ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q5I085 | MADGELNVDSLISRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 37173
Sequence Length: 327
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
Q8MJ46 | MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECVSINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGETDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPLRGMITKQAKK | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (By similarity).
PTM: Phosphorylated by NEK2.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 37015
Sequence Length: 323
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
P36873 | MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective .
PTM: Phosphorylated by NEK2.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 36984
Sequence Length: 323
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
P63087 | MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQAKK | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.
PTM: Phosphorylated by NEK2.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 36984
Sequence Length: 323
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
Q8SRZ0 | MDIREMDLKRQEANALFKKQMIDEALEIYKTSFLEATKSVVPGTRNDLLEEQLSLLAYNISVVYYKRKNFPKSLAFGLESLKHRKSDKVLCKICAIYLRLGMLREYKEMYDQMVTRSSGPEVAFLLKRMKLSEVIVEKHLEKRVTLESLHELSKEISGGRSIPADTLESILEQGESILLGCENVVHTESSGEVLIFGDTHGQYFDVVSILNKVFDKDRMVIFNGDYVDRGSHSVENFALLLSLKILFPGRVHLTRGNHELSDINRVYGFYDEVKRKYPFSSDSVYRRFQDAFRALPISIIVNEKVFITHGGLPEAPVKVDNLQEIYRMTDTHTDELLKGLLWSDPEEILGTEESKRRAGVVFGADVTARFLERNGLDLLVRSHQAVDDGYRVHHGGKVVTIFSAPEYEGSKGPGSYLVLNPSAGEADEIVEISPLTRYKAVKFGRSDGKEVLRLLCN | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 51851
Sequence Length: 457
EC: 3.1.3.16
|
Q7YSW8 | MSTNNNKAPTSQSSDKSATTESKLNDNENTETETKTDENNEEKPKMTLKPPQPKIENKVSTIDRVVPSVKYPKSLPLPHDVLFNEDKTINLPKLQEHFFAEGRLNHDDVIEIVKMAAEILEKEPTLIQVEAPITVCGDTHGQFYDLIKIFENDIGGNPANTNYLFLGDYVDRGYFSMEVIIYLYACKINYPNTFFLLRGNHECRHLTEYFTFKEECLHKYSEEVYDFITESFNALPLAALMNGKFLCIHGGLSPDIKTLDDIANIDRFKEPPSSGPMCDLLWSDPMEEFSPEIREHFVPNDVRGCSYLYSYRAVCSFLQKNKLLSVIRAHEAQNAGYKMHLQNDATGFPSVITLFSAPNYLDAYNNKGAVLRYENNVMNIRQFTCSPHPYWLPNFMDVFTWSMPFVSEKVAEMLLVLLNLCNDEEAEKNENAQTVKDTSEEEKRRQMLRAKVKSVSKMMRMFSLLRQERETIMMIKSFSPSRKIPQGLLTEGKDALKKALGDFAQARKMDLINEKRPPILDRVNSRGELLRMNSRGELFRINSKGDLFRSNSYADLKPPQGPQETIKITECHEQNITTNNINPNSITTNENNSNEQLQQQQQQQQQQQPPTTTSTTTQTEVAK | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Catalytic subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals.
PTM: The N-terminus is blocked.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 71393
Sequence Length: 623
Domain: The autoinhibitory domain prevents access to the catalytic site.
EC: 3.1.3.16
|
Q08209 | MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals . Many of the substrates contain a PxIxIT motif and/or a LxVP motif . In response to increased Ca(2+) levels, dephosphorylates and activates phosphatase SSH1 which results in cofilin dephosphorylation . In response to increased Ca(2+) levels following mitochondrial depolarization, dephosphorylates DNM1L inducing DNM1L translocation to the mitochondrion . Positively regulates the CACNA1B/CAV2.2-mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity). Dephosphorylates heat shock protein HSPB1 (By similarity). Dephosphorylates and activates transcription factor NFATC1 . In response to increased Ca(2+) levels, regulates NFAT-mediated transcription probably by dephosphorylating NFAT and promoting its nuclear translocation . Dephosphorylates and inactivates transcription factor ELK1 . Dephosphorylates DARPP32 . May dephosphorylate CRTC2 at 'Ser-171' resulting in CRTC2 dissociation from 14-3-3 proteins . Dephosphorylates transcription factor TFEB at 'Ser-211' following Coxsackievirus B3 infection, promoting nuclear translocation . Required for postnatal development of the nephrogenic zone and superficial glomeruli in the kidneys, cell cycle homeostasis in the nephrogenic zone, and ultimately normal kidney function (By similarity). Plays a role in intracellular AQP2 processing and localization to the apical membrane in the kidney, may thereby be required for efficient kidney filtration (By similarity). Required for secretion of salivary enzymes amylase, peroxidase, lysozyme and sialic acid via formation of secretory vesicles in the submandibular glands (By similarity). Required for calcineurin activity and homosynaptic depotentiation in the hippocampus (By similarity). Required for normal differentiation and survival of keratinocytes and therefore required for epidermis superstructure formation (By similarity). Positively regulates osteoblastic bone formation, via promotion of osteoblast differentiation (By similarity). Positively regulates osteoclast differentiation, potentially via NFATC1 signaling (By similarity). May play a role in skeletal muscle fiber type specification, potentially via NFATC1 signaling (By similarity). Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB (By similarity). Required for antigen-specific T-cell proliferation response (By similarity). Dephosphorylates KLHL3, promoting the interaction between KLHL3 and WNK4 and subsequent degradation of WNK4 . Negatively regulates SLC9A1 activity .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58688
Sequence Length: 521
Domain: The autoinhibitory domain prevents access to the catalytic site.
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
P16298 | MAAPEPARAAPPPPPPPPPPPGADRVVKAVPFPPTHRLTSEEVFDLDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLSICSDDELMTEGEDQFDGSAAARKEIIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLAGGRQTLQSATVEAIEAEKAIRGFSPPHRICSFEEAKGLDRINERMPPRKDAVQQDGFNSLNTAHATENHGTGNHTAQ | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals . Dephosphorylates TFEB in response to lysosomal Ca(2+) release, resulting in TFEB nuclear translocation and stimulation of lysosomal biogenesis . Dephosphorylates and activates transcription factor NFATC1 . Dephosphorylates and inactivates transcription factor ELK1 . Dephosphorylates DARPP32 . Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB (By similarity). May play a role in skeletal muscle fiber type specification (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 59024
Sequence Length: 524
Domain: The poly-Pro domain may confer substrate specificity.
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
P48453 | MAAPEPARAAPPPPPPPPPPLGADRVVKAVPFPPTHRLTSEEVFDMDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLSICSDDELMTEGEDQFDVGSAAARKEIIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLAGGRQTLQSATVEAIEAEKAIRGFSPPHRICSFEEAKGLDRINERMPPRKDAVQQDGFNSLNTAHTTENHGTGNHSAQ | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals (By similarity). Dephosphorylates TFEB in response to lysosomal Ca(2+) release, resulting in TFEB nuclear translocation and stimulation of lysosomal biogenesis (By similarity). Dephosphorylates and activates transcription factor NFATC1 (By similarity). Dephosphorylates and inactivates transcription factor ELK1 (By similarity). Dephosphorylates DARPP32 (By similarity). Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB . May play a role in skeletal muscle fiber type specification .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 59173
Sequence Length: 525
Domain: The poly-Pro domain may confer substrate specificity.
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
P48454 | MSGRRFHLSTTDRVIKAVPFPPTQRLTFKEVFENGKPKVDVLKNHLVKEGRLEEEVALKIINDGAAILRQEKTMIEVDAPITVCGDIHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTDYFTFKQECRIKYSEQVYDACMETFDCLPLAALLNQQFLCVHGGMSPEITSLDDIRKLDRFTEPPAFGPVCDLLWSDPSEDYGNEKTLEHYTHNTVRGCSYFYSYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELISDDEAEGSTTVRKEIIRNKIRAIGKMARVFSILRQESESVLTLKGLTPTGTLPLGVLSGGKQTIETATVEAVEAREAIRGFSLQHKIRSFEEARGLDRINERMPPRKDSIHAGGPMKSVTSAHSHAAHRSDQGKKAHS | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 58129
Sequence Length: 512
Domain: The autoinhibitory domain prevents access to the catalytic site.
Subcellular Location: Mitochondrion
EC: 3.1.3.16
|
P48455 | MSVRRPQFSTTERVIKAVPFPPTRRLTLKEVFENGKPKMDLLKNHLVKEGRVEEEVALKIINDGAAILKQEKTMIEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSEMVYDACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLEDIRKLDRFSEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSYPAVCEFLQNNSLLSIIRAHEAQDAGYRMYRKNQATGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNILNICSDEEMNVTDEEGATTGRKEVIKNKIRAIGKMARVFTVLREESENVLTLKGLTPTGTLPLGVLSGGKQTIETAKQEAAEEREAIRGFTIAHRIRSFEEARGLDRINERMPPRKEASYHHDAGRMHSHSHPPHPQASRRTDHGKKAL | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 58699
Sequence Length: 513
Domain: The autoinhibitory domain prevents access to the catalytic site.
Subcellular Location: Mitochondrion
EC: 3.1.3.16
|
Q0G819 | MASTSAGQNSAAKPDTTNTTTTASNNNRERERDLKQFTERFVKTVQFPVSERLTVDQVYDRRTGKPRHEVLRDHFIKEGRIEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDRFKEPPAFGPMCDLLWSDPLEDFGNERNSEQFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAILKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVHILNICSDDELMAECDDTFEGGVGSARKEVIRHKIRAIGKMARAFSVLRHESESVLQLKGLNAGGKLPQGALSEGRTGLNAAYRIEQSVAAESGCDSGHLIQSFEEARRLDKINERMPPTMATPPAQSPSQSPIPSRQTTPQPPQNGPSNS | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase . Dephosphorylates arrd-17 . Dephosphorylates daf-16 at 'Ser-319' which regulates daf-16 nuclear translocation . Dephosphorylates calcium permeable cation channel pkd-2 at 'Ser-534' . Regulates male mating behavior including response to hermaphrodite contact and vulva location and localization of pkd-2 to neuronal cilium . Negatively regulates several sensory behaviors including thermotaxis in ADF neurons, osmosensation in ASH neurons, olfaction adaptation in AWC neurons and sensitivity to CO2 levels . Plays a role in modulating temperature-dependent calcium responses in AFD neurons and together with tax-6 inhibitor rcan-1 regulates thermotaxis in AFD neurons . Regulates expression of rcan-1 . In response to changes in intracellular calcium levels may also regulate nuclear translocation of transcriptional regulators such as crtc-1 . Plays a role in egg-laying, body-size, fertility, growth, movement and cuticle development . Negatively regulates lifespan . Promotes transcription activator crtc-1 nuclear localization, probably by dephosphorylating crtc-1 and thereby negatively regulates lifespan . Regulates expression of chemoreceptor srt-2 in AWC neurons probably downstream of Ser/Thr kinase kin-29 . Negatively regulates nicotinic acetylcholine receptor (nAChR) sensitivity to nicotine . Plays a role in several endocytic processes including in coelomocyte endocytosis, intestine apical endocytosis and synaptic vesicle recycling . May negatively regulate excitatory GABA receptor exp-1 during enteric muscle contraction . May negatively regulate autophagy .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 61505
Sequence Length: 542
Domain: The autoinhibitory domain prevents access to the catalytic site.
Subcellular Location: Perikaryon
EC: 3.1.3.16
|
Q12705 | MTSGPHNLEDPIVRAIRQKNQAPSHDFTIFVQEDGSSVSTLDRVVKNVQAPATYIPTDVEFFDINEPDKPDLHFLRNHFIREGRLSEEQTLYIIKKATEILKSEDNLIEVDAPVTVCGDIHGQYYDLMKLFEVGGNPANTQYLFLGDYVDRGYFSIECLLYLWALKIWYPKTLWLLRGNHECAHLTDYFTFKLECTHKYNIKVYEACLQSFNALPLAAIMNKQFLCVHGGLSPELHTLNDIRMINRFCEPPTHGLMCDLLWSDPLEDFGSEKSNKHFIHNNVRGCSYFYSYQAVCTFLENNNLLSVIRAHEAQDVGYRMYRKTKTTGFPSLMTIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVSEMLISMLNICSKEELYETDLKESAPTQHKQPAPSENENKADQEIDIEARRQIIKNKIMAIGRISRVFSVLREERESVSELKNVSGTQRLPAGTLMLGAEGIKNAINSFDDARKLDIQNERLPPSNSRRRSTDLKAFEEVMNSSEDDTSIDHLVERFADKKSSL | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Appears to be involved in cytokinesis, mating, transport, nuclear and spindle pole body positioning, and cell shape.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 63714
Sequence Length: 554
EC: 3.1.3.16
|
P49444 | MGPYLSQPKRDKTTTTGQGKSVIFAASEMQGWRNTMEDAHIHRPDIIQDVSVFGVFDGHGGREVAQFVEKHFVDELLKNKNFKEQKFEEALKETFLKMDELLLTPEGQKELNQYKATDTDESYAGCTANVALIYKNTLYVANAGDSRSVLCRNNTNHDMSVDHKPDNPEEKSRIERAGGFVSDGRVNGNLNLSRALGDLEYKRDNKLRSNEQLIIALPDVKKTELTPQDKFILMGCDGVFETLNHQELLKQVNSTIGQAQVTEELLKKAAEDLLDQLLAPDTSQGTGCDNMTTILVYLRR | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Enzyme with a broad specificity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33699
Sequence Length: 300
Subcellular Location: Membrane
EC: 3.1.3.16
|
P40371 | MKGSHPNAGSLLEPLHKLNPFSENSTSGHRKNASDHSADGETRPIAIEMKDSKGNTVPVGNSRPSKASNWLAGLMEDKNQRWRRSMEDTHICLYDFGGNQDDGFVAVYDGHAGIQASDYCQKNLHKVLLEKVRNEPDRLVTDLMDETFVEVNSKIAKATHNDICGCTAAVAFFRYEKNRTRRVLYTANAGDARIVLCRDGKAIRLSYDHKGSDANESRRVTQLGGLMVQNRINGVLAVTRALGDTYLKELVSAHPFTTETRIWNGHDEFFIIACDGLWDVVSDQEAVDFVRNFVSPREAAVRLVEFALKRLSTDNITCIVVNLTRNPGDLDDSGLTADNDSYSNDYY | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: It has a serine and threonine phosphatase activity. Has a specialized role in the heat shock response. May be responsible for the dephosphorylation of hsp90. Also has a role in maintaining osmotic stability.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 38676
Sequence Length: 347
EC: 3.1.3.16
|
P35182 | MSNHSEILERPETPYDITYRVGVAENKNSKFRRTMEDVHTYVKNFASRLDWGYFAVFDGHAGIQASKWCGKHLHTIIEQNILADETRDVRDVLNDSFLAIDEEINTKLVGNSGCTAAVCVLRWELPDSVSDDSMDLAQHQRKLYTANVGDSRIVLFRNGNSIRLTYDHKASDTLEMQRVEQAGGLIMKSRVNGMLAVTRSLGDKFFDSLVVGSPFTTSVEITSEDKFLILACDGLWDVIDDQDACELIKDITEPNEAAKVLVRYALENGTTDNVTVMVVFL | Cofactor: Binds 2 magnesium or manganese ions per subunit. Manganese is about 20 times more efficient than magnesium.
Function: It has a serine and a weak tyrosine phosphatase activity with ratios of serine to tyrosine phosphatase activity as high as 200:1. It is essential for growth or germination at 37 degrees Celsius. May have a role in the heat shock response. Involved in tRNA splicing and cell separation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 31550
Sequence Length: 281
Subcellular Location: Peroxisome
EC: 3.1.3.16
|
P49596 | MGQTLSEPVTKKESASCANENYLVGSSCMQGWRVDMEDAHTHLLSLPDDPKCAFFAVYDGHGGSKVSQYSGINLHKKVVAQKEFSEGNMKEAIEKGFLELDQQMRVDEETKDDVSGTTAVVVLIKEGDVYCGNAGDSRAVSSVVGEARPLSFDHKPSHETEARRIIAAGGWVEFNRVNGNLALSRALGDFAFKNCDTKPAEEQIVTAFPDVITDKLTPDHEFIVLACDGIWDVMTNQEVVDFVREKLAEKRDPQSICEELLTRCLAPDCQMGGLGCDNMTVVLVGLLHGQSPDTLFTKCARPAVFTGVNNEDGDQNQIQQDISRVINNFDGEQRVNAANQEEEEDDNEPAPANFQV | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 39064
Sequence Length: 356
EC: 3.1.3.16
|
Q09172 | MGQTLSEPVLDKHSSSGGDRWLHFGVSHMQGWRISMEDAHCALLNFTDSNSSNPPTSFFGVFDGHGGDRVAKYCRQHLPDIIKSQPSFWKGNYDEALKSGFLAADNALMQDRDMQEDPSGCTATTALIVDHQVIYCANAGDSRTVLGRKGTAEPLSFDHKPNNDVEKARITAAGGFIDFGRVNGSLALSRAIGDFEYKKDSSLPPEKQIVTAFPDVVIHNIDPDDEFLILACDGIWDCKSSQQVVEFVRRGIVARQSLEVICENLMDRCIASNSESCGIGCDNMTICIVAFLHGRGLEDWYNWITQRVNSGEGPCAPPSYAELRGPNTIADARNLQLEYDHIASHEYGSGDTYDSDSDDETIAYDRYYLH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Has an important role in osmotic stability and cell shape control. It may negatively regulate the osmosensing signal transmitted through wis1 map kinase.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 40878
Sequence Length: 370
EC: 3.1.3.16
|
Q9SFU3 | MTFLLLLLFCFLSPAISSAHSIPSTLDGPFVPVTVPLDTSLRGQAIDLPDTDPRVRRRVIGFEPEQISLSLSSDHDSIWVSWITGEFQIGKKVKPLDPTSINSVVQFGTLRHSLSHEAKGHSLVYSQLYPFDGLLNYTSGIIHHVRITGLKPSTIYYYRCGDPSRRAMSKIHHFRTMPVSSPSSYPGRIAVVGDLGLTYNTTDTISHLIHNSPDLILLIGDVSYANLYLTNGTSSDCYSCSFPETPIHETYQPRWDYWGRFMENLTSKVPLMVIEGNHEIELQAENKTFEAYSSRFAFPFNESGSSSTLYYSFNAGGIHFVMLGAYIAYDKSAEQYEWLKKDLAKVDRSVTPWLVASWHPPWYSSYTAHYREAECMKEAMEELLYSYGTDIVFNGHVHAYERSNRVYNYELDPCGPVYIVIGDGGNREKMAIEHADDPGKCPEPLTTPDPVMGGFCAWNFTPSDKFCWDRQPDYSALRESSFGHGILEMKNETWALWTWYRNQDSSSEVGDQIYIVRQPDRCPLHHRLVNHC | Cofactor: Binds 1 Fe cation per subunit.
Function: Acid phosphatase activity with p-nitrophenyl phosphate (pNPP), D-myoinositol 1-phosphate (Ins(1)P1), phytic acid and Myo-inositol hexakisphosphate. Low or no activity with Glc-6-P and ATP. Confers shoot growth stimulation, enhanced salt and osmotic stress tolerance, and ABA insensitivity. May modulate ascorbic acid (AsA) levels by controlling the input of myoinositol into this branch of AsA biosynthesis.
Catalytic Activity: 1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
Sequence Mass (Da): 60435
Sequence Length: 532
Subcellular Location: Secreted
EC: 3.1.3.-
|
Q9SCX8 | MNSGRRSLMSATASLSLLLCIFTTFVVVSNGELQRFIEPAKSDGSVSFIVIGDWGRRGSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFYDNGLFSEHDPNFEQSFSNIYTAPSLQKQWYSVLGNHDYRGDAEAQLSSVLREIDSRWICLRSFVVDAELVEMFFVDTTPFVKEYYTEADGHSYDWRAVPSRNSYVKALLRDLEVSLKSSKARWKIVVGHHAMRSIGHHGDTKELNEELLPILKENGVDLYMNGHDHCLQHMSDEDSPIQFLTSGAGSKAWRGDINPVTINPKLLKFYYDGQGFMSARFTHSDAEIVFYDVFGEILHKWVTSKQLLHSSV | Cofactor: Binds 1 Fe cation per subunit.
Function: Metallo-phosphoesterase involved in phosphate metabolism. Has a peroxidase activity.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 38297
Sequence Length: 338
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q9LJU7 | MEKWGILLLVTLSVSIIFTSAAADDYVRPKPRETLQFPWKQKSSSVPEQVHISLAGDKHMRVTWVTNDKSSPSFVEYGTSPGKYSYLGQGESTSYSYIMYRSGKIHHTVIGPLEADTVYYYRCGGEGPEFHLKTPPAQFPITFAVAGDLGQTGWTKSTLDHIDQCKYAVHLLPGDLSYADYMQHKWDTFGELVQPLASVRPWMVTQGNHEKESIPFIVDEFVSFNSRWKMPYEESGSNSNLYYSFEVAGVHAIMLGSYTDYDRYSDQYSWLKADLSKVDRERTPWLIVLFHVPWYNSNNAHQHEGDEMMAEMEPLLYASGVDIVFTGHVHAYERTKRVNNGKSDPCGPVHITIGDGGNREGLARKYKDPSPEWSVFREASFGHGELQMVNSTHALWTWHRNDDDEPTRSDEVWLNSLVNSGCLKKRPQELRKMLLEP | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 49870
Sequence Length: 437
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q9LX83 | MGLNHLTLVCSAIALLSIFVVSQAGVTSTHVRVSEPSEEMPLETFPPPACYNAPEQVHITQGDHAGRGMIISWVTPLNEDGSNVVTYWIANSDGSDNKSALATTSSYRYFNYTSGYLYHATIKGLETLYNYMSNPKGQAVLFAGDLSYADDHPNHDQRKWDSYGRFVEPSAAYQPWIWAAGNHEIDYAESIPHKVHLHFGTKSNELQLTSSYSPLTQLMDELKKVNRSETPWLIVLVHAPWYNSNNYHYMEGESMRVTFEPWFVENKVDIVFAGHVHAYERSERISNIQYNITDGMSTPVKDQNAPVYITIGDGGNIEGIANNFIDPQPSYSAFREASFGHAILEIKNRTHAHYTWHRNKEDEFIPEAVIADSIWLKNRYYLREEETS | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 44053
Sequence Length: 388
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q9LXI7 | MVKVLGLVAILLIVLAGNVLSYDRQGTRKNLVIHPTNEDDPTFPDQVHISLVGPDKMRISWITQSSISPSVVYGTVSGKYEGSANGTSSSYHYLLIYRSGQINDVVIGPLKPNTVYYYKCGGPSSTQEFSFRTPPSKFPIKFAVSGDLGTSEWSKSTLEHVSKWDYDVFILPGDLSYANMYQPLWDTFGRLVQPLASQRPWMVTHGNHELEKIPILHSNPFTAYNKRWRMPFEESGSSSNLYYSFNVYGVHIIMLGSYTDFEPGSEQYQWLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESVEMKESMETLLYKARVDLVFAGHVHAYERFSRVYQDKFDKCGPVYINIGDGGNLEGLATKYRDPNPEISLFREASFGHGQLVVENATHARWEWHRNDDDVSVEKDSVWLTSLLADSSCKI | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 48462
Sequence Length: 427
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q8S340 | MKLFGLFLSFTLLFLCPFISQADVPELSRQPPRPIVFVHNDRSKSDPQQVHISLAGKDHMRVTFITEDNKVESVVEYGKQPGKYDGKATGECTSYKYFFYKSGKIHHVKIGPLQANTTYYYRCGGNGPEFSFKTPPSTFPVEFAIVGDLGQTEWTAATLSHINSQDYDVFLLPGDLSYADTHQPLWDSFGRLVEPLASKRPWMVTEGNHEIEFFPIIEHTTFKSYNARWLMPHTESFSTSNLYYSFDVAGVHTVMLGSYTDFDCESDQYQWLQADLAKVDRKTTPWVVVLLHAPWYNTNEAHEGEGESMREAMESLLFNARVDVVFSGHVHAYERFKRVYNNKADPCGPIHITIGDGGNREGLALSFKKPPSPLSEFRESSFGHGRLKVMDGKRAHWSWHRNNDSNSLLADEVWLDSLSTSSSCWPSSRSNDEL | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 49357
Sequence Length: 434
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q6TPH1 | MTLLIMITLTSISLLLAAAETIPTTLDGPFKPLTRRFEPSLRRGSDDLPMDHPRLRKRNVSSDFPEQIALALSTPTSMWVSWVTGDAIVGKDVKPLDPSSIASEVWYGKEKGNYMLKKKGNATVYSQLYPSDGLLNYTSGIIHHVLIDGLEPETRYYYRCGDSSVPAMSEEISFETLPLPSKDAYPHRIAFVGDLGLTSNTTTTIDHLMENDPSLVIIVGDLTYANQYRTIGGKGVPCFSCSFPDAPIRETYQPRWDAWGRFMEPLTSKVPTMVIEGNHEIEPQASGITFKSYSERFAVPASESGSNSNLYYSFDAGGVHFVMLGAYVDYNNTGLQYAWLKEDLSKVDRAVTPWLVATMHPPWYNSYSSHYQEFECMRQEMEELLYQYRVDIVFAGHVHAYERMNRIYNYTLDPCGPVYITIGDGGNIEKVDVDFADDPGKCHSSYDLFFFNSLNLSN | Cofactor: Binds 1 Fe cation per subunit.
Function: Acid phosphatase activity with ATP, ADP, dATP, pyrophosphate, polyphosphate, phosphoserine and phosphothreonine. Low or no activity with phosphotyrosine, AMP and phytate.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 51551
Sequence Length: 458
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q949Y3 | MNHLVIISVFLSSVLLLYRGESGITSSFIRSEWPAVDIPLDHHVFKVPKGYNAPQQVHITQGDYDGKAVIISWVTPDEPGSSQVHYGAVQGKYEFVAQGTYHNYTFYKYKSGFIHHCLVSDLEHDTKYYYKIESGESSREFWFVTPPHVHPDASYKFGIIGDMGQTFNSLSTLEHYMESGAQAVLFLGDLSYADRYQYNDVGVRWDSWGRFVERSTAYQPWLWSAGNHEVDYMPYMGEVTPFRNYLQRYTTPYLASKSSSPLWYAVRRASAHIIVLSSYSPFVKYTPQWHWLSEELTRVDREKTPWLIVLMHVPIYNSNEAHFMEGESMRAAFEEWFVQHKVDVIFAGHVHAYERSYRISNVRYNVSSGDRYPVPDKSAPVYITVGDGGNQEGLAGRFTEPQPDYSAFREASYGHSTLDIKNRTHAIYHWNRNDDGKKVATDEFVLHNQYWGKNIRRRKLKKHYIRSVVGGWIAT | Cofactor: Binds 1 Fe cation per subunit.
Function: Metallo-phosphoesterase involved in phosphate metabolism. Acid phosphatase activity with phosphoenolpyruvate, inorganic pyrophosphate, phenyl-phosphate and p-nitrophenyl-phosphate as the most effective substrates. No activity with phytic acid, phosphocholine or bis-p-nitrophenyl-phosphate. Has a peroxidase activity at alkaline pH.
PTM: Glycosylated.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 55010
Sequence Length: 475
Subcellular Location: Vacuole
|
P08371 | MPVKEQGFSLLEVLIAMAISSVLLLGAARFLPALQRESLTSTRKLALEDEIWLRVFTVAKHLQRAGYCHGICTGEGLEIVGQGDCVIVQWDANSNGIWDREPVKESDQIGFRLKEHVLETLRGATSCEGKGWDKVTNPDAIIIDTFQVVRQDVSGFSPVLTVNMRAASKSEPQTVVNASYSVTGFNL | Function: Not yet known.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20520
Sequence Length: 187
Subcellular Location: Membrane
|
P08372 | MSASLKNQQGFSLPEVMLAMVLMVMIVTALSGFQRTLMNSLASRNQYQQLWRHGWQQTQLRAISPPANWQVNRMQTSQAGCVSISVTLVSPGGREGEMTRLHCPNRQ | Function: Not yet known.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12004
Sequence Length: 107
Subcellular Location: Membrane
|
P36647 | MDKQRGFTLIELMVVIGIIAILSAIGIPAYQNYLRKAALTDMLQTFVPYRTAVELCALEHGGLDTCDGGSNGIPSPTTTRYVSAMSVAKGVVSLTGQESLNGLSVVMTPGWDNANGVTGWTRNCNIQSDSALQQACEDVFRFDDAN | Function: Major component of the type IV pilus (T4P) that plays a role in cell adhesion and motility. Not produced when grown under standard laboratory conditions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15622
Sequence Length: 146
Subcellular Location: Fimbrium
|
Q9RUV0 | MRVLFIGDVFGQPGRRVLQNHLPTIRPQFDFVIVNMENSAGGFGMHRDAARGALEAGAGCLTLGNHAWHHKDIYPMLSEDTYPIVRPLNYADPGTPGVGWRTFDVNGEKLTVVNLLGRVFMEAVDNPFRTMDALLERDDLGTVFVDFHAEATSEKEAMGWHLAGRVAAVIGTHTHVPTADTRILKGGTAYQTDAGFTGPHDSIIGSAIEGPLQRFLTERPHRYGVAEGRAELNGVALHFEGGKATAAERYRFIED | Cofactor: Mn(2+) is the preferable metal for phosphatase activity. Phosphodiesterase activity is observed in the presence of Co(2+), Mn(2+) or Fe(2+).
Function: Has a dual activity phosphatase/phosphodiesterase in vitro, with a preference to phosphoenolpyruvate (PEP) and 2',3'-cAMP, respectively. Can also use 2',3'-cGMP, 2',3'-cCMP and various model substrates such as p-nitrophenyl phosphate (pNPP), bis-p-nitrophenyl phosphate (bis-pNPP) and p-nitrophenyl thymidine monophosphate (pNP-TMP).
Catalytic Activity: a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-phosphate + H(+)
Sequence Mass (Da): 27936
Sequence Length: 255
|
P11155 | MAASVSRAICVQKPGSKCTRDREATSFARRSVAAPRPPHAKAAGVIRSDSGAGRGQHCSPLRAVVDAAPIQTTKKRVFHFGKGKSEGNKTMKELLGGKGANLAEMASIGLSVPPGFTVSTEACQQYQDAGCALPAGLWAEIVDGLQWVEEYMGATLGDPQRPLLLSVRSGAAVSMPGMMDTVLNLGLNDEVAAGLAAKSGERFAYDSFRRFLDMFGNVVMDIPRSLFEEKLEHMKESKGLKNDTDLTASDLKELVGQYKEVYLSAKGEPFPSDPKKQLELAVLAVFNSWESPRAKKYRSINQITGLRGTAVNVQCMVFGNMGNTSGTGVLFTRNPNTGEKKLYGEFLVNAQGEDVVAGIRTPEDLDAMKNLMPQAYDELVENCNILESHYKEMQDIEFTVQENRLWMLQCRTGKRTGKSAVKIAVDMVNEGLVEPRSAIKMVEPGHLDQLLHPQFENPSAYKDQVIATGLPASPGAAVGQVVFTAEDAEAWHSQGKAAILVRAETSPEDVGGMHAAVGILTERGGMTSHAAVVARWWGKCCVSGCSGIRVNDAEKLVTIGSHVLREGEWLSLNGSTGEVILGKQPLSPPALSGDLGTFMAWVDDVRKLKVLANADTPDDALTARNNGAQGIGLCRTEHMFFASDERIKAVRQMIMAPTLELRQQALDRLLTYQRSDFEGIFRAMDGLPVTIRLLDHPSYEFLPEGNIEDIVSELCAETGANQEDALARIEKLSEVNPMLGFRGCRLGISYPELTEMQARAIFEAAIAMTNQGVQVFPEIMVPLVGTPQELGHQVTLIRQVAEKVFANVGKTIGYKVGTMIEIPRAALVADEIAEQAEFFSFGTNDLTQMTFGYSRDDVGKFIPVHLAQGILQHDPFEVLDQRGVGELVKFATERGRKARPNLKVGICGEHGGEPSSVAFFAKAGLDFVSCSPFRVPIARLAAAQVLV | Function: Formation of phosphoenolpyruvate, which is the primary acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants.
PTM: Phosphorylation of Thr-527 in the dark inactivates the enzyme, dephosphorylation upon light stimulation reactivates the enzyme . More highly phosphorylated when grown under high rather than low light regimes (70 vs 900 umol photons/m-2/s). the degree of phosphorylation is strictly regulated by light intensity and the light/dark transition has no influence . Phosphorylated in both mesophyll and bundle sheath cells . The phosphorylation at Ser-528 may be important for the phosphorylation at Thr-527 and may also be regulated by light intensity .
Catalytic Activity: ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 102674
Sequence Length: 947
Domain: The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Pathway: Photosynthesis; C4 acid pathway.
Subcellular Location: Plastid
EC: 2.7.9.1
|
Q6AVA8 | MPSVSRAVCVQRASGNNGRRCRDGAAAAGRRSVVAQRARHGKPEVAIRSGSGGSARGGHCSPLRAVAAPIPTTKKRVFHFGKGKSEGNKAMKDLLGGKGANLAEMASIGLSVPPGFTVSTEACQQYQAAGKTLPAGLWEEIVEGLQWVEEYMAARLGDPARPLLLSVRSGAAVSMPGMMDTVLNLGLNDEVAAGLAAKSGDRFAYDSYRRFLDMFGNVVMDIPHALFEEKLEAMKAVKGLHNDTDLTATDLKELVAQYKDVYVEAKGEPFPSDPKKQLQLAVLAVFNSWDSPRAIKYRSINKITGLKGTAVNVQTMVFGNMGNTSGTGVLFTRNPSTGEKKLYGEFLVNAQGEDVVAGIRTPEDLDAMRDHMPEPYEELVENCKILESHYKEMMDIEFTVQENRLWMLQCRTGKRTGKGAVKIAVDMVNEGLVERRTALKMVEPGHLDQLLHPQFENPSGYKDKVIATGLPASPGAAVGQIVFTAEDAEAWHAQGKDVILVRTETSPEDVGGMHAAVGILTARGGMTSHAAVVARGWGKCCVSGCSSVRVNDASKIVVIEDKALHEGEWLSLNGSTGEVIIGKQPLCPPALSGDLETFMSWVDEVRKLKVMANADTPEDATTARQNGAEGIGLCRTEHMFFASDERIKAVRQMIMASSLELRQKALDRLLPYQRSDFEGIFRAMDGLPVTIRLLDPPLHEFLPEGHVEDMVRELCSETGAAQDDVLARVEKLSEVNPMLGFRGCRLGISYPELTEMQARAIFEAAITMTNQGIQVFPEIMVPLVGTPQELGHQVDVIRQIANKVFTDMGKTIGYKVGTMIEIPRAALVADEIAEQAEFFSFGTNDLTQMTFGYSRDDVGKFLPIYLSQGILQHDPFEVLDQRGVGELVKLATERGRKARPNLKVGICGEHGGEPLSVAFFAKAGLDYVSCSPFRVPIARLAAAQVLL | Function: Formation of phosphoenolpyruvate. The cytoplasmic isoform supports the biosynthetic processes in the nascent endosperm and provides an efficient mechanism for glycolytic ATP synthesis in oxygen depleted tissues. May be involved in regulating the flux of carbon into starch and fatty acids of seeds and in the remobilization of nitrogen reserves in senescing leaves.
PTM: Phosphorylation of Thr-527 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme. Phosphorylation increases during the first 20 days post-pollination and then remains constant through the 40-day mature seed stage. Reactivation by dephosphorylation during germination is negligible.
Catalytic Activity: ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 102788
Sequence Length: 947
Domain: The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
Subcellular Location: Plastid
EC: 2.7.9.1
|
Q75KR1 | MAPAAHRDGAAEAVGQRVFHFGKGRSDGNKTMKDLLGGKGANLAEMASIGLSVPPGFTVSTEACQQYQAQKAMPAGLWDEILAALTWVEGNMGAVLGDPRRPLLLSVRSGAAVSMPGMMDTVLNLGLNDHVVAGLAHRSGERFAYDSYRRFLDMFGNVVMDIPHSLFEEKIEAMKAALGLRNDTELTARDLKELVAQYKNVYVEAKGEEFPSDPKKQLHLSVLAVFNSWDSARAKKYRSINQITGLKGTAVNVQCMVFGNMGDTSGTGVLFTRNPSTGERKLYGEFLVNAQGEDVVAGIRTPQDLDTMKDCMPEPYAELVENCKILESHYKEMMDIEFTVQENRLWMLQCRTGKRTGKGAVKIAVDMVNEGLIDRRSAIKMVEPRHLDQLLHPQFESPSSYGDKVIATGLPASPGAAVGQIVFTADDAEAWHAQGKSVILVRTETSPEDVGGMNAAAGILTARGGMTSHAAVVARGWGKCCVAGCSGIRVNDAEKVVLVADKVLCEGEWLSLNGSTGEVILGKLPLSPPALSGDLGEFMSWVDEVKKLKVKANADTPADALTARNNGAEGIGLCRTEHMFFSSDERIKAMRQMIMAETIEHRQIALDRLLPYQRLDFEGIFRAMDGLPVTIRLLDPPLHEFLPEGNVEDMVRLLSSGNVYTQEEILTRIEKLSEVNPMLGFRGCRLGISYPELTAMQARAIFEAAISMTEQGVKVFPEIMVPLIGTPQELAQQVDVIREVAEKVFANAETTISYKIGSMIEVPRAALIADEIAALAEFFSFGTNDLTQMTFGYSRDDVGKFLPTYLSKGILQNDPFEVFDQKGVGELVKVAVERGRKARPDLEVGICGEHGGEPSSVAFFAKVGLNYVSCSPFRVPIARLAAAQVML | Function: Formation of phosphoenolpyruvate.
Catalytic Activity: ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 96553
Sequence Length: 887
Subcellular Location: Cytoplasm
EC: 2.7.9.1
|
P22983 | MAKWVYKFEEGNASMRNLLGGKGCNLAEMTILGMPIPQGFTVTTEACTEYYNSGKQITQEIQDQIFEAITWLEELNGKKFGDTEDPLLVSVRSGARASMPGMMDTILNLGLNDVAVEGFAKKTGNPRFAYDSYRRFIQMYSDVVMEVPKSHFEKIIDAMKEEKGVHFDTDLTADDLKELAEKFKAVYKEAMNGEEFPQEPKDQLMGAVKAVFRSWDNPRAIVYRRMNDIPGDWGTAVNVQTMVFGNKGETSGTGVAFTRNPSTGEKGIYGEYLINAQGEDVVAGVRTPQPITQLENDMPDCYKQFMDLAMKLEKHFRDMQDMEFTIEEGKLYFLQTRNGKRTAPAALQIACDLVDEGMITEEEAVVRIEAKSLDQLLHPTFNPAALKAGEVIGSALPASPGAAAGKVYFTADEAKAAHEKGERVILVRLETSPEDIEGMHAAEGILTVRGGMTSHAAVVARGMGTCCVSGCGEIKINEEAKTFELGGHTFAEGDYISLDGSTGKIYKGDIETQEASVSGSFERIMVWADKFRTLKVRTNADTPEDTLNAVKLGAEGIGLCRTEHMFFEADRIMKIRKMILSDSVEAREEALNELIPFQKGDFKAMYKALEGRPMTVRYLDPPLHEFVPHTEEEQAELAKNMGLTLAEVKAKVDELHEFNPMMGHRGCRLAVTYPEIAKMQTRAVMEAAIEVKEETGIDIVPEIMIPLVGEKKELKFVKDVVVEVAEQVKKEKGSDMQYHIGTMIEIPRAALTADAIAEEAEFFSFGTNDLTQMTFGFSRDDAGKFLDSYYKAKIYESDPFARLDQTGVGQLVEMAVKKGRQTRPGLKCGICGEHGGDPSSVEFCHKVGLNYVSCSPFRVPIARLAAAQAALNNK | Function: Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
PTM: Phosphorylation of Thr-453 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme (By similarity).
Catalytic Activity: ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 96654
Sequence Length: 874
Domain: The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
EC: 2.7.9.1
|
P37213 | MQRVYAFEDGDGTNKKLLGGKGAGLCTMTKIGLPVPQGFVITTEMCKQFIANGNKMPEGLMEEVKKNMQLVEKKSGKVFGGEENPLLVSVRSGAAMSMPGMMDTILNLGLNDKTVVALAKLTNNERFAYDSYRRFVSLFGKIALNVDDEVYDKTLENKKVEKGVKLDTELDANDMKELAQVFIKKTEEFTKQPFPVDPYAQLEFAICAVFRSWMGKRAVDYRREFKITPEQADGTAVSVVSMVYGNMGNDSATGVCFTRDPGTGENMFFGEYLKNAQGEDVVAGIRTPQIISKMAEDADLPGCYEQLLDIRKKLEGYFHEVQDFEFTIERKKLYMLQTRNGKMNATATVRTGVDMVEEGLITKEQAIMRIAPQSVDQLLHKNMPANYAEAPLVKGLPASPGAATGAVVFDADDAVEQAKGKKVLLLREETKPEDIHGFFVAEGILTCRGGKTSHAAVVARGMGKPCVSGAEGIKVDVAKKIAKIGSLEVHEGDILTIDGSTGCVYKGEVPLEEPQVGSGYFGTILKWANEIKKIGVFANADLPSAAKKALEFGAEGIGLCRTERMFNAVERLPIVVKMILSNTLEERKKYLNELMPLQKQDFIGLLKTMNGLPVTVRLLDPPLHEFLPTLEELMREIFEMKLSGKTEGLAEKEVVLKKVKELMEVNPMIGHRGIRLGTTNPEIYEMQIRAFLEATAEVIKEGIKTHAEIMIPNVTEVNELINLRKNVLEPVHEEVEKKYGIKVPFMYGTMVECVRAALTADKIATEASFFSFGTNDLTQGTFSYSREDSENKFIPKYVELKILPANPFEILDRPGVGEVMRIAVTKGRQTRPELLVGICGEHGGEPSSIEWCHMIGLNYVSCSSYRIPVARIAAAQAQIRHPREN | Function: Catalyzes the dephosphorylation of phosphoenolpyruvate and diphosphate to produce ATP.
Catalytic Activity: ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 97899
Sequence Length: 885
Domain: The N-terminal domain contains the ATP/Pi active site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate active site.
EC: 2.7.9.1
|
P51776 | MSTRRVYFFGETPENQPANSELCRKVLGGKGISLAAMIKLGMPVPLGFTITCQTCVEYQKTASWPKGLKEEVASNLKLLEEKMGKTFGDNTNPLLVSVRSGAAVSMPGMMDTILNLGLNDESVKGLAAVTGNARFAYDSYRRFMQMFGDVCLGIDHDKFEHALDAVKTRYGRKTDPELTADELEEVCEAYRKICVAATGKTFPQCPHEQLELAINAVFKSWTNPRAQAYRTLNKLDHNMGTAVNVQSMVFGNTGDDSGTGVGFTRCPKTGEKFSYLYGEFLQNAQGEDVVAGIRTPVNLKEMPTINASWKACYDELSLIYAKLEGYYNDMVDLEFTVENGKLWMLQARAGKRTGFAMVRIAIDMCKEGMLTEEEALLRIDANKINEFLFKRFDPSVKPVVLGKGIPASPGAAVGVICFCPMRTCELAEQGKKVILTRIETSPEDILGMDRAVGILTARGGQTSHAAVVARGMGKCCVAGADCCQINYATKTLVIGDRKFKEGDFISINGTTGEIYNGAVQTIEPGITDDLQTIMDWSDKYRVLKIRTNADTPHDAAVARKFGAEGIGLCRTEHMFFAADRIMAMREMILSDDEGARRTALNKLLPFQREDFIGIFKAMDGKGVNIRLLDPPLHEFLPHTRDLQKKLAEDMNKKHRHIHERVEDLHEVNPMLGFRGVRLGIVYPEISEMQVRAILEAACIVSREGVTVKPEIMIPVLFSENEMEIMHALVNRVAASVFKEHGTTVDYEVGTMIELPRACVMADKIAQTAQYFSFGTNDLTQTTFGISRDDAGKFIPKYIDRGIFKVDPFVTLDQQGVGALMKMAIEGGRSTRTDMKIGICGEQTDPASILFLHKIGLNYVSCSPYRVPVARVAAAIAAIKARTNQ | Function: Catalyzes the reversible phosphorylation of pyruvate and phosphate.
PTM: Phosphorylation of Thr-462 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme (By similarity).
Catalytic Activity: ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 97630
Sequence Length: 884
Domain: The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
EC: 2.7.9.1
|
Q59754 | MAKWVYTFGAGQAEGSAEDRDRLGGKGANLAEMCNLGLPVPPGLTIVTAACNSYLEKGRSMPEGLREQVREGITRMEKITGRVFGDTNRPLLLSVRSGARASMPGMMDTVLNLGLNDQSVHALGHDAGDARFAWDSYRRFIQMYGDVVMGVDHEVFEEVLEDEKARLGHEQDTELSAVEWQHVISRYKEAIEEVLGLPFPQDPEVQLWGAIGAVFSSWMNPRAITYRHLHGIPAGWGTAVNVQAMVFGNLGNSSATGVAFTRNPSTGEKELYGEFLVNAQGEDVVAGIRTPQNITEAARIASGSDKPSLEKLMPEAFAEFEKICNALERHYRDMQDIEFTIERGKLWMLQTRSGKRTAKSALKIAVDMAEEGLISKEEAVARIDPASLDQLLHPTIDPHARRDIIGSGLPASPGAATGEIVFSSDEAVQAVKEGRKVILVRVETSPEDIHGMHAAEGILTTRGGMTSHAAVVARGMGTPCVSGAGSIRVDQRNELLIAASVTLRKGDVITIDGSSGQVLKGEIPMLQPELSGDFGKIMQWADASRRMTVRTNAETPADARAARSFGAEGIGLCRTEHMFFEDDRINVMREMILAEDEAGRRTALAKLLPMQRSDFVELFSIMHGLPVTIRLLDPPLHEFLPKTDEEIAEVARVLTIDPAELRQRVDALHEFNPMLGHRGCRLAISYPEIAEMQARAIFEAAVQAAHDTGAAVVPEIMVPLVGLRAELDYVKARIEAVAKEVIGEAGVNIDYLIGTMIELPRAALRADTIAESADFFSFGTNDLTQTTFGISRDDAALFLATYQQKGIIEQDPFVSLDFEGVGELIQIAAERGRRTKNGLKLGICGEHGGDPASIRFCEEAGLDYVSCSPFRVPIARLAAAQATINGREVAEVQALAAS | Function: Catalyzes the reversible phosphorylation of pyruvate and phosphate.
PTM: Phosphorylation of Thr-466 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme (By similarity).
Catalytic Activity: ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate
Sequence Mass (Da): 97561
Sequence Length: 898
Domain: The N-terminal domain contains the ATP/Pi active site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate active site.
EC: 2.7.9.1
|
A4FV72 | MATTKRVLYVGGLAEEVDDKVLHAAFIPFGDITDIQIPLDYETEKHRGFAFVEFELAEDAAAAIDNMNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGSEPPKVETQEGEPAVKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVIISDCGEYV | Function: Involved in pre-mRNA splicing as component of the spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. Inhibits KMT2A activity; this requires proline isomerase activity.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 33461
Sequence Length: 301
Domain: The RRM domain mediates both interaction with RNA and with KMT2A (via the third PHD-type zinc-finger), but has much higher affinity for the KMT2A PHD-type zinc-finger.
Subcellular Location: Nucleus
EC: 5.2.1.8
|
Q4G338 | MAASNFPHNKKRTLYVGGFGEEVTEKVLMAAFITFGDIVAISIPMDYETGKHRGFGFVEFELAEDAAAAIDNMNESELFGRTIRCNFARPPKATERSSRPVWADDEWLKRYGKGSGIADAKESNGSASTAKGLPRVYLGVKIGIRYIGRIVIELRSDVVPRTAENFRCLCTGEKGFGYEGSSFHRIIPKFMLQGGDFTKGDGTGGKSIYGPKFEDENFKLKHLMPGTVSMANCGPNTNGSQFFICAEKTDWLDGKHVVFGHVVEGMNVVRQVEQQGTPSGKPQMVVKIVECGELDPVPQTEPQENEENSDPQTPMDVEPQKETA | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 35631
Sequence Length: 324
Domain: The N-terminal RRM domain binds to nucleic acids including single-stranded DNA and RNA homopolymers poly(A), poly(G) and poly(U), but not to poly(C) nor double-stranded DNA. Binds most strongly to G-rich RNA species.
Subcellular Location: Nucleus
EC: 5.2.1.8
|
Q9UNP9 | MATTKRVLYVGGLAEEVDDKVLHAAFIPFGDITDIQIPLDYETEKHRGFAFVEFELAEDAAAAIDNMNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGSEPPKAETQEGEPIAKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEVTEGLDVLRQIEAQGSKDGKPKQKVIIADCGEYV | Function: Involved in pre-mRNA splicing as component of the spliceosome . Combines RNA-binding and PPIase activities . Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules . Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins . Inhibits KMT2A activity; this requires proline isomerase activity .
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 33431
Sequence Length: 301
Domain: The RRM domain mediates both interaction with RNA and with KMT2A (via the third PHD-type zinc-finger), but has much higher affinity for the KMT2A PHD-type zinc-finger.
Subcellular Location: Nucleus
EC: 5.2.1.8
|
Q9QZH3 | MATTKRVLYVGGLAEEVDDKVLHAAFIPFGDITDIQIPLDYETEKHRGFAFVEFELAEDAAAAIDNMNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGPEPPKAEAQEGEPTAKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEVTEGLDVLRQIEAQGSKDGKPKQKVMIADCGEYM | Function: Involved in pre-mRNA splicing as component of the spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. Inhibits KMT2A activity; this requires proline isomerase activity.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 33449
Sequence Length: 301
Domain: The RRM domain mediates both interaction with RNA and with KMT2A (via the third PHD-type zinc-finger), but has much higher affinity for the KMT2A PHD-type zinc-finger.
Subcellular Location: Nucleus
EC: 5.2.1.8
|
P0C1I2 | MPSVNITKNNKTTLYISGLDQQVNEAVLHAAFIPFGEIIAVQMATDTEIDSNNIHRGFGFVEYELAEDCQAAMDNMHLSELYGKVIKVQLAKTINVTTTSNRAVWTDESWLQKYGNVEDVEEKQEDEKENNQETTSEKKEVSSYIPSSEKRGKKSRVYLDIQIGNTLAGRIEIELRGDVVPKTAENFRALCTGEAGFGYKKSSFHRIIPQFMCQGGDFTKGNGTGGKSIYGGKFEDENFVLKHTGPGTLSMANAGSNTNGSQFFICTEKTTWLDGKHVVFGQVVSGMNVVREMERCGSASGKPSKRVVIVDCGEL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 34739
Sequence Length: 315
EC: 5.2.1.8
|
Q26516 | EDVSDDEMRTKKQKRNLPRVFFDIRIGNADRGRIVMELRSDIVPRTAENFRALCTGDRGFGYHNCCFHRVIPQFMCQGGDFVKGDGTGGKSIYGRKFDDENFQLRHEGFGVLSMANSGPNTNGSQFFICTTKCDWLDGKHVVFGRVVDGQNVVKKMESVGSKSGKVKEPVTISRCGELI | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 20050
Sequence Length: 179
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
Q26548 | MPMDYQTEKHRGFAFVEFEEVEDAMSAIDNMNESEIFGRTIRVNVARPVRIREGWSRPVWSDENWLKKYGSAPLEGRKLDEPDIVNPSDTSENVEDLSDEEMRTKKQKRNLPRVFFDIRIGNGDAGRIVMELRSDIVPRTAENFRALCTGERGFGYHNCCFHRVIPQFMCQGGDFVKGDGTGGKSIYGRKFDDENFQLRHEGFGVLSMANSGPNTNGSQFFICTTKCDWLDGKHVVFGRVVDGQNVVKKMESVGSKSGKVKEPVIISRCGELI | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 30905
Sequence Length: 273
Subcellular Location: Cytoplasm
EC: 5.2.1.8
|
P30404 | MMLALRCGPRLLGLLSGPRSAHLRLPAVRACSSGSGSHGSSSSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFKLKHEGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS | Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (By similarity). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).
PTM: Acetylated at Lys-168; deacetylated at Lys-168 by SIRT3.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 22019
Sequence Length: 208
Subcellular Location: Mitochondrion matrix
EC: 5.2.1.8
|
P30405 | MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS | Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding . Involved in regulation of the mitochondrial permeability transition pore (mPTP) . It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated . In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis . Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis .
PTM: Acetylated at Lys-167; deacetylated at Lys-167 by SIRT3.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 22040
Sequence Length: 207
Subcellular Location: Mitochondrion matrix
EC: 5.2.1.8
|
Q99KR7 | MLALRCGPRLLGLLSGPRSAPLLLSATRTCSDGGARGANSSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS | Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (By similarity). Involved in regulation of the mitochondrial permeability transition pore (mPTP) . It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated . In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis . Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels . Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).
PTM: Acetylated at Lys-166; deacetylated at Lys-166 by SIRT3.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 21737
Sequence Length: 206
Subcellular Location: Mitochondrion matrix
EC: 5.2.1.8
|
Q13427 | MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPKSKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRKHKKEKKKRKKSKKSASSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERKNRERERERECNPPNSQPASYQRRLLVTRSGRKIKGRGPRRYRTPSRSRSRDRFRRSETPPHWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKERKITDHRNVSESPNRKNEKEKKVKDHKSNSKERDIRRNSEKDDKYKNKVKKRAKSKSRSKSKEKSKSKERDSKHNRNEEKRMRSRSKGRDHENVKEKEKQSDSKGKDQERSRSKEKSKQLESKSNEHDHSKSKEKDRRAQSRSRECDITKGKHSYNSRTRERSRSRDRSRRVRSRTHDRDRSRSKEYHRYREQEYRRRGRSRSRERRTPPGRSRSKDRRRRRRDSRSSEREESQSRNKDKYRNQESKSSHRKENSESEKRMYSKSRDHNSSNNSREKKADRDQSPFSKIKQSSQDNELKSSMLKNKEDEKIRSSVEKENQKSKGQENDHVHEKNKKFDHESSPGTDEDKSG | Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding . May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 88617
Sequence Length: 754
Domain: The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II.
Subcellular Location: Nucleus matrix
EC: 5.2.1.8
|
Q4WCM6 | MEDIHSGPATNTNPIVFFDIALGGVPLGRIKMELFADVTPRTAENFRRFCTGESKNSQGKPQGYKNSKFHRVIKDFMIQGGDFVNGDGTGSCTIYGTPKFADENFVLKHDRAGVLSMANSGPNTNGCQFFITTTATPFLNGKHVVFGQVVDGMDIVRMIENTRTIRDKPSQDVIITQCGEM | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 19860
Sequence Length: 181
Subcellular Location: Nucleus
EC: 5.2.1.8
|
Q2TZ33 | MDSQVTSSAKTPNPVVFFDITLGGESLGRIKMELFTSITPRTAENFRQFCTGESKSPQGRPQGYKNSKFHRVIKDFMIQGGDFVNGDGTGSRTIYGTPRFQDENFILKHDQPGLLSMANSGPNTNGCQFFITTTATPFLNNKHVVFGQVVEGMDVVRMIENTRTTRDKPNQDVTIIQCGEM | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 20110
Sequence Length: 181
Subcellular Location: Nucleus
EC: 5.2.1.8
|
Q5E022 | MLTVNSYFEDKVKSIGFEQNSNAISVGVMLPGNYTFGTAAAEKMSVITGALTIKRSTDADWVTFSSGEDFSVEGNSSFEVKVEIETAYLCEYL | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 10139
Sequence Length: 93
EC: 2.4.2.1
|
Q9V521 | MADKKNLLLLFDHPTEPVFMDKGKRVTVFDVPDSFLTDRYRPISNEVQSRVGDKVEQRVPVREISIPDLRIPMSLGRDEQFSLFLPKHRRIAGRLIDIFMNMRSVDDLQSVAVYARDRVNPVLFNYALSVALLHRPDTQGLDLPSFSQTFPDRFIDSQVIRKMREESFVVQPGSRMPITIPRDYTASDLDPEHRLWYFREDLGINLHHWHWHLVYPFEASDRSIVAKDRRGELFYYMHQQVIARYNAERFSNNLARVLPFNNLRDPIAEGYFPKMDSLVASRAWPPRFESTRLSDLNRESDQLNVEIGDLERWRDRIYEAIHQGFVMDERGNRVPLDEATGIDTLGNMIESSILSPNRVLYGDLHNNGHTFISYAHDPTSKHLESFGVMGDVSTAMRDPVFYKWHSYIDRIFQEHKSRLPAYTENQLNYPGVSIAGIQVDTNGGRPNNLTTFWQQSDVDMSRGFDFLPRGNVFARFTHLQHLPFTYTISLNNDSGAQRFGYVRIFMAPKNDERGQPMLMRDQRSMMIELDKFVTSLNPGPNTIRRRSTESSVTIPFERTFRNLDANRPAAGTPEELEFNFCGCGWPNHMLVPKGLPEGLQCVLFIMVSNYENDRIDQQLVGRCSDAASYCGVRDRLYPDRQSMGFPFDRLPRSGVDRLVNFLTPNMSIVDVNIRHENRTVQRPN | Cofactor: Binds 2 copper ions per subunit.
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinonee (By similarity).
PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme.
Catalytic Activity: 2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone
Sequence Mass (Da): 79285
Sequence Length: 684
Subcellular Location: Secreted
EC: 1.14.18.1
|
Q8I6K2 | MSNTAVLNDLVALYDRPTEPMFRVKAKKSFKVPKEYVTDRFKNVAVEISNRFGEDDSETVTIDSVPLPDLADILTLGREENFSLFIPKHRNLSAKLINIFLQAENPKHLLSIACYAHDRVNPYLFIYALSVALIHRKDTKSLKIPNQIQTFPDKYFDSQVFSQGKEEMTVVPQGLRRPIEIPRDYTASDLEEEHRVAYWREDLGINLHHWHWHLVYPTDGGEIVTKKDRRGELFYYSHQQIVARYNFERFCNALKRVERLTDWQGPIKEAYFPKLDSLVAKRAYPARVQDMTMQDLDIPGQNIKVDVDDMIRWRDRIYRAIADGFITATNGSKMNLDDVTGIDILGNIMESSELSPNRQLYGNLHGFGHLMLSYIHDPRSHHLEPFGVIGDFTTAMRDPIFYRWHAFVDDVFQQFNGSLPRYTAEQLDYAGVQITDVNIKTPNAPDNEFRTFWQQSDVDMSRGVDFQDPGSVFVRFTHLNHEPFSYNITVNNTGNGVQEGTCRIFLAPATDERGNPWLFNNQRVMFVEMDRFKVTLRQGQNTITRNSTQSSVTIPFERTFRDLDTNRPAEGSEELDIFNFCGCGWPHHLLVPKGTPDGFKAQLFVMISNYADDKVEQDLSGSCNDAESYCGVRGGKYPDKRPMGYPFNRVARQGADTLQRFLTGNMIVQNCRIVHSDRTVRPRS | Cofactor: Binds 2 copper ions per subunit.
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (By similarity). Catalyzes the oxidation of o-diphenols (N-acetyldopamine, 4-methylcatechol and dopamine) . Cannot oxidize monophenols and p-phenols (L-tyrosine, tyramine, gentisic acid and hydroquinone) . Binds to the surface of hemocytes and is involved in hemocyte melanization (By similarity). Activation of the enzyme in response to bacterial lipopolysaccharides (LPS) suggests it may play a role in innate immunity .
PTM: Precursor cleaved by PPAF1.
Sequence Mass (Da): 78820
Sequence Length: 684
Subcellular Location: Secreted
EC: 1.14.18.-
|
Q9MB14 | MASFTTSPCTSAAPKTPKSLSSSATISSPLPKPSQIHIATAKRTHHFKVSCNAPNGDSQPKLDRRDVLLGLGGLAGAASLINNPLAFAEPIHAPEISKCVVPPKDLPPDAIVDNCCPPLATNVIPYKVPKTSPSAMKIRPAIHRMDKEYIAKFEKAIRLMKELPADDPRNFYQQALVHCAYCNGGYVQTDYPDKEIQVHNSWLFFPFHRWYLYFYERILGKLIGDPTFGLPFWNWDTPAGMLIPQYFRNQNSPLYDENRNQSHLPLVMDLGYAGTDTDVTDQERISNNLALMYKSMVTNAGTAELFLGKPYKAGDDPVNKGGGSIENIPHTPVHRWVGDVKPRTQNGEDMGNFYSAGRDILFYCHHSNVDRMWTIWQQLGGKGRRRDFTDSDWLDATFIFYDENKQAVRVRVGDALDNQKLGYKYEFTNLPWLNSKPLPTKKKTGLAARSKAPFVTDVFPLTLDKVVQVKVPRPKKSRSKEEKEAEEEILEIQGIEVAIDQYAKFDVYLNDEDEPEAGKEKAEYAGSFAHLPHKHTGSKKIRTSLSLGLNEPLEDLGAEDDDAVLVTLAPKVGGGVVTVENIKIVYGS | Cofactor: Binds 2 copper ions per subunit.
Function: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.
Catalytic Activity: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
Sequence Mass (Da): 65651
Sequence Length: 588
Subcellular Location: Plastid
EC: 1.10.3.1
|
C7FF04 | MSDKKSLMPLVGIPGEIKNRLNILDFVKNDKFFTLYVRALQVLQARDQSDYSSFFQLGGIHGLPYTEWAKAQPQLHLYKANYCTHGTVLFPTWHRAYESTWEQTLWEAAGTVAQRFTTSDQAEWIQAAKDLRQPFWDWGYWPNDPDFIGLPDQVIRDKQVEITDYNGTKIEVENPILHYKFHPIEPTFEGDFAQWQTTMRYPDVQKQENIEGMIAGIKAAAPGFREWTFNMLTKNYTWELFSNHGAVVGAHANSLEMVHNTVHFLIGRDPTLDPLVPGHMGSVPHAAFDPIFWMHHCNVDRLLALWQTMNYDVYVSEGMNREATMGLIPGQVLTEDSPLEPFYTKNQDPWQSDDLEDWETLGFSYPDFDPVKGKSKEEKSVYINDWVHKHYGFVTTQTENPALRLLSSFQRAKSDHETQYALYDWVIHATFRYYELNNSFSIIFYFDEGEGCTLESIIGTVDAFRGTTSENCANCARSQDLIAEGFVHLNYYIGCDIGQHADHEDDAVPLYEPTRVKEYLKKRKIGCKVVSAEGELTSLVVEIKGAPYYLPVGEARPKLDHEKPIVILDDIIHRVN | Cofactor: Binds 2 copper ions per subunit.
Function: Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores (By similarity).
PTM: The C-ter is probably cleaved after Gly-392 since the mature active protein is smaller than the protein encoded by the gene.
Catalytic Activity: 2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone
Sequence Mass (Da): 66267
Sequence Length: 576
EC: 1.14.18.1
|
C0HJM0 | HWHLVYPIEAPDRSIVDKDRRGELFYYMHQQIIARYNAERYNAERLSNHMARVQPFNNLDEPIAEGYFPKM | Cofactor: Binds 2 copper ions per subunit.
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone (By similarity).
PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme.
Catalytic Activity: 2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone
Sequence Mass (Da): 8623
Sequence Length: 71
Subcellular Location: Secreted
EC: 1.14.18.1
|
Q8MZM3 | MATLTQKFHGLLQHPLEPLFLPKNDGTLFYDLPERFLTSRYSPIGQNLANRFGPNSPASSQVSNDTGVPPTVVTIKDLDELPDLTFATWIKRRDSFSLFNPEHRKAAGKLTKLFLDQPNADRLVDVAAYARDRLNAPLFQYALSVALLHRPDTKSVSVPSLLHLFPDQFIDPAAQVRMMEEGSIVLDENRMPIPIPMNYTATDAEPEQRMAFFREDIGVNLHHWHWHLVYPASGPPDVVRKDRRGELFYYMHQQLLARYQIDRYAQGLGRIEPLANLREPVREAYYPKLLRTSNNRTFCPRYPGMTISDVARSADRLEVRIADIESWLPRVLEAIDAGFAVSDDGVRVPLDETRGIDVLGNILERSAISINRNLYGDVHNMGHVLLAFIHDPRGTYLESSGVMGGVATAMRDPIFYRWHKFIDNIFLRNKARLAPYTMAELSNSNVTLEALETQLDRAGGAVNSFVTFWQRSQVDLRAGIDFSAAGSAFVSFTHLQCAPFVYRLRINSTARSNRQDTVRIFLLPRQNEQGRPLSFEDRRLLAIELDSFRVNLRPGMNNIVRQSSNSSVTIPFERTFGNVEQANAGNAQSRFCGCGWPAHMLLPKGNANGVEFDLFAMVSRFEDDNANVNYDENAGCDDSYAFCGLRDRVYPSRRAMGFPFDRRASNGVRSVADFVAPYKNMRLATVTLRFMNTIIDRPTN | Cofactor: Binds 2 copper ions per subunit.
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (Probable). Catalyzes the oxidation of o-diphenols such as dopamine . Also oxidizes monophenols such as tyramine .
PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme.
Catalytic Activity: O2 + 2 tyramine = 2 dopamine
Sequence Mass (Da): 79293
Sequence Length: 700
Subcellular Location: Secreted
EC: 1.10.3.-
|
Q08303 | MASLCSNSSSTSLKTPFTSSTTCLSSTPTASQLFLHGKRNKTFKVSCKVTNTNGNQDETNSVDRRNVLLGLGGLYGVANAIPLAASAAPTPPPDLSSCNKPKINATTEVPYFCCAPKPDDMSKVPYYKFPSVTKLRIRPPAHALDEAYIAKYNLAISRMKDLDKTQPDNPIGFKQQANIHCAYCNGGYSIDGKVLQVHNSWLFFPFHRWYLYFYERILGSLIDDPTFGLPFWNWDHPKGMRFPPMFDVPGTALYDERRGDQIHNGNGIDLGYFGDQVETTQLQLMTNNLTLMYRQLVTNSPCPLMSLVDLTLFGSTVEDAGTVENIPHSPVHIWVGTRRGSVLPVGKISNGEDMGNFYSAGLDPLFYCHHSNVDRMWNEWKATGGKRTDIQNKDWLNSEFFFYDENGNPFKVRVRDCLDTKKMGYDYHATATPWRNFKPKTKASAGKVNTGSIPPESQVFPLAKLDKAISFSINRPASSRTQQEKNAQEEVLTFNAIKYDNRDYIRFDVFLNVDNNVNANELDKAEFAGSYTSLPHVHRVGDPKHTATATLRLAITELLEDIGLEDEDTIAVTLVPKKGDISIGGVEIKLAIVKLVCVVNLLTLQLNKDRFCYDSVFVCWFVCLFFNFHV | Cofactor: Binds 2 copper ions per subunit.
Function: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.
Catalytic Activity: 2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
Sequence Mass (Da): 70616
Sequence Length: 630
Subcellular Location: Plastid
EC: 1.10.3.1
|
Q8S9J1 | MASGAVADHQIEAVSGKRVAVVGAGVSGLAAAYKLKSRGLNVTVFEADGRVGGKLRSVMQNGLIWDEGANTMTEAEPEVGSLLDDLGLREKQQFPISQKKRYIVRNGVPVMLPTNPIELVTSSVLSTQSKFQILLEPFLWKKKSSKVSDASAEESVSEFFQRHFGQEVVDYLIDPFVGGTSAADPDSLSMKHSFPDLWNVEKSFGSIIVGAIRTKFAAKGGKSRDTKSSPGTKKGSRGSFSFKGGMQILPDTLCKSLSHDEINLDSKVLSLSYNSGSRQENWSLSCVSHNETQRQNPHYDAVIMTAPLCNVKEMKVMKGGQPFQLNFLPEINYMPLSVLITTFTKEKVKRPLEGFGVLIPSKEQKHGFKTLGTLFSSMMFPDRSPSDVHLYTTFIGGSRNQELAKASTDELKQVVTSDLQRLLGVEGEPVSVNHYYWRKAFPLYDSSYDSVMEAIDKMENDLPGFFYAGNHRGGLSVGKSIASGCKAADLVISYLESCSNDKKPNDSL | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 55630
Sequence Length: 508
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Plastid
EC: 1.3.3.4
|
P55826 | MELSLLRPTTQSLLPSFSKPNLRLNVYKPLRLRCSVAGGPTVGSSKIEGGGGTTITTDCVIVGGGISGLCIAQALATKHPDAAPNLIVTEAKDRVGGNIITREENGFLWEEGPNSFQPSDPMLTMVVDSGLKDDLVLGDPTAPRFVLWNGKLRPVPSKLTDLPFFDLMSIGGKIRAGFGALGIRPSPPGREESVEEFVRRNLGDEVFERLIEPFCSGVYAGDPSKLSMKAAFGKVWKLEQNGGSIIGGTFKAIQERKNAPKAERDPRLPKPQGQTVGSFRKGLRMLPEAISARLGSKVKLSWKLSGITKLESGGYNLTYETPDGLVSVQSKSVVMTVPSHVASGLLRPLSESAANALSKLYYPPVAAVSISYPKEAIRTECLIDGELKGFGQLHPRTQGVETLGTIYSSSLFPNRAPPGRILLLNYIGGSTNTGILSKSEGELVEAVDRDLRKMLIKPNSTDPLKLGVRVWPQAIPQFLVGHFDILDTAKSSLTSSGYEGLFLGGNYVAGVALGRCVEGAYETAIEVNNFMSRYAYK | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 57695
Sequence Length: 537
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Plastid
EC: 1.3.3.4
|
P0AFL8 | MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTASSLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQEQQLMMATLVRYHRKAIKLDDLPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNALVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA | Function: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain.
Catalytic Activity: [phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58136
Sequence Length: 513
Subcellular Location: Cell membrane
EC: 3.6.1.11
|
P44828 | MNDSILEPKHRGNVREIAAIDLGSNSFHMIVARIVNGSIQVLSRLKQKVKLAEGLDENAVLNQEAITRGVNCLALFAERLQGFPMENVNVVGTYTLRRAVNNDEFLRQAAKVFPYPINIISGQTEAKTIYAGVCHTQPEKGRKLVIDIGGGSTEMIIGDDFTPLMAESRHMGCVSFATQFFTDGIISPENFQRARQSAVNKIEDLGLEYRKLGWQSVLGSSGTIKTVAQVIATNLDPNGTITAERLNALIEQTLQAKHFTELNINGLNQDRVDVFVPGLAILSAVFDVFHIQQMRYSDGALREGVIYSLEKNFQVADIRASTA | Function: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain.
Catalytic Activity: [phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35566
Sequence Length: 323
Subcellular Location: Cell membrane
EC: 3.6.1.11
|
Q9ZN70 | MDLQSMPQKPAEAFPLIAALDLGSNSFHLCLAKANIHGEVRILERLGEKVQLAAGLDEERNLSEEATQRGLDCLRRFAQFISGMPQGSVRVVATNALREARNRSDFIRRAEEVLGHPVEVISGREEARLIYLGVANSMPDSGGRRLVSDIGGGSTEFIIGQGFESELRESLQMGCVSYTQRYFRDGKITPARYAQAYTAARLELMGIENSLRRLGWQQAVGASGTIRAVALAIKAGGHGNGEISPDGLAWLKRKVLKLGDVEKLDLEGIKPDRRTIFPAGLAILEAIFDALELEQMVHSEGALREGVLYDLVGRHQHEDVRERTISSLMQRYHVDPEQASRVEAKALKVLAEVGDAWELNGELHRDLLSWGARVHEIGLDIAHYHYHKHGAYLIEHSDLAGFSRQDQQMLSLLVRGHRRNIPADKLAEFAEEGDKLVRLCIVLRFAILFHHIRGTQEMPSVRLKAEPKSLSVTFPEGWLEANPLTQADFAQEAEWLKRVGYSLNVR | Function: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain . Has also polyphosphate:ADP phosphotransferase activity, catalyzing the production of ATP from ADP and polyP .
Catalytic Activity: [phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56419
Sequence Length: 506
Domain: The catalytic activity is found in the N-terminal region formed by subdomains I and II. The peptide that connects subdomains II and III is also essential for activity. The C-terminal domain may be important for the recognition and/or interaction with long polyP chains.
Subcellular Location: Cell membrane
EC: 3.6.1.11
|
Q9KU08 | MTTVVSNAREIAAIDLGSNSFHMVVAKVVDQDLQLISRHKQRVRLAAGLDEQKNLDEESIQRGLECLAMFAERLQGFEPRNVRIAATHTLRQARNANLFIQRALDVLPFPIEIIPGSEEARLIYLGVAHTQPQADSMLVVDIGGGSTEMIIGKGFEAELLNSKQMGCVNFTERYFANGKLSRKNFAQAIVASEQKLESIASKYRKKGWQMAFGSSGTIKAIHEVLIGQGHEDGLITFERLSKLIEKLCEWDSIDDLQLPGLTDDRKPVFAAGVAILSAIFHGLNIKEMHFSDGALREGLLYEMEDRFKYSDIRLRTTENLAAKHLVDLEHAAKVKGHAREFLAQVANELGLPEGSELCDLLEWGALLHEVGLSINLQGFHRHSAYILRHNNMAGFNSEQQLVLSNLARFQRKSLKLNELDDFSLFKKKHIIGLIRVLRLAIVVNGQRNDDPLPPLTLSAKDDEWRLECEQPDWLENNKLLHADLQTEQEYWREVGWQLLF | Function: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain.
Catalytic Activity: [phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56445
Sequence Length: 500
Subcellular Location: Cell membrane
EC: 3.6.1.11
|
P11612 | MAVLTTHEIDCIIKELTSLNGSECTLKEELIERLIQQTREVIKWQPMLLELQAPVNICGDIHGQFTDLLRIFKACGFPPKANYLFLGDYVDRGKQSLETICLLFAYKVKYPLNFFLLRGNHESASINKIYGFYDEIKRRHTVRLWHSFTDCFNWLPVAALVGERIFCCHGGLSPSLRNLQQINHIQRPTDIPDEGIMCDLLWADLNHTTKGWGHNDRGVSFTFDKVIVRDFLKAFDLQLMVRAHEVVEDGYEFFANRQLVTVFSAPNYCGMMNNAGGVMSVSTDLICSFVIILPCHKYKMIATDANQMPTNEEE | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35980
Sequence Length: 314
EC: 3.1.3.16
|
P26570 | MGNSSSKSSKKDSHSNSSSRNPRPQVSRTETSHSVKSAKSNKSSRSRRSLPSSSTTNTNSNVPDPSTPSKPNLEVNHQRHSSHTNRYHFPSSSHSHSNSQNELLTTPSSSSTKRPSTSRRSSYNTKAAADLPPSMIQMEPKSPILKTNNSSTHVSKHKSSYSSTYYENALTDDDNDDKDNDISHTKRFSRSSNSRPSSIRSGSVSRRKSDVTHEEPNNGSYSSNNQENYLVQALTRSNSHASSLHSRKSSFGSDGNTAYSTPLNSPGLSKLTDHSGEYFTSNSTSSLNHHSSRDIYPSKHISNDDDIENSSQLSNIHASMENVNDKNNNITDSKKDPNEEFNDIMQSSGNKNAPKKFKKPIDIDETIQKLLDAGYAAKRTKNVCLKNNEILQICIKAREIFLSQPSLLELSPPVKIVGDVHGQYGDLLRLFTKCGFPPSSNYLFLGDYVDRGKQSLETILLLFCYKIKYPENFFLLRGNHECANVTRVYGFYDECKRRCNIKIWKTFIDTFNTLPLAAIVAGKIFCVHGGLSPVLNSMDEIRHVVRPTDVPDFGLINDLLWSDPTDSPNEWEDNERGVSYCYNKVAINKFLNKFGFDLVCRAHMVVEDGYEFFNDRSLVTVFSAPNYCGEFDNWGAVMSVSEGLLCSFELLDPLDSAALKQVMKKGRQERKLANQQQQMMETSITNDNESQQ | Cofactor: Binds 2 manganese ions per subunit.
Function: Essential for the maintenance of cell size and integrity in response to osmotic stress.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 77491
Sequence Length: 692
EC: 3.1.3.16
|
B0XUR7 | MGQSHSKGNSGPGDSLQSYPSFSRSDTKESLRSLRGSIRSKIRSSDSPRGSTAGLSDDKSDAASVKSTTSRRSSTNQSVQSPDDTPSQPDAPEPPPSPSLSSSLKRGHKDVNAMQQSGEVDHVSDVPPTGAAPTGPSTQKVGESILIKRENQLNPILDFIMNAPLETSGSPGMGMGALKSIDLDDMISRLLDAGYSTKVTKTVCLKNAEIMAICSAARELFLSQPALLELSAPVKIVGDVHGQYTDLIRLFEMCGFPPASNYLFLGDYVDRGKQSLETILLLLCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNIKIWKTFIDTFNCLPIAATVAGKIFCVHGGLSPSLSHMDDIRGIARPTDVPDYGLLNDLLWSDPADMEEDWEPNERGVSYCFGKKVIMNFLQRHDFDLVCRAHMVVEDGYEFYQDRILVTVFSAPNYCGEFDNWGAIMSVSGELLCSFELLKPLDSTALKNHIKKGRKERNSMLSSPVSPPLLRFVVAKEDHNLFVQHRRDACGLFLAYPSLVTSWGISR | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalytic subunit of protein phosphatase Z (PPZ) involved in iron assimilation . Regulates secondary metabolites production, including gliotoxin, pyripyropene A, fumagillin, fumiquinazoline A, triacetyl-fusarinine C, and helvolic acid . Plays a key role in pathogenicity .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 59548
Sequence Length: 540
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
A0A166Z003 | MPDNHGPWGLRWRAKPSFILTTVAMGLFTDLVLYGILLPALPFTMRNRFDIPNAEIQHYTSAFLATYAGASVFFSVPAGWAASKLGSRQLFLGGLMFLVVATAIFAFSTSLVLLVVSRLLQGMSTAVVWTAGLDMVQDTVEPSQVGETIGTIFATISVGELAAPVLGGVLYERGGISAVFAVSAVLLAIDLALRALVIDKKTAVKYESPRLIRFPVERNMSDDHVASAPTVMEAQESVHEGTRLLPQVDDDGDHYKIDRELGSIVRAIPLLYCFREPRLHLAMLLSFVQALFIGTFDATVPTVAESLFHFSSLQVGLVFIALMLPYFALGRLSGQAIDRFGTKAAATSGYAFLVPCLMLLGLPEKNLVPKEANVALFCTILALNGIGLAVVTSPGYVEAIDVTTKYQVANPGHFGENGPYAQLFGFSSLYFFTGLAVGPLLGGFLRANFGNAVMGAVYAAISGVTAIVSFLFVGVRRFGPGLV | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity . Probably involved in the secretion of peramine and other pyrrolopyrazines (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51735
Sequence Length: 483
Subcellular Location: Membrane
|
A0A166YZY9 | MATDTAVTGAPETTELRLASGNGPVTRTVLRTPVRDALPSEVPLIDISPIFSTCVADRKAVARKIHDAATNIGFFYIQNHRVPSQDIDLAYSASQDFFRQEMEVKVEADAKDGPFDSGYRGPGTQRVNPTEGADLRETYSILYDPMLDPTVPDPANIPEPASRFLHLGRAPFESTATLPHFKDAFVRYFQACLVLARALTRAFALSLDLPESAFDGKVQYPDASLEINFYPPISTGHAVSAPGDADTRVSIGSHTDFLLFTILWQDSNGGLQVLNREGQWIRAIPVEGTFVVNIGDYLQRVTNDKYVSTVHRAQNFSGRERVSMPFFWGFGMHESCQVLRNCCGEDEKSKYDEVKCVDWVSRRLGNLFDLSDKG | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity . The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine . The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine (By similarity). The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine (By similarity). The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase (By similarity). Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine (By similarity). This final oxidation to give the pyrrole functionality may be spontaneous (By similarity). In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium rileyi that contains additionnal pyrrolopyrazine biosynthesis genes (Probable). The 2-oxoglutarate-Fe(II) type oxidoreductases ppzC and ppzD could be candidates for conversion of proline into an oxidized derivative to be used by the ppzA A1-domain as substrate (Probable). The other ppz genes encode proteins predicted to derivatize peramine into more complex pyrrolopyrazine metabolites (Probable).
Sequence Mass (Da): 41480
Sequence Length: 374
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.11.-
|
A0A166YZY4 | MARTPERRVRTLDFAQFCHGEPSSSHGFCRELVDCLRSLGFVKIRNHGISGEEIEKVFVMNKLFFSLPQAAKAKAAHPPEANPHRGYSYVGQEKLSRVKDYEKGKRSIVDVYDIKESYDQGPAVDKLYPNRWPDKQDIPGFRVVMEKFYERCHQVHQDVLRAIATGFDLSPSFLTDLCCENTSELRLNHYPGVHPSSLRKGAKRISEHTDFGTVTLLFQDSVGGLEIEDQNSPGTYFPVSSERKSDMIVNVGDCIQRWTNDKILSTSHRVVLPEDRDALIKDRYSVAYFGKPSRSQLVSPLREFVKEGEKPKYSAISAWQYNQEKLVLTYGGDEEILVPKPSSSVCTGVGQLQ | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: 2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity . The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine . The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine (By similarity). The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine (By similarity). The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase (By similarity). Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine (By similarity). This final oxidation to give the pyrrole functionality may be spontaneous (By similarity). In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium rileyi that contains additionnal pyrrolopyrazine biosynthesis genes (Probable). The 2-oxoglutarate-Fe(II) type oxidoreductases ppzC and ppzD could be candidates for conversion of proline into an oxidized derivative to be used by the ppzA A1-domain as substrate (Probable). The other ppz genes encode proteins predicted to derivatize peramine into more complex pyrrolopyrazine metabolites (Probable).
Sequence Mass (Da): 39996
Sequence Length: 353
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.11.-
|
A0A166YZU9 | MLSIIHVGWLELVWFVALYPFACWTLFAVLKSVYRITLHPLAKFPGPKLAGASYCYEFWYEIVCGIQYTQKIIKLHEQYGPIVRINPDELHFNDIDFVDVVYTAGARKRDKSRHYLAGFEGSIIRFVSSDFHSFLIDTRVKKPERLKRVVLGAERHHDAKDCPMFLELLNSNLPAQEKSKQRLMYEANGATLAGSGSTAIALSNIVYNLVANPRIGHKLRSELMRKVSASKNLPTWSTLEELPYLTAVIHEGLRSMYDPSKERLPYDPSQERLPRVATEEELIYEGGSALGKSKYVIPRGYAISTSAHVVHSDESIFPNASQFDPERWLDRDGQRNKELERHLLSFSKGSRHCLGMHCRRATCLAIPASARNGTSGYQFTSGQLEYKVQERQ | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity . The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine . The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine (By similarity). The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine (By similarity). The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase (By similarity). Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine (By similarity). This final oxidation to give the pyrrole functionality may be spontaneous (By similarity). In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium rileyi that contains additionnal pyrrolopyrazine biosynthesis genes (Probable). The 2-oxoglutarate-Fe(II) type oxidoreductases ppzC and ppzD could be candidates for conversion of proline into an oxidized derivative to be used by the ppzA A1-domain as substrate (Probable). The other ppz genes encode proteins predicted to derivatize peramine into more complex pyrrolopyrazine metabolites (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 44641
Sequence Length: 392
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
Q89FG1 | MLEKQRSTAETFGIPLAVLLEITHRCPLQCPYCSNPVELDRSGKELTTDEWKKVLSELAEIGVLQVHFSGGEPTARKDLVELVKHASDVGLYTNLITSAVLLTRERLSELADAGLCHVQISFQGVEEGLADRVAGYRNAHRKKLEVAKWTRELDLPLTVNAVMHRQNLHQLPDIIQMSIDLDADRLEVANVQYYGWALKNRAALMPTVAQLDECTRLVEEARERLKGRLSIDYVVPDYYALRPKKCMGGWGRQFFNISPAGKVLPCHAAESITGLDFESVRSNHSIAWIWQNSEAFNRYRGTGWMKEPCKSCEFREIDFGGCRCQAFALTGDAANTDPACALSPLHETIFKQAEREAEGETNRFLYRNFAGGTLEPENDA | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
Catalytic Activity: [PQQ precursor protein] + S-adenosyl-L-methionine = 5'-deoxyadenosine + E-Y cross-linked-[PQQ precursor protein] + H(+) + L-methionine
Sequence Mass (Da): 42687
Sequence Length: 380
Pathway: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
EC: 1.21.98.4
|
Q9L3B0 | MTLPSPPMSLLAELTHRCPLSCPYCSNPLELERKAAELDTATWTAVLEQAAELGVLQVHFSGGEPMARPDLVELVSVARRLNLYSNLITSGVLLDEPKLEALDRAGLDHIQLSFQDVTEAGAERIGGLKGAQARKVAAARLIRASGIPMTLNFVVHRENVARIPEMFALARELGAGRVEIAHTQYYGWGLKNREALLPSRDQLEESTRAVEAERAKGGLSVDYVTPDYHADRPKPCMGGWGQRFVNVTPSGRVLPCHAAEIIPDVAFPNVQDVTLSEIWNISPLFNMFRGTDWMPEPCRSCERKERDWGGCRCQAMALTGNAANTDPVCSLSPYHDRVEQAVENNMQPESTLFYRRYT | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
Catalytic Activity: [PQQ precursor protein] + S-adenosyl-L-methionine = 5'-deoxyadenosine + E-Y cross-linked-[PQQ precursor protein] + H(+) + L-methionine
Sequence Mass (Da): 39656
Sequence Length: 358
Pathway: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
EC: 1.21.98.4
|
P27507 | MSQSKPTVNPPLWLLAELTYRCPLQCPYCSNPLDFARQDKELTTEQWIEVFRQARAMGSVQLGFSGGEPLTRKDLPELIRAARDLGFYTNLITSGIGLTESKLDAFSEAGLDHIQISFQASDEVLNAALAGNKKAFQQKLAMAKAVKARDYPMVLNFVLHRHNIDQLDKIIELCIELEADDVELATCQFYGWAFLNREGLLPTREQIARAEQVVADYRQKMAASGNLTNLLFVTPDYYEERPKGCMGGWGSIFLSVTPEGTALPCHSARQLPVAFPSVLEQSLESIWYDSFGFNRYRGYDWMPEPCRSCDEKEKDFGGCRCQAFMLTGSADNADPVCSKSPHHHKILEARREAACSDIKVSQLQFRNRTRSQLIYQTRDL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
Catalytic Activity: [PQQ precursor protein] + S-adenosyl-L-methionine = 5'-deoxyadenosine + E-Y cross-linked-[PQQ precursor protein] + H(+) + L-methionine
Sequence Mass (Da): 42914
Sequence Length: 380
Pathway: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
EC: 1.21.98.4
|
Q608P0 | MAGSEKSSLTKPRWLLAELTYACPLQCPYCSNPLDYARLGDELSTEEWKRVLSEARALGAVQLGLSGGEPLTRRDLAEIVTHARQLGYYTNLITSGYGLDEVRIAELKSAGLDHIQVSIQSPEKLLNDELAGTESFEHKLKVARWVKQHGYPMVLCVVIHRQNIHQMQQILEMADELGADYLELANTQYYGWALLNRDHLLPTREQFAEAEAIAQSYKEKVKGRMKIYYVVPDYYEDRPKACMNGWGTTFLTIAPDGMALPCHAARELPGLNCPSVRDFSIREIWYESAAFNRFRSYGWMKEPCRSCPEKEKDFGGCRCQAYLMTGDMADADPVCSKSPHHHRVLEAIASTQRSASDKPLFFRNARNSRALTG | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
Catalytic Activity: [PQQ precursor protein] + S-adenosyl-L-methionine = 5'-deoxyadenosine + E-Y cross-linked-[PQQ precursor protein] + H(+) + L-methionine
Sequence Mass (Da): 42180
Sequence Length: 373
Pathway: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
EC: 1.21.98.4
|
P71517 | MNAPTPAPSPVDVIPAPVGLLAELTHRCPLRCPYCSNPLELDRRSAELDTQTWLRVLTEAAGLGVLHVHLSGGEPTARPDIVEITAKCAELGLYSNLITSGVGGALAKLDALYDVGLDHVQLSVQGVDAANAEKIGGLKNAQPQKMQFAARVTELGLPLTLNSVIHRGNIHEVPGFIDLAVKLGAKRLEVAHTQYYGWAYVNRAALMPDKSQVDESIRIVEAARERLKGQLVIDLVVPDYYAKYPKACAGGWGRKLMNVTPQGKVLPCHAAETIPGLEFWYVTDHALGEIWTKSPAFAAYRGTSWMKEPCRSCDRREKDWGGCRCQALALTGDAANTDPACSLSPLHAKMRDLAKEEAAETPPDYIYRSIGTNVQNPLSEKAPL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
Catalytic Activity: [PQQ precursor protein] + S-adenosyl-L-methionine = 5'-deoxyadenosine + E-Y cross-linked-[PQQ precursor protein] + H(+) + L-methionine
Sequence Mass (Da): 41661
Sequence Length: 384
Pathway: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
EC: 1.21.98.4
|
Q9VAF7 | MGRKRGRKEYCPPIYKRQKVARVTNNGYLNFMTEYKKRFYGLSPQDMVHYAAKQWTQLSMAEKEAFKSKKPSTITLKSPAQYVACEMKSDVAGGQQSSCQRQSPSARLRESERRSSRSKTLCRSAKNRQRGKPKPQQSKRRLSHMGSAVAYIHFLRKFQRKNTELRTIDLLKTATRLWCRLPERHRHAFERPLWIVTIGKS | Function: Regulates chromatin compaction in spermatid nuclei and is essential for male fertility. Functions in parallel with other chromatin-condensing proteins such as ProtA, ProtB and Mst77F.
Sequence Mass (Da): 23554
Sequence Length: 201
Domain: The C-terminal part (169-201) is essential for male fertility and correct chromatin compaction in mature sperm.
Subcellular Location: Nucleus
|
Q1G3K7 | MIFRTNYIVIFIVSIFISMLWQPVHLSVFVILIVAWLYVYSRDNEPWVIFGSVIDDSTLVLVLLVLTIGIFLLTDVSRGIVIGVLAGLPVVLVHGMCRRNTEMLFVLEDDEEKVAMNTSSSSLSSSS | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14210
Sequence Length: 127
Subcellular Location: Endoplasmic reticulum membrane
|
P93829 | MANQVITGIKETAQSITGAARPWGDFLDLSAFSFPSSIADATTRVTQNLTHFRINYSIILSILLGLTLITRPIAILAFIAVGLAWFFLYFAREEPLTIFGFTIDDGIVAVLLIGLSIGSLVTTGVWLRALTTVGFGVLVLILHAALRGTDDLVSDDLESPYGPMLSTSGGGNDGARGDYSGI | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19325
Sequence Length: 182
Subcellular Location: Endosome membrane
|
Q9FRR1 | MNQKPPPYGYGGAGGGGVGPSSTSNTTIIGTLSARAKQTTQSMITTLRPWREILDLSALSLPRGYDEAMAHLKHNISYFRGNYALAVLAIVFLGLIYHPMSMIAFIVVFIGWILLYFSRDANDSIVISGKEVDDKIVLVLLSLVTVLALVYTDVGENVLVSLIIGLLIVGAHGAFRNTDDLFLDEESARRGGLVSAGSGNRPPSSYTPI | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22415
Sequence Length: 209
Subcellular Location: Endosome membrane
|
Q54SE2 | MSRIQQVNKSILIRSFCTGAPSKSNFSPVGNFLRIGDVVPDFSQDSSVGQINLYKTLGDSWGLFVSHPKDFTPICTTELGRLAKLKPEFEKRNCKILALSVDSVKDHLEWMKDIEETQKVKINYPIIADQDRKVADLYGMIHPNADNTFTVRSVFFISPDKRLRAQITLPASTGRNFNEIIRILDSFQLTDKYKVATPADWVDGDDCIIVPTVFDEDAKKLFPKGFPKIKSYLRVTPQPNK | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
Sequence Mass (Da): 27301
Sequence Length: 241
EC: 1.11.1.24
|
Q9NL98 | MSKAMIGKPAPEFTATAVVDGDFKSISLSDYKGKYVVLFFYPMDFTFVCPTEIIAFSEHVGEFKKLGVEVLAASTDSQFSHLAWINTPRKQGGLGEMKIPIISDNNHQISRDYGVLKEDDGIAYRGLFIIDPKGILRQITVNDLPVGRSVTETLRLVQAFQFVDKHGEVCPAGWTPGADTIKPGVKESKAYFEKH | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
Sequence Mass (Da): 21590
Sequence Length: 195
EC: 1.11.1.24
|
A0A0K3AUJ9 | MSLAPKMSKAFIGKPAPQFKTQAVVDGEFVDVSLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRAEEFKAINTVVLAASTDSVFSHLAWINQPRKHGGLGEMNIPVLADTNHQISRDYGVLKEDEGIAFRGLFIIDPSQNLRQITINDLPVGRSVDETLRLVQAFQFVEKHGEVCPAGWTPGSDTIKPGVKESQEYFKKH | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively . In I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide . In the intestine, plays a role in protecting cells against oxidative stress by detoxifying peroxides such as hydrogen peroxide . In addition, plays a role in the recovery from oxidative stress induced by hydrogen peroxide . In its hyperoxidized form (induced by hydrogen peroxide), confers protection against heat stress . However, has a low tendency for overoxidation during the normal lifespan . Increases sensitivity to cytotoxity caused by metalloids and heavy metals such as arsenic and cadmium by playing a role in inhibiting the expression of phase II detoxification genes such as gcs-1 in intestinal cells . In addition, in response to arsenite, promotes the secretion of the insulin ligand daf-28 into the pseudocoelom, which negatively regulates the activities of daf-16 and skn-1 . Plays a role in promoting longevity . Plays a role in the mitohormetic pathway by promoting the activation of pmk-1 in response to the drug metformin .
PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
Sequence Mass (Da): 22413
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 1.11.1.24
|
A0A2Z5VKM8 | MSIRVGQKAPDFTATAVFDQEFGTIRLSDYLDKRYVVLFFYPLDFTFVCPTEITAFSDRFKEFKELSTEVLGVSVDSEFSHLAWTQIDRKSGGLGELEYPLVSDLKKEISSSYNVLTEDGVALRALFIIDKEGIIQHSTVNNLSFGRNVDEALRTLQAIQYSQENPDEVCPVNWKPGSKTMKPDPVGSKVYFEAI | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O
Sequence Mass (Da): 22013
Sequence Length: 195
Subcellular Location: Plastid
EC: 1.11.1.24
|
Q6C0U8 | MLRLKSLKKPVQAVVRRFATTSAPTLSVGDNIHGFNVLRTKEIPEFDLQATLLEHSTGAQHLHIARDDSNNVFSIGFKTNPPDRTGVPHILEHTTLCGSEKYQVRDPFFKMLNRSLANFMNAMTAQDYTFYPFATTNATDMKNLRDVYLDATLKPLLRELDFSQEGWRLENEDSKDKTSPIILKGVVFNEMKGQMSNAAYAFYIRYLEKIYPSLNNSGGDPLVIPELTYEGLKKFHADHYNPSNAKTFSYGDISVADHLEALNAKFENCEISKTPGNTERLPLEFSSAAENTRIVEEGPIDTLLDTSKQHKMSMSWLMGSPKDIYESFCVKIISSLLIDGHSSPLHQKLIDSGLGSSYSPNTGLDSAPGANIFSVGLQGVTESDLTKVETVILDTIKTTVAEGFDKGRIDGLLHQTELARKDQNAKFGMALMNGVLPGWFNQVDPLEALEWNSVLDRFNKDMEADPEFLQKVMKKYLLDNKYFHFQMNPNPDYEKNVQEKEDEILTDKLAKLTESDKEEIFETGANLEKMQEEPENLDCLPTLHVSDIPRSKPRVALEHTKNPYPIQWRLAPTNGLTYFHSISSLEGLPHEYYPFLPLFTSSLTFLGTKDKTMGQLEDEIKLNTGGLDFSVSCSSSPLSLPSSQLNFAMDGVALDKNVETMFGLFQELLRNTDFTNVEKLKTMIAASTANLSNALAQSGHSFAMLRAASDISPVKKIDDILGGVAQVRFLSELAAKSEQQLVDEVIPKLQEIAKFALTREQRFAVTCGQDMQTKNDELVRKFAESFETNESPFNISSLSIPMTTPTSTLFKLPFQVNYAGIAIPGVPYTHADGAPLQVLANMLTHKHLHREIREKGGAYGGGASYNPTDGFFSYYSYRDPNLERTLQTCQEAGEWSVKKDWSSSDLQEAKLSLFQRIDAPISVKSEGMALYANGLTYEQREKRRRQLLDVAVDDVKRVAKQYLVNPSGYSVAALGPGYETMDKKKWTVLE | Cofactor: Binds 1 zinc ion per subunit.
Function: Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running (By similarity). Preferentially cleaves the N-terminal side of paired basic amino acid residues (By similarity). Also degrades other unstructured peptides (By similarity). May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase (