYGEELLSTHFGYVNGTKELKAIAHKLNYEAIKTMLELETPNLHELDLDRVIAYGHTWSPTLELAPMIPLFHGHAVNIDMALSATIAARRGYITSGERDRILSLMSRIGLSIDHPLLDGDLLWYATQSISLTRDGKQRAAMPKPIGECFFVNDFTREELDAALAEHKRLCATYPRGGDGIDAYIETQEESKLLGV | Function: Catalyzes the conversion of sedoheptulose 7-phosphate to demethyl-4-deoxygadusol (DDG) . Involved in the synthesis of the mycosporine-like amino acid shinorine, a natural sunscreen compound that protects the cell against UV radiation .
Catalytic Activity: D-sedoheptulose 7-phosphate = (R)-demethyl-4-deoxygadusol + H(+) + H2O + phosphate
Sequence Mass (Da): 45646
Sequence Length: 410
EC: 4.2.3.154
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Q3M6C3 | MSIVQAKFEAKETSFHVEGYEKIEYDLVYVDGIFEIQNSALADVYQGFGRCLAIVDANVSRLYGNQIQAYFQYYGIELRLFPITITEPDKTIQTFERVIDVFADFKLVRKEPVLVVGGGLITDVVGFACSTYRRSSNYIRIPTTLIGLIDASVAIKVAVNHRKLKNRLGAYHASRKVFLDFSLLRTLPTDQVRNGMAELVKIAVVAHQEVFELLEKYGEELLRTHFGNIDATPEIKEIAHRLTYKAIHKMLELEVPNLHELDLDRVIAYGHTWSPTLELAPRLPMFHGHAVNVDMAFSATIAARRGYITIAERDRILGLMSRVGLSLDHPMLDIDILWRGTESITLTRDGLLRAAMPKPIGDCVFVNDLTREELAAALADHKELCTSYPRGGEGVDVYPVYQKELIGSVK | Function: Catalyzes the conversion of sedoheptulose 7-phosphate to demethyl-4-deoxygadusol (DDG) . Involved in the synthesis of the mycosporine-like amino acid shinorine, a natural sunscreen compound that protects the cell against UV radiation (By similarity).
Catalytic Activity: D-sedoheptulose 7-phosphate = (R)-demethyl-4-deoxygadusol + H(+) + H2O + phosphate
Sequence Mass (Da): 46172
Sequence Length: 410
EC: 4.2.3.154
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Q8GPG4 | MLRTTRRTLMQGASLVGAGLFAAGRGWALNRLEPIGDTLAEEYPYRDWEDLYRNEFTWDYVGKAAHCINCLGNCAFDIYVKDGIVIREEQLAKYPQISPDIPDANPRGCQKGAIHSTSMYEADRLRYPMKRVGARGEGKWQRISWDQATEEIADKIIDIYEKYGPGKLMTHTGSGNMSMMRMAAPYRFASLVGGVQLDIFTDVGDLNTGAHLAYGNALESFTSDAWFGADYIMFLLFNPVATRIPDAHFLWEAKWNGARVVSVAPDYNPSSIHSDLWMPIKQGADPFLAMSMVNVIIEGKLYNEAFMKEQTDLPILVRSDNGMLLREADLEEGGSDQVFYHWDSRTGAAVKVKGSMGSEEKTLVLGDVDPALEGSFEVGGIPVTTVFEKVRAEAAKYPPEETAAITGIGPGVVRAEAETFARAKKALLMTGFNIGRYSNGIYTSWALTLMLALTGHGGRTGGLDTSWIAWNQPALLELAFFDFKKLPRLEAGGLGEFVRGGMMEHSRQHYDNDKLKARTGFDLDELQEMIDESIDAGWMPYYGDMKGLISIADNKFRRNKNAEAYRERILEEVEELFVDINVRMDSTAQWADYLLPAAAHYEAWDLRSIAFHRFVNVFSRPVPPIGEAKSDWEIMEILTRKIQERAIARGITGYEDGDVTRDFATIHDDYTMDGTLMTDHDVVSWLVENGPEFAGATLEEGVERGFFVMGEDAGPTQKLRPSEPYHAFLQQTEGKEPYKTMTGRITFFVDHPRFVRLGATVPTARHHAGRDASNYPLNFFSPHTRWGIHSNWRSNKFMLRLQRGEPNIYISPQLAAAKGIADGAQVRVFNELSFFFAQAKFYPSLPPDTIMMEHGWEPHQFPNWRPMNVCMATLLQPLELVGGWGHLNFSLWHWNANQLAHESSVDIEPA | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Allows photoautotrophic growth on dimethyl sulfide (DMS) as the sole electron donor.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Catalytic Activity: dimethyl sulfide + 2 Fe(III)-[cytochrome c2] + H2O = dimethyl sulfoxide + 2 Fe(II)-[cytochrome c2] + 2 H(+)
Sequence Mass (Da): 102309
Sequence Length: 910
Subcellular Location: Periplasm
EC: 1.8.2.4
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Q8GPG1 | MPGFRFLLAATAAFLATSPALPLSADSLNAGNIRLVDPEETVPVIKIPDGIYLRTPNDPDDIIWARVPEFRVEMVMAPPVHPSVGLRYRDEYPEQDLVVQLARTSERFYVRLRWVDPTRDMSTLRDRFRDGAAIEFSESDDSVSYMMGTDAESPVNIWYWHPDGDRVESLAAGSPGSLTRLDRQPVTGASEYRTGHGPDDSQWIVVMSRPLASEGDHQVSFERDTIPVAFALWQGADAQRDGLKLVSLNWIFARMTPDAAPAPGN | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: May transfer electrons to the iron-sulfur centers of DdhB.
Sequence Mass (Da): 29499
Sequence Length: 265
Subcellular Location: Periplasm
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O46606 | MNYPGHGSPRSSERNGGRGGDGAAWELGSDTEPAFGGSVCRFDHLPVGEPGDDEVPLALLRGEPGLHLAPGAEDHNHHLALDPCLSDDNYDFSSAESGSSLRYYSEGESGGGGSSSSLHPPQQPLVPSNSGGGGAAGGGPGERKRTRPGGAAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQATGARARAQDPDGDHVCGPASPAGPASSSVEDEDEDRVCGFCPRIAGHGREMEELVNIERVCVRGGLYEVDVTQGECYPVYWNQSDKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLSRFRGQQMQESFDIEVSKPIDGKDAIHSFKLSRNHVDWHSVDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTTHIVFVVHGIGQKMDQGRIIKNTAMMREAARKIEERHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPNFEEKGGKVSIVSHSLGCVITYDIMTGWNPVRLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLREIEERLHGLKASSMTQTPALKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEYMKPSFLHPAKDPTSISENEGISTIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSASQPSETSRDSIEDEKKPVASPPMTTVATQTLPHSSSGFLDSALELDHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDNNVKPSLDPV | Function: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid . Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) . Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology. These dynamic changes may be due to PA hydrolysis at the mitochondrial surface (By similarity). May play a regulatory role in spermatogenesis or sperm function .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 2-acyl-sn-glycerol 3-phosphate + a fatty acid + H(+)
Sequence Mass (Da): 97576
Sequence Length: 875
Subcellular Location: Cytoplasm
EC: 3.1.1.111
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Q8NEL9 | MNYPGRGSPRSPEHNGRGGGGGAWELGSDARPAFGGGVCCFEHLPGGDPDDGDVPLALLRGEPGLHLAPGTDDHNHHLALDPCLSDENYDFSSAESGSSLRYYSEGESGGGGSSLSLHPPQQPPLVPTNSGGGGATGGSPGERKRTRLGGPAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQTTGARPQGGDRDGDHVCSPTGPASSSGEDDDEDRACGFCQSTTGHEPEMVELVNIEPVCVRGGLYEVDVTQGECYPVYWNQADKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLNCFRGQQMQENFDIEVSKSIDGKDAVHSFKLSRNHVDWHSVDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTTHIVFVVHGIGQKMDQGRIIKNTAMMREAARKIEERHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPDFEEKGGKVSIVSHSLGCVITYDIMTGWNPVRLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLKEIEERLHGLKASSMTQTPALKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEHMKPSFLNPAKEPTSVSENEGISTIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSTTQSSETSKDSMEDEKKPVASPSATTVGTQTLPHSSSGFLDSAYFRLQESFFNLPQLLFPENVMQNKDNALVELDHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDDDAKPNLDPI | Function: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid . Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (By similarity). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology . These dynamic changes may be due to PA hydrolysis at the mitochondrial surface . May play a regulatory role in spermatogenesis or sperm function .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 2-acyl-sn-glycerol 3-phosphate + a fatty acid + H(+)
Sequence Mass (Da): 100435
Sequence Length: 900
Subcellular Location: Cytoplasm
EC: 3.1.1.111
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O94830 | MSSVQSQQEQLSQSDPSPSPNSCSSFELIDMDAGSLYEPVSPHWFYCKIIDSKETWIPFNSEDSQQLEEAYSSGKGCNGRVVPTDGGRYDVHLGERMRYAVYWDELASEVRRCTWFYKGDKDNKYVPYSESFSQVLEETYMLAVTLDEWKKKLESPNREIIILHNPKLMVHYQPVAGSDDWGSTPTEQGRPRTVKRGVENISVDIHCGEPLQIDHLVFVVHGIGPACDLRFRSIVQCVNDFRSVSLNLLQTHFKKAQENQQIGRVEFLPVNWHSPLHSTGVDVDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIVDTVASEMNRIYTLFLQRNPDFKGGVSIAGHSLGSLILFDILTNQKDSLGDIDSEKDSLNIVMDQGDTPTLEEDLKKLQLSEFFDIFEKEKVDKEALALCTDRDLQEIGIPLGPRKKILNYFSTRKNSMGIKRPAPQPASGANIPKESEFCSSSNTRNGDYLDVGIGQVSVKYPRLIYKPEIFFAFGSPIGMFLTVRGLKRIDPNYRFPTCKGFFNIYHPFDPVAYRIEPMVVPGVEFEPMLIPHHKGRKRMHLELREGLTRMSMDLKNNLLGSLRMAWKSFTRAPYPALQASETPEETEAEPESTSEKPSDVNTEETSVAVKEEVLPINVGMLNGGQRIDYVLQEKPIESFNEYLFALQSHLCYWESEDTVLLVLKEIYQTQGIFLDQPLQ | Function: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane.
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+)
Sequence Mass (Da): 81032
Sequence Length: 711
Domain: SAM and DDHD domains together are required for phospholipid binding.
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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Q80Y98 | MSSGESHQEQLSQSDPSPSPNSCSSFELIDMDASSSYEPVSPHWFYCKVLDSKELWIPFNSEDSQQLEDAYGSGKDCNERIVPTDGGRYDVHLGERMRYAVYWDELPSEVRRCTWFYKGDKDNKYVPYSESFSQVLEDTYMLAVTLDEWKKKIESPNREIIVLHNPKLMVHYQPIAGSDEWGSTSTEQGRPRSVKRGVENIPVDIHCGEPLQIDHLVFVVHGIGPACDLRFRSIVQCVNDFRSVSLNLLQTHFKKAQENEQIGRVEFLPVNWHSPLHSTGVDIDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIVDTVASEMNRIYTLFLQRNPDFKGGVSIAGHSLGSLILFDILTNQKNSIGDIDSEKGSLSSAEDRGDASTLEEDLKKLQLSEFVTVFEKEKVDREALALCTDRDLQEMGIPLGPRKKILNHFSARKNSVSINRPAMSASEVNISKENGDYLDVGIGQVSVKYPRLNYKPEIFFAFGSPIGMFLTVRGLRRIDPNYKFPTCKGFFNIYHPFDPVAYRIEPMVAPGIEFEPMLIPHHKGRKRMHLELREGLTRMSMDLKNNLLGSLRMAWKSFTRGPYPALQASETAEETEAEPESSSEKSNEANTEEPPVEVKEEAPISVGMLNGGQRIDYVLQEKPIESFNEYLFALQSHLCYWESEDTVLLVLKEIYQTQGVFLDQPLQ | Function: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane (By similarity).
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+)
Sequence Mass (Da): 79577
Sequence Length: 699
Domain: SAM and DDHD domains together are required for phospholipid binding.
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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Q1EBV4 | MRITVMTAGEQIITLDVDSQETVENVKALLEVESNVPIQQQQLLYNGNEMGNSDKLSALGVKDDDLLMMMVSNASSGSATSAAGNDLGMNPDGSALNPAAFQQHIRGDSNLMGQLFQNDPELAQVISGSDLNKLQDVLRARHRQRSVLQRQKEEELALLYADPFDVEAQRKIEAAIRQKGIDENWEAALEHNPEGFARVIMLYVDMEVNGVPLKAFVDSGAQSTIISKSCAERCGLLRLMDQRYKGIAHGVGQTEILGRIHVAPIKIGNNFYPCSFVVLDSPNMEFLFGLDMLRKHQCTIDLKENVMTVGGGEVSVPFLQEKDIPSRFLDEERVPNDASSSGATVPSGFTEKKNNTVANPTSQQPKRQNTSEGPEFEAKIAKLVELGFSRDSVIQALKLFEGNEEQAAGFLFGG | Function: Receptor of ubiquitinated protein targeted to ubiquitin/proteasome-mediated proteolysis (UPP). Relatively weak affinity for both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains with a slight preference for 'Lys-48-'linked chains of three or more ubiquitin units.
Sequence Mass (Da): 45359
Sequence Length: 414
Subcellular Location: Cytoplasm
EC: 3.4.23.-
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Q754R2 | MNVTVSNEVTDELLGPFELSDDITLMDFMALIDFDENEQALWHNMRQLKSVDREKTLMQLGIVGESLVVVKAIKKKATEGSTTRASKASAKAAKAAAKAAAVARDTPAEQATTVSPVAQVPVAVSPAVTAAVPTQPTSPSGGPAAANDIITPEDEYIETFRKSLLNSPSLASNIPIPGVNQLIQDSQLFKQLIGPVLLHRRAQQQAANQMGTAQSEYVKLMSNPDDPSNQARISELINQQEIDEQLHKAMEYTPEVFASVNMLYINMEINGHPVKAFVDSGAQSTIMSTALAERTGLGRLVDKRFRGIARGVGKGEIIGRVHAAQVKIETQFIPCSFIVLDTNVDLLLGLDMLRRYQACVDLKENVLKIAGIVTPFLPEAEIPKHFDMDPSAEATNLPSTSPLGNQKAAPEARDAGVGSALLNRSTPATAERTHAEEDVRRLMDLGFSRAEVLKALDHSQGNAEYAAAFLFQ | Function: Probable aspartic protease. May be involved in the regulation of exocytosis. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control.
Sequence Mass (Da): 50975
Sequence Length: 472
Subcellular Location: Cytoplasm
EC: 3.4.23.-
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O51927 | MKKKIAVLLGGNSSERKISIKSGYAILQSLLRSGFNAYAIDTRDFPIMQLKKQGFDSAYIALHGTGGEDGSIQGILEYLNIPYTGSGIMSSAISLDKWRTKLLWKSLSLRVLPDIYLQKKDISKYTYSYILKKILKLKFPVVIKPNNAGSSIGITIVNHPDLLIDSINLAFNYSNNIIIEKFLKGTEYTVSILNKKVLPPIKIITKNNFYDYSSKYIESSTEYICPSGLNYQKEEELKKIVEIAWNSLGCKGCGRIDAILDNKDKFWLLEINTIPGMTHRSLVPMAAKSIGISFDELILKILKINK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34388
Sequence Length: 306
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q9JSZ9 | MQNFGKVAVLMGGFSSEREISLDSGTAILNALKSKGIDAYAFDPKETPLSELKAQGFQTAFNILHGTYGEDGAVQGALELLGIPYTGSGVAASAIGMDKYRCKLIWQALGLPVPEFAVLHDDTDFDAVEEKLGLPMFVKPAAEGSSVGVVKVKGKGRLKSVYEELKHFQGEIIAERFIGGGEYSCPVLNGKGLPGIHIIPATEFYDYEAKYNRNDTIYQCPSEDLTEAEESLMRELAVRGAQAIGAEGCVRVDFLKDTDGKLYLLEINTLPGMTGHSLVPKSAAVMGVGFADLCIEILKTAHVG | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32587
Sequence Length: 304
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q82VS0 | MNTRDVGKVAVLLGGRSAEREISLRSGQAVLAALQRSRVNAHAFDPAGQPLENLLQQGFDRVFIALHGRYGEDGSVQGALELMELPYTGSGILASALAMDKWRTKMIWQAAGINTPDYVMLDASSRFRDVADRLGLPLIIKPAREGSTLGLNKVDNEQDFRSAYQAAAEYDSLVLAEQFIQGIELTAAILDDMPLPLVRIDVAEGLYDYQAKYFSESTRYTCPSGLSAALTTRIQEQALYAHRILGCTGWSRVDLILDENEQPFFLETNTSPGMTDHSLVPMAAKAAGISFDELVVQILELSCEH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33442
Sequence Length: 305
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q2Y641 | MAGSHDFGKVAVLLGGRSAEREISLESGKAVLDALRSSGVDAHPFDPSEQHMDALLQQGYTRAHIALHGRYGEDGTVQGALELLGIPYTGSGVLASALAMDKWRTKLLWQSAGINTPRHILLDEQSDFDAVAKELGLPLIVKPSREGSTIGLSKVREAGEVAAAWHLAARHDAMVLAEQFIEGTELTASILGDVALPLVRIQVEGDLYDYQAKYLSDKTQYFCPSGVSEEQECLIRKQALQAHRLLGCEGWGRVDLILDKSGTPYFLEANTSPGMTTHSLVPMAAKAAGISFEELVLKILGLAHVG | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32910
Sequence Length: 306
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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Q3J792 | MIGRVDVKAWGKVVVLMGGYSAEREISLKSGTAVLQSLLRQGIEAHGIDVDKGVLTQLSKGQFTRAFIALHGRGGEDGVIQGVLETLNLPYTGSGVLGSALTMDKLRSKRLWRGMDLPTADFSVLTRDTNPALIAADLGLPLIVKPAREGSSLGMMKVESIEALQSAYREAVIFDTAVFAERWLPGAEYTAAILADRVLPLIRLETPRVFYDFEAKYHANTTRYFCPCGLSEKQEQDLQALALEAFQALGASGWGRVDLRCDEKAHPYLLEINTVPGMTDHSLVPMAAQAAGIEFDEMVLQILASSLERRMFQDGT | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34489
Sequence Length: 316
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A6Q3Z7 | MQYAVVFGGKSYEHEISIVSTIAIKDIIPGAIFIFLDGNRDFYLIEKADLKSNYFSSGNYKKSPKLELKKGGFYQKSLLKEKKIPADVVINLVHGADGEDGKLASLLEFFEIDYIGPRIEGSVISYSKLLTKLYAKECGIEVLPYQLLRKQDKKIIDFEYPVIIKPNHLGSSIGVSVVYDSSELEYALDVAFEFDDEVLIEPFIEGIEEYNLAGAKGQTFHFSKIEAVKKEKLLDFEKKYLDFGRSGEVKDASLNETLRLHIRNAFEKIYDPLFSGAIIRIDFFVRDGKLYLNEINPVPGSLANYLFGDFRAVLEDVAKHLPKSKNIVIDYRYINSIQSAKK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 38808
Sequence Length: 342
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.2.4
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A6NHG4 | MPFLELDTNLPANRVPAGLEKRLCAAAASILGKPADRVNVTVRPGLAMALSGSTEPCAQLSISSIGVVGTAEDNRSHSAHFFEFLTKELALGQDRFPTVLSTSPAAHGGPRCPGEIIEGKKSCLNEEALFIYFI | Function: May have lyase activity.
Sequence Mass (Da): 14195
Sequence Length: 134
Subcellular Location: Cytoplasm
EC: 4.1.1.-
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Q54Q94 | MNKDKSKQKPQKKENNNNNNKNNNNNNNKTENNKTNKDFTKNKFDKDAKIDKVDNKKIFHNRSSQKRIAKLKKIELQKKPLTLKLNEIKSIEQRLIDEAPQRGTNPLANISSTTATTTTTTATKNDKEKEKEYKIDYPSATDFKDLPISQLTLKALTESKFLKLTDIQRASLPHTLCGRDILGAAKTGSGKTLSFILPILETLWRNRWGRDDGIGAIVLSPTRELAIQIFDVLKAVGKYHTFSAGLIIGGRNVQQEKDKINAMNILIATPGRLLQHMDETYGFDCSNLKILVLDEADRILDLGFSKCLNSIVENLPRERQTLLFSATQTKSIRDLARLSLQEPEYISVYEKDITTTPQNLTQTLCVIPLEMKLNMLFSFIKTHLTSKIIVFFASCKQVRFAHETFKLLNPGTTLFPLHGKMKQWTRLEVFEDFCKKKAGTLFATDIAARGLDFPAVEWVIQVDCPDDIETYIHRVGRTARNDAPGQSITILLPSEKDGMVNLMEKQKMKFEILEPNPEKLVSIDSKLSSFLSEKTDLKYLAQKSFVSYLRSVYRQSNKEIFKIQELNINEFSKSLGLLGTPNIQFGKASADSKNKSFVVSNIQKQLKDKKSKGEKDIDSSDDDDDDEERNKIGNSDDEDSEDDSDFQDDSDDDNKKVTKQQPKTNIEKLFDRKNANVMSETYQKLRTKEEDEEDDSMFVVKRRDHDLDNLDIVKRLSRKENKEKNFINDPTKLKFQESTSVPKDGKLPTSYIEKVKSEVEKGDVQDKILLKERLKRKKLKLQSKELRKQSGGGATGDDEEESVAYFVPPGEKDPYENGENDSDDESNDDDVWGQEYNSDDDDDDEESESEEQPKPITKKRTLEDHEESALKFLKKNRI | Function: Probable ATP-dependent RNA helicase which may be involved in ribosome biogenesis.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 100358
Sequence Length: 878
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q13206 | MGKTANSPGSGARPDPVRSFNRWKKKHSHRQNKKKQLRKQLKKPEWQVERESISRLMQNYEKINVNEITRFSDFPLSKKTLKGLQEAQYRLVTEIQKQTIGLALQGKDVLGAAKTGSGKTLAFLVPVLEALYRLQWTSTDGLGVLIISPTRELAYQTFEVLRKVGKNHDFSAGLIIGGKDLKHEAERINNINILVCTPGRLLQHMDETVSFHATDLQMLVLDEADRILDMGFADTMNAVIENLPKKRQTLLFSATQTKSVKDLARLSLKNPEYVWVHEKAKYSTPATLEQNYIVCELQQKISVLYSFLRSHLKKKSIVFFSSCKEVQYLYRVFCRLRPGVSILALHGRQQQMRRMEVYNEFVRKRAAVLFATDIAARGLDFPAVNWVLQFDCPEDANTYIHRAGRTARYKEDGEALLILLPSEKAMVQQLLQKKVPVKEIKINPEKLIDVQKKLESILAQDQDLKERAQRCFVSYVRSVYLMKDKEVFDVSKLPIPEYALSLGLAVAPRVRFLQKMQKQPTKELVRSQADKVIEPRAPSLTNDEVEEFRAYFNEKMSILQKGGKRLEGTEHRQDNDTGNEEQEEEEDDEEEMEEKLAKAKGSQAPSLPNTSEAQKIKEVPTQFLDRDEEEEDADFLKVKRHNVFGLDLKDEKTLQKKEPSKSSIKKKMTKVAEAKKVMKRNFKVNKKITFTDEGELVQQWPQMQKSAIKDAEEDDDTGGINLHKAKERLQEEDKFDKEEYRKKIKAKHREKRLKEREARREANKRQAKAKDEEEAFLDWSDDDDDDDDGFDPSTLPDPDKYRSSEDSDSEDMENKISDTKKKQGMKKRSNSEVEDVGPTSHNRKKARWDTLEPLDTGLSLAEDEELVLHLLRSQS | Function: Putative ATP-dependent RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 100888
Sequence Length: 875
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
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F1R345 | MESKSGRFPFPFQPYPIQESFMEALYTALDQRKVGIFESPTGTGKSLSLICGALTWLRDYEEQRKQEAARLLEGQKDSDVVKEKNSNSGPPEPDWVSEFVQKKAERDMVNKLKDEELKRKKREERLEMIRHNAQLRYAMKRKADEDDEAVKLLQLSREGAEPETHSPEEEGLIVAEYESDDEATPKSRLCDDDNDDDDDLEEEHVTKIYYCSRTHSQLAQFVHEVQKSPYGDAVRLVNLGSRQNLCINPEVVRLGNVQMMNERCLEMQKNKHEKRQKASDSESKRSRGLAKATCVFSRFENLMAMKDEVLVKVRDVEQLIQHGRETHTCPYYSTRMSIPAAQVVVLPYQSLLHASTRKASGIKLKDQIVIIDEAHNLMDTISAIHSAEISGGQLCRAHSQLSQYCERYRSRLKAKNLMYIKQILFVLEGLVRTLGGKVGQNPNTQSCQTGSELLTINDFLFKAQVDNINLFKVQKYFEKSMISRKLCGFAEKYEGSGINTHSSSKNKENRRTEGLGRFLQTLQSKPTDVSEQQMAVEDKPIMASPMMLAESFLFALTNANKDGRVVIQRQACVAQSSLKFLLLNAAVHFAQILQECRAVIIAGGTMQPVADFKEQLLFSAGVTEERILEFSCGHVIPPENILPIVLCAGPSGQQLEFTFQTRDSPQMMEETGRVLSNLCNIVPGGVVCFFPSYEYEKRILGHWESTGILQRLQSKKKIFQEPKKASQVEQVLSEYSKCIQRCSNIGGGQTGALLFSVVGGKMSEGINFSDDLGRCIVMVGMPYPNIKSPELQEKMAYLDKHMPHVAGKSPGKALVESLCMKAVNQSIGRAIRHRGDYACIVLCDHRYARTGTLQKLPEWIRSSTHTHATFGPAFASARRFFLEKRQKATL | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage. Plays a role in the regulation of sister chromatid cohesion and mitotic chromosome segregation. Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner. Also plays a role in heterochromatin organization (By similarity). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery . Plays a role in embryonic development . Associates with chromatin at DNA replication fork regions. Binds to single- and double-stranded DNAs (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 100475
Sequence Length: 890
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q96FC9 | MANETQKVGAIHFPFPFTPYSIQEDFMAELYRVLEAGKIGIFESPTGTGKSLSLICGALSWLRDFEQKKREEEARLLETGTGPLHDEKDESLCLSSSCEGAAGTPRPAGEPAWVTQFVQKKEERDLVDRLKAEQARRKQREERLQQLQHRVQLKYAAKRLRQEEEERENLLRLSREMLETGPEAERLEQLESGEEELVLAEYESDEEKKVASRVDEDEDDLEEEHITKIYYCSRTHSQLAQFVHEVKKSPFGKDVRLVSLGSRQNLCVNEDVKSLGSVQLINDRCVDMQRSRHEKKKGAEEEKPKRRRQEKQAACPFYNHEQMGLLRDEALAEVKDMEQLLALGKEARACPYYGSRLAIPAAQLVVLPYQMLLHAATRQAAGIRLQDQVVIIDEAHNLIDTITGMHSVEVSGSQLCQAHSQLLQYVERYGKRLKAKNLMYLKQILYLLEKFVAVLGGNIKQNPNTQSLSQTGTELKTINDFLFQSQIDNINLFKVQRYCEKSMISRKLFGFTERYGAVFSSREQPKLAGFQQFLQSLQPRTTEALAAPADESQASTLRPASPLMHIQGFLAALTTANQDGRVILSRQGSLSQSTLKFLLLNPAVHFAQVVKECRAVVIAGGTMQPVSDFRQQLLACAGVEAERVVEFSCGHVIPPDNILPLVICSGISNQPLEFTFQKRELPQMMDEVGRILCNLCGVVPGGVVCFFPSYEYLRQVHAHWEKGGLLGRLAARKKIFQEPKSAHQVEQVLLAYSRCIQACGQERGQVTGALLLSVVGGKMSEGINFSDNLGRCVVMVGMPFPNIRSAELQEKMAYLDQTLSPRPGTPREGSGGEPVHEGRQPVHRQGHQAPEGFCQRSAPGPAICPAPCPGQAAGLDPSPCGGQSYLWPRHCCCAEVSPGEVGLFLMGNHTTAWRRALPLSCPLETVFVVGVVCGDPVTKVKPRRRVWSPECCQDPGTGVSSRRRKWGNPE | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis . Its double-stranded DNA helicase activity requires either a minimal 5'-single-stranded tail length of approximately 15 nt (flap substrates) or 10 nt length single-stranded gapped DNA substrates of a partial duplex DNA structure for helicase loading and translocation along DNA in a 5' to 3' direction . The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended up to 500 bp by the replication protein A (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC) complex activities . Shows also ATPase- and helicase activities on substrates that mimic key DNA intermediates of replication, repair and homologous recombination reactions, including forked duplex, anti-parallel G-quadruplex and three-stranded D-loop DNA molecules . Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage . Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity . Cooperates also with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation . Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner; and hence it may contribute in Okazaki fragment processing at DNA replication fork during lagging strand DNA synthesis . Its ability to function at DNA replication fork is modulated by its binding to long non-coding RNA (lncRNA) cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase activity and binding to DNA replicating regions . Also plays a role in heterochromatin organization . Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery . Plays a role in embryonic development and prevention of aneuploidy (By similarity). Involved in melanoma cell proliferation and survival . Associates with chromatin at DNA replication fork regions . Binds to single- and double-stranded DNAs .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 108313
Sequence Length: 970
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q6AXC6 | MADENQEIGGIHFPFPFPPYPIQKDFMAELYKVLEGGKIGIFESPTGTGKSLSLICGALSWLRDFEKKKLQAEALLLAPGSGPPSSEKNSLLTSSSCQEPTDTPRPAGEPDWVTEFVQKKEERDLVERLREEQVRRRKREERLKEVCQDGRLRFAAKRTKHEEEETEALLRLSREMLDAGTGPEQLEQLECGEEHLVLAEYESDEERRGSRVDEAEDDLEEEHITKIYYCSRTHSQLAQFVREVLKSPFGKETRLVSLGSRQTLCVNEDVKNLGSVQLMNDRCVDMQRSKREKNGTGEDKPKRKRQKIQTSCPFYNHEQMELLRDEILLEVKDMEQLVALGKEARACPYYGSRFAIPAAQLVVLPYPMLLHAATRQAAGIRLQGQVVIIDEAHNLIDTITNIHSTEVNGSQLCQAHSQLLQYMERYRKRLKAKNLMYIKQILYLLEKFVAVLGGNVKQNPTTQSLSQTGSELKSINDFLFQSQVDNINLFKVQRYLEKSMLSRKLFGFTECFGVVLPSLSDSQENRGLAGFQQFLKSLQSGPTEDSPEEGQAVALRPASPLMHIEAFLAALTTANQDGRVIVNRQGSVGQSSLKFLLLNPAVHFAQVVKECRAVVIAGGTMQPMSDFREQLLACSGVEAGRVVEFSCGHVIPPDNILPLIICSGPSNQQLEFTYQRRELPQMVEETGRILCNLCNVVPGGVVCFLPSYEYLRQVHAHWDKTGLLTRLSVRKKIFQEPKRASQVEQVLMAYSKCIMSCSHSEGHLTGALLLSVVGGKMSEGINFSDDLGRCVVMVGMPYPNIKSPELQEKMAYLNQTLPRTQGQPLPGTVLIENLCMKAINQSIGRAIRHQRDFASIVLLDHRYARPSILAKLPAWIRDRVEVKATFGPAFAAVRKFHREKSHPSLV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis. Its double-stranded DNA helicase activity requires either a minimal 5'-single-stranded tail length of approximately 15 nt (flap substrates) or 10 nt length single-stranded gapped DNA substrates of a partial duplex DNA structure for helicase loading and translocation along DNA in a 5' to 3' direction. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended up to 500 bp by the replication protein A (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC) complex activities. Shows also ATPase- and helicase activities on substrates that mimic key DNA intermediates of replication, repair and homologous recombination reactions, including forked duplex, anti-parallel G-quadruplex and three-stranded D-loop DNA molecules. Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage. Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity (By similarity). Cooperates also with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation . Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner; and hence it may contribute in Okazaki fragment processing at DNA replication fork during lagging strand DNA synthesis. Its ability to function at DNA replication fork is modulated by its binding to long non-coding RNA (lncRNA) cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase activity and binding to DNA replicating regions (By similarity). Plays also a role in heterochromatin organization . Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery (By similarity). Plays a role in embryonic development and prevention of aneuploidy . Involved in melanoma cell proliferation and survival. Associates with chromatin at DNA replication fork regions. Binds to single- and double-stranded DNAs (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 101968
Sequence Length: 906
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q54CE0 | MSYNSSNSGSGRYDDNRSGNSSYSSTSRGGSSYGNRSGSDRDYNRDGGSYNRDSSRDYNSSSGSGSGNGSSSYNKYPSSSSSSSSSSSTSSYGPSKGKDFQDSWGSSSTGTTNGYNGSSNGYNSSSNGYNSSNSSSSYGASNNGYNNSSGSSSSGSSGSSNGGSYNNSGSSNSNGYSKPTSNYSYSNGYTGPTTNYSSYSNGYSTPPTSTSTSSSSTTTTTTTTPSTSYNGGSTSYGYSTSGSSNGYGGYSQPPIPSYDPSSVSSYGAVTPASSSYNASVPGSSYGNSTYRSSGYGNQSYATTNSYGSSSYGSSGFYGNAKANTGSFGSALSPISWDLSKLPRFEKNFYLEHPDVSKFTQEEIEKFRASFQMTVKGREVPPPIMQFTQAPFPGYLMKEIIGAGFPNPTPIQSQAWPIALKGRDIIGLAKTGSGKTLAFLLPSIVHINAQPVLREDDGPIVLVLAPTRELALQIQEETNKFGGTSQISNTCVYGGASKHTQVAALKKGVEIVIATPGRLIDILESGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIISQIRPDRQTLMFSATWPKEVQALAHDFLTDHIQVHIGSTEITANHNVRQIVEVCQDFEKKERMLSFLGSVGRDEKVIVFAETRKGVDDLQRVLQFSGFKSIGIHGNKSQPERDFVLSQFKNGMVPIMIATDVASRGLDIKDIKYVVNYDFPNTIEVYIHRIGRTARAGASGVSYSLLTTDNARLANELIKVLTEAKQKIPIELSNLSVTPSTSSNTKKFSPYPTYSKRY | Function: Probable ATP-dependent RNA helicase which may be involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84021
Sequence Length: 785
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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P19109 | MLKLVQYIAPRVGGATPRPTACGWGNLLLISPRSGASSEKCITQRRHFLFSSASSSGTFASSSSLCTEQRQQFHGSRRNRETILFPSTYSSLQAQSQRAFRDSSKPDSDDYVDSIPKAEQRTRTRKSLFNDPDERTEEIKIEGVMAPHDRDFGHSGRGGRGGDRGGDDRRGGGGGGNRFGGGGGGGDYHGIRNGRVEKRRDDRGGGNRFGGGGGFGDRRGGGGGGSQDLPMRPVDFSNLAPFKKNFYQEHPNVANRSPYEVQRYREEQEITVRGQVPNPIQDFSEVHLPDYVMKEIRRQGYKAPTAIQAQGWPIAMSGSNFVGIAKTGSGKTLGYILPAIVHINNQQPLQRGDGPIALVLAPTRELAQQIQQVATEFGSSSYVRNTCVFGGAPKGGQMRDLQRGCEIVIATPGRLIDFLSAGSTNLKRCTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVKQLAEDFLGNYIQINIGSLELSANHNIRQVVDVCDEFSKEEKLKTLLSDIYDTSESPGKIIIFVETKRRVDNLVRFIRSFGVRCGAIHGDKSQSERDFVLREFRSGKSNILVATDVAARGLDVDGIKYVINFDYPQNSEDYIHRIGRTGRSNTKGTSFAFFTKNNAKQAKALVDVLREANQEINPALENLARNSRYDGGGGRSRYGGGGGGGRFGGGGFKKGSLSNGRGFGGGGGGGGEGRHSRFD | Function: As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, rRNA processing and miRNA processing, as well as transcription regulation (By similarity) . Plays a role in innate immunity. Specifically restricts bunyavirus infection, including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-independent manner .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 78548
Sequence Length: 719
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q23116 | MACKNPKKFFPIRKSPVLRDGAFKGKLVLVTGGGTGIGKAIATTFAHLRATVVIAARRMEKLEQTARDITKITGGTCEPFQMDIKDPGMVSDAFDKIDMKFGKVPEILVNNAAGNFIMATELLSSNAYGTIIDIVLKGTFNVTTELGKRCIQNKTGASITSITAGYARAGAPFIVPSAVSKAGVETMTKSLATEWSKYGLRFNAVSPGPIPTKGAWGRLNSGEMGDIAEKMKFLNPEGRVGSPEEVANLVAFISSDHMSFLNGAIIDLDGGQQHFNHGSHMGDFLHSWDHKNWEDAENLIRGRTGKEKA | Function: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Catalytic Activity: a (2E,4E)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-enoyl-CoA + NADP(+)
Sequence Mass (Da): 33263
Sequence Length: 309
EC: 1.3.1.124
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P18170 | MRLFSLLPLLALLVVQAAGQSEVTSDDPATDAGSTTNSTTDTKPRIPSQDEILGQMPSINPIRTGNPQMDAFYMMFPALGSLLKWGSLFPAYSILGAIPDNLQPTAAASKVVLVLADDATAKTRVARQNPPPNPLGQLMNWPALPQDFQLPSMDLGPQVGSFLAQLPAMPTVPGLLGAAAPVPAPAPAPAAAPPPAPAPAADPPAAPVPDAPQPAILGQAALQNAFTFFNPANFDASSLLGQSVPTFAPPNLDFVAQMQRQFFPGMTPAQPAAAGTDAQASDISEVRVRPEDPYSQEAQMKIKSALEMEQERQQQAQVKDQEQVPLLWFRMPTTQNQDATEEKTLEDLRVEAKLRAFERQVIAELRMLQKIELMAKQMRSSAAAQNGDSPYRISYPLSRTPIHKITRADIEQALRDDYVRRLVNKEAQRRARNSGINTQKANALKRQAKSQDQTLSKEDIVQIMAYAYRMANEQMESEKGKQDKVYAAYRTEQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMVQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQHDQQMAQQMAQQGLMMTEQRQRQWSEDQAKIQQAQQMAQQTPMMMPQMQQRQWTEDPQMVQQMQQRQWAEDQTRMQMAQQNPMMQQQRQMAENPQMMQQRQWSEEQTKIEQAQQMAQQNQMMMQQMQQRQWSEDQAQIQQQQRQMMQQTPMMMKERQWAEENPQSVQQQGPMMMQQQMPSMMQREVEDEDNKAEDDLVGEAGPQMPENEGTARHKVDALGVGGNKRKKSKSKSAPPTVINYYYAAPQRPVVQSYGTSYGGGGYGSNAYGVPRPVNSYQSQGYRAAVGNDEVDEMLRQHQTMARATHFRQ | Function: Required for proper assembly of the eggshell.
PTM: Proteolytic cleavage of isoform FC106 generates 2 further products, S80 and S60.
Sequence Mass (Da): 108371
Sequence Length: 950
Subcellular Location: Secreted
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Q8NJQ3 | MTITGQINSETLNNGVPIFAPPYRWSKHWPRFTDVNCITIRYRTDGSSIRQYIPDNLQIEETPIVTIMLLDFGFSVIGPYHELIHCVEVTYEGKKYNYSFLLILDNEEACIGGRELLGNPKVLGTIEFDRQNRPPTAFIHGRVLRPSNTVIADIHFKPLCLVLDAGESKTPITGLNLRLIPSLIPGAPPSVREYTNVDFTLQGGEVWEGVGSLNFPSNSEFEPLHKFPVLEYLSATYHRGAWVEQRLLNVYSF | Function: Decarboxylase; part of the Tox1B locus, one of the 2 loci that mediate the biosynthesis of T-toxin, a family of linear polyketides 37 to 45 carbons in length, of which the major component is 41 carbons, and which leads to high virulence to maize . One of the PKSs (PKS1 or PKS2) could synthesize a precursor, used subsequently by the other PKS as starter unit, to add additional carbons . Variability in the length of the final carbon backbone C35-47 could be achieved by varying the number of condensation cycles, or use of different starter or extender units or might be due to decarboxylation of the penultimate product, catalyzed by DEC1 . Additional proteins are required for the biosynthesis of T-toxin, including oxidoreductases RED1, RED2, RED3, LAM1 and OXI1, as well as esterase TOX9 .
Sequence Mass (Da): 28654
Sequence Length: 253
Pathway: Mycotoxin biosynthesis.
EC: 4.1.1.-
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Q6QGD6 | MIDYSGLRTIFGEKLPESHIFFATVAAHKYVPSYAFLRRELGLSSAHTNRKVWKKFVEAYGKAIPPAPPAPPLTLSKDLTASMSVEEGAALTLSVTATGGTGPYTYAWTKDGSPIPDASGATYTKPTAAAEDAGSYKVTVTDSKQVSKDSTTCAVTVNPTVPGG | Function: Decoration protein that binds asymmetrically to the center of each capsid protein hexamer after capsid expansion. Stabilizes the capsid and protects from DNA release.
Sequence Mass (Da): 17247
Sequence Length: 164
Domain: The N-terminus binds to the capsid proteins with high affinity and high cooperativity while the C-terminus displays an IG-like fold.
Subcellular Location: Virion
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Q9LTV6 | MDSPFKPDVVRGQVALITGGGSGIGFEISSQFGKHGASIAIMGRRKQVLDDAVSALRSLGIQAIGLEGDVRKQEDARRVVEATFQHFGKLDILVNAAAGNFLAAAEDLSPNGFRTVLDIDAVGTFNMCHAALKYLKKGAPGRDSSSGGGSIINISATLHYTASWYQIHVSAAKAAVDATTRNLALEWGTDYDIRVNGIAPGPIGGTPGMSKLVPEEIENKTREYMPLYKVGEKWDIAMAALYLSCDSGKYVSGLTMVVDGGLWLSKPRHLPKEAVKQLSRAVEKRSRAKPVGLPTSKL | Function: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity).
Catalytic Activity: a (2E,4Z)-dienoyl-CoA + H(+) + NADPH = a 4,5-saturated-(3E)-enoyl-CoA + NADP(+)
Sequence Mass (Da): 31796
Sequence Length: 298
Subcellular Location: Peroxisome
EC: 1.3.1.124
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Q8PCN7 | MIREIIRMGDKRLLRVAPPVTNLGSDELHALVADMFETMDAARGVGLAAPQIAVDLQLMVFGFEASERYPEAPAVPRTALANVQIEPLSDEMENGWEGCLSIPGLRAVIPRHRVIRYSGFAPDGTPIEREAEGFHARVVQHEYDHLVGRLYPSRIENFDTFGFEDVLSYDL | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 19106
Sequence Length: 171
EC: 3.5.1.88
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P35732 | MSTQFRKSNHNSHSSKKLNPALKSKIDTLTELFPDWTSDDLIDIVQEYDDLETIIDKITSGAVTRWDEVKKPAKKEKYEKKEQQHSYVPQQHLPNPEDDITYKSSNNSNSFTSTKHNSSNNYTQARNKKKVQTPRAHTTGKHVNLDKGKHVPSKPVSNTTSWAAAVSVDTKHDVPQDSNDNNNEELEAQGQQAQEKNQEKEQEEQQQQEGHNNKEEHKQIEQPSLSSKKTTSRTSASQPKKMSWAAIATPKPKAVKKTESPLENVAELKKEISDIKKDDQKSEASEEKVNEQETSAQEQEEETAEPSEENEDRVPEVDGEEVQEEAEKKEQVKEEEQTAEELEQEQDNVAAPEEEVTVVEEKVEISAVISEPPEDQANTVPQPQQQSQQPQQPQQPQQPQQPQQPQQQQQPQQPQQPQQQLQQQQQQQQQPVQAQAQAQEEQLSQNYYTQQQQQQYAQQQHQLQQQYLSQQQQYAQQQQQHPQPQSQQPQSQQSPQSQKQGNNVAAQQYYMYQNQFPGYSYPGMFDSQGYAYGQQYQQLAQNNAQTSGNANQYNFQQGYGQAGANTAAANLTSAAAAAAASPATAHAQPQQQQPYGGSFMPYYAHFYQQSFPYGQPQYGVAGQYPYQLPKNNYNYYQTQNGQEQQSPNQGVAQHSEDSQQKQSQQQQQQQPQGQPQPEVQMQNGQPVNPQQQMQFQQYYQFQQQQQQAAAAAAAAAQQGVPYGYNGYDYNSKNSRGFY | Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II . Also involved in telomere length regulation . Binds DNA .
PTM: Ubiquitinated at Lys-281 or Lys-288, and at Lys-328 or Lys-329. in a manner dependent on RSP5; ubiquitination accelerates its proteolytic processing by the proteasome.
Sequence Mass (Da): 83973
Sequence Length: 738
Domain: The C-terminal part appears to promote nuclear export.
Subcellular Location: Cytoplasm
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C5E4K0 | MSAQSRKSNSHNGKNSRVNPEIKFKLETLTELFPDWTNDDLIDLVHEYDDLETIIDKITSGAVTRWDEVKKPSKKERLEKRLEQQQQLQKEQQQHQLQQQHYHAQDLDGHHGGSSSHHHTKAGQGSGSRYSRDNNGTHSSSGGSNAKSKKQQQQQQQQQNGKPSLPSDNARAAISRGKPASGGGSWAAVASSDSKKHQQEEEEEEDQQQQRPESSPEEPSATTVQASETKTDGVEASASATSTAQSSTHATATASTGNAAHNEKPKKMSWAAIAAPKPKVVQKKQSSLNNVGGLKKEINEVAKETETPAAGQAQREPVSETNDKATNNQGKKADAQHEDTASKLSEQQQQQQEQLQAQQQEQQQTQQQDQSPIEFQSQGTNQEDTAQHNRPEEQKDTREITSNQVQIDEQEVAATSEPQEPSQTAQAVATEVNDGSKVKQQQQQPTVGVEAGKPQQQQQQEAYYQQQQQQQQQQQQQYFAQQQQYAQSQTPQHAPQQLSGQQAAVGQPNANANASANANAAAAATAAQQQYYMYQNQFPGYTYPGMFDSPSYAYGQQQAYQQPSQPSAQAGFGTGTASQYSIPQGYAAAPAADMTTASTATASPVAGHAQPQQQQPYGGSFLPYYAHFYQQSFPYAQPQYGMAGQYPYQVPKAGYNYYQPQRQTQGRNVQQGQQSPGHSPSQQGEDVQQQSQPTQQNQLQNGQQPLNPQQLQFQQYYQFQQQQQAAAAAAAAAAAQQGLPYGYTGYDYTSQASRGFY | Function: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA.
PTM: Ubiquitinated.
Sequence Mass (Da): 83228
Sequence Length: 757
Subcellular Location: Cytoplasm
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Q9H4E7 | MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLHIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKVEEGAFVKEHFDELCWTLTAKKNYRADSNGNSMLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKVLSSMSLEVSLGELEELLAQEAQVAQTTGGLSVWQFLELFNSGRCLRGVGRDTLSMAIHEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQLQPSCLCYFGSEECKEKRGIIPLDAHCCVEVLPDRDGKRCMFCVKTANRTYEMSASDTRQRQEWTAAIQMAIRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHRELQQALEGQLREAEQARASMQAEMELKEEEAARQRQRIKELEEMQQRLQEALQLEVKARRDEESVRIAQTRLLEEEEEKLKQLMQLKEEQERYIERAQQEKEELQQEMAQQSRSLQQAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKRPVTSSSFSGFQPPLLAHRDSSLKRLTRWGSQGNRTPSPNSNEQQKSLNGGDEAPAPASTPQEDKLDPAPEN | Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42 . Can regulate cell morphology in cooperation with activated RAC1 (By similarity). Involved in immune homeostasis by ensuring proper trafficking and availability of T-cell regulator CTLA-4 at T-cell surface . Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling (By similarity).
PTM: Tyrosine-phosphorylated by tyrosine-protein kinase LCK in response to T-cell activation.
Sequence Mass (Da): 73910
Sequence Length: 631
Domain: The PH domain is essential for phosphatidylinositol 3,4,5-trisphosphate binding.
Subcellular Location: Cytoplasm
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P80571 | GFGCPNNYQCHRHCKSIPGRCGGYCGGWHRLRCTCYRCGGRREDVEDIFDIFDNEAADRF | Function: Active against both Gram-positive and Gram-negative bacteria but is not cytotoxic towards human erythrocytes or protozoa .
PTM: The hydroxylation of the Trp-28 is not important for the antibacterial activity.
Sequence Mass (Da): 6920
Sequence Length: 60
Subcellular Location: Secreted
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Q88VB2 | MIKMRDIIREGNHTLRAEAKQVKFPLSEADQKLANDMMEYLENSQDPELAKKYGLRAGVGLAAPQVDVSEQMAAVLVPSENEDDEPVFKDVIINPVIISHSVQPGALTEGEGCLSVDRDIAGYVIRHDRITLRYYNMAGEEKKIRLKNYPAIVCQHEIDHLHGILFYDHINGDNPFAADDDLVLIS | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 20855
Sequence Length: 186
EC: 3.5.1.88
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Q72S74 | MSVRKILRMGDPILRKISEPVTEDEIQTKEFKKLIRDMFDTMRHAEGVGLAAPQIGILKQIVVVGSEDNERYPGTPDVPERIILNPVITPLTKDTSGFWEGCLSVPGMRGYVERPNQIRMQWMDEKGNQFDETIDGYKAIVYQHECDHLQGILYVDRLKDTKLFGFNETLDSSHNVLD | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 20379
Sequence Length: 178
EC: 3.5.1.88
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Q0AXL3 | MSVYQVITVPNDILRGKALPVKEINAGVLRVLDNMRDTMYAADGVGLAAPQIGIPKRMIVVDIGENLLELINPEILKQEGNQLGSEGCLSVPGIVGRVNRAKKVLVKGLDRNGQELNFAAVDLLAKVLQHEIDHLEGILFIDKAIETRIEKL | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 16598
Sequence Length: 152
EC: 3.5.1.88
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P96113 | MYRIRVFGDPVLRKRAKPVTKFDENLKKTIERMIETMYHYDGVGLAAPQVGISQRFFVMDVGNGPVAVINPEILEIDPETEVAEEGCLSFPEIFVEIERSKRIKVKYQNTRGEYVEEELEGYAARVFQHEFDHLNGVLIIDRISPAKRLLLRKKLMDIARTVKR | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 19024
Sequence Length: 164
EC: 3.5.1.88
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B0KA11 | MAIRYVRKIGDEVLRKKAKPVTEINSHILTILEDMAQTMYLNDGVGLAANQIGVLRRLVVIDVGEGLLELINPEIVYEEGEQVGAEGCLSIPGVVGEVKRPKKVKVKYLDREGKEREIEGEDLLARALCHEIDHLNGVLFIDKAIRFLDEEEKEQVKEV | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 17874
Sequence Length: 159
EC: 3.5.1.88
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B9L0C1 | MAVRTIITEGDPRLRQKAIRIRVVDEEVRQLARDLWDTVRAARGLGLAAPQIGVLRRIIVVAIPPDYVEEGDPGVELTLINPEIVRASGRQVGLEGCLSIPGWYGEVPRSMHVTVKALDLDGREVRVKGSGLLARVLQHEIDHLEGILFVDRIEDRSTLRYIPDEEEETAEAATGT | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 19517
Sequence Length: 176
EC: 3.5.1.88
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Q72H33 | MVYPIRLYGDPVLRRKARPVEDFSGIKRLAEDMLETMFEAKGVGLAAPQIGLSQRLFVAVEYADEPEGEEERPLRELVRRVYVVANPVITYREGLVEGTEGCLSLPGLYSEEVPRAERIRVEYQDEEGRGRVLELEGYMARVFQHEIDHLDGILFFERLPKPKREAFLEANRAELVRFQKEARALLKELSQG | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 22092
Sequence Length: 192
EC: 3.5.1.88
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B5YIL7 | MAILEIKKYPDEVLKKKAETISEINGDLQKLIDNMIETMYNANGIGLAAPQVGVLKRLIVVDTSPREQNQSLIVLINPEITDSEGEILSEEGCLSLPGFTTRLKRKERVIVKGLDRNGKEIEIEATGLLARALQHEIDHLDGILLIDKISPLKRELFRKKFKTKK | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Mass (Da): 18570
Sequence Length: 165
EC: 3.5.1.88
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Q0KBD2 | MNVLITGGAGFLGLQLARLLLQRGTLNLDGQPVAIKRLTLLDVVAPQGLDDARVRVVTGDLSDPAVLRQAIDTDTGAVFHLAAVVSGQAEADFDLGMRVNLDASRALLETCRELGHQPRVLFTSSVAVYGGQLPPVVQDDTALNPQSSYGVQKAIGELLLSDYSRRGFVDGRVLRLPTISVRPGKPNAAASSFASGIIREPLSGVAANCPVAPETPLWLLSPRAAVAALVNGIELAGERLGNRRVVNLPGLSVTAAGMIEALRRVAGNAVADRVTWEREARVENIVGTWPAAWNAERALALGFQSDASFDEVIRAYMEDAGLAK | Function: Catalyzes oxidation of D-erythronate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+).
Catalytic Activity: D-erythronate + NAD(+) = 2-dehydro-D-erythronate + H(+) + NADH
Sequence Mass (Da): 34270
Sequence Length: 324
EC: 1.1.1.410
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P44094 | MKVVITGGQGFLGQRLAKTLLAQNNVHIDDLILIDVVKPIAPNNDPRVRCYEMNLRYPTGLDELITEETDAIFHLAAIVSSHAEQDPDLGYETNFLATRNILEICRKNNPKVRFIFSSSLAIFGGELPETILDSTAFTPQSTYGTQKAMCELLINDYSRKGFVDGIVVRLPTICIRPGKPNKAASSFVSSIMREPLHGEDAVCPVSEELRLWLSSPNTVVANFIHALQLPSLPLRSWHTINLPGFSVTVKQMLSDLTQVKGEAILEHIKFEFDESINNIVASWPSRIDNTQALALGFKVDSNFQNVIQQFIEYDM | Function: Catalyzes oxidation of D-erythronate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+).
Catalytic Activity: D-erythronate + NAD(+) = 2-dehydro-D-erythronate + H(+) + NADH
Sequence Mass (Da): 35145
Sequence Length: 315
EC: 1.1.1.410
|
P50617 | MLDGPLFSEGPDSPRELQDEESGSCLWVQKSKLLVIEVKTISCHYSRRAASRQSMDIQASYWARGPQNRTCRLRPGSPEPPPRRPWASRVLQEATNWRAGPPAEVRAREQEKRKAASQEREAKETERKRRKAGGARRSPLGQPRPELRNALRAAQPTGFPVFSRPERFGQVGRAPRPSALPQGDPGVAWAGPWGGRRPGPPSYEAHLLLRGAAGTAPRRRWDRPPPYVAPPSYEGPHRTLGTKRGPELSRAPTSSAPVPATTRTEGGRTKKRLDPRIYRDVLGAWGLRQGRGLLGGAPGCAAARARPESCKGAVEKSSGLAAAGLNSGGDGHSQAKTTGPVTEVALSGSTISSPPRPVPRSRQHLRGSRKGKEGSEEMWLPTCWLSSPKKPPVRHSQTLPRPWAPGGTGWKESLGQREGTEHETLEVWKVTRRAHTLPRSSRGPAGREGIFVIDATCVVIKSQYVPTPRTQQRQLAPSGESCIVSDSLRQPKPCLEEEGKGAAANPSVCQKRLLSSRVLNPPSEGREFEAEGRQQGDSSLEERSSSGLGFPVGEVNPRDAPTHPGSPEHSTLGPAAPGCAGSVKGPEAAGVPRRAGGGWARTPGPYAGALREAVSRIRRHTAPDSDSDEAEDLSAHSGSSDGSDTDAPGASWRNERTLPAVGNTRPREGGKTAELGDSIGEILDVISQTEEGLVREDTRKTPQGKRE | Function: Promotes apoptosis of kidney glomerular podocytes. Podocytes are highly specialized cells essential to the ultrafiltration of blood, resulting in the extraction of urine and the retention of protein.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76004
Sequence Length: 707
Subcellular Location: Cell projection
|
B0TBI9 | MSNVVIIADDLTGANATGVLLARKGYKTATFLQLPQDPLENGNRFDVISITTDSRAVAPEEAYRRVAEAARAMLGNKPGLFTKRIDSTLRGNLGPEIDAMLDVLGPDSLAVVVAAFPTSGRITVGGYLLVHSIPLEQTDVARDPKTPVHQTLVADIVAAQSKHSVGFIPLATVLQGSTAVMEALGAQKEAGKRIVVMDAATQKDLDTIAHGAYLSGLSVVAVDPGPFTEALAAYVLPKPKQGRGKKVLMVVGSVTALTRQQLKAVENAYSTCFTTVDVHALIDPWRNAEEIERVSGEVLDHLDDHQVLGVRTVEEAGQVLDLASVALAYMISEEEIASRIADGLAAIARRVLQVSHGEVGGLYTSGGDVTVAVCQALAASGVEVKDEVVPLAAYGRLIGGAFHQTPIITKGGLVGNSDAACTCVDYLLTKISNETYPAE | Function: Catalyzes the ATP-dependent phosphorylation of D-erythronate to D-erythronate 4-phosphate. Can also phosphorylate D-threonate and 4-hydroxy-L-threonine, with lower efficiency.
Catalytic Activity: ATP + D-erythronate = 4-phospho-D-erythronate + ADP + H(+)
Sequence Mass (Da): 46168
Sequence Length: 439
EC: 2.7.1.220
|
Q892U4 | MEIQKFIDHTILKPEATEEQVKKLCKEARDYKFASVCVNPYYTSLVSKELQGTDVKTCVVIGFPLGANTKEVKAFETKQAIENGAKEVDMVINIGALKDKKYDVVKEDIEAVVNEAKGKALVKVIIETCLLTDEEKVKACEISKEVGADFVKTSTGFSTGGAKKEDVKLMRETVGENIGVKASGGIRDYKTSLEMIEAGANRIGASAGIKIVEESK | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23516
Sequence Length: 216
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
|
P0CH94 | MSSLNNEEWDLLISGKKATLQYPIPLLCYPAPEVVSIAQIIDHTQLSLSATGSQIDVLCAEAKEYGFATVCVRPDYVSRAVQYLQGTQVGVTCVIGFHEGTYSTDQKVSEAKRAMQNGASELDMVMNYPWLSEKRYTDVFQDIRAVRLAAKDAILKVILETSQLTADEIIAGCVLSSLAGADYVKTSTGFNGPGASIENVSLMSAVCDSLQSETRVKASGGIRTIEDCVKMVRAGAERLGASAGVKIVNETRLGNRQVDEPMEPTNY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 28872
Sequence Length: 267
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
|
Q8FSJ0 | MTITRAEMASILDYTLLGPEVTTADLQALIDDALTLGVPTICIPPSMMNATKRAQDAGLRIATVAGFPHGKSAPLVKAAEARLAVQYGASEVDVVLDIAAVKAADDNALLAEMVAIREALASPVTLKFIVESAVVDDVALEVATHAARAAGADFIKTSTGFHPAGGATVEAVRVLAGAAQGQIGVKASGGIRTWEQAVAMVEAGATRIGTSNARAILEGAPA | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 22539
Sequence Length: 222
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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Q9RV25 | MSLASYIDHTLLKATATLADIRTLCEEAREHSFYAVCINPVFIPHARAWLEGSDVKVATVCGFPLGAISSEQKALEARLSAETGADEIDMVIHIGSALAGDWDAVEADVRAVRRAVPEQVLKVIIETCYLTDEQKRLATEVAVQGGADFVKTSTGFGTGGATVDDVRLMAEVIGGRAGLKAAGGVRTPADAQAMIEAGATRLGTSGGVGLVSGGENGAGY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 22792
Sequence Length: 220
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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Q24SU9 | MRTMNLAGMIDHTFLKPEATEKDIVNLCHEAKQHKFATVCINPAYICTAAKLLHGSGVGVATVIGFPLGATMTEIKVQEIFAAKAHGAREVDIVINIGWAKSGNWEAVAKDITRAVEAAHCCGVTIKVIIETSLLTEEEKQKAAEIVKASGADYIKTSTGFAGGGATVEDVRNLKAWVGQSVKVKASGGIRSRETALQMVEAGADRLGTSSGVQIITV | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23020
Sequence Length: 218
Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Subcellular Location: Cytoplasm
EC: 4.1.2.4
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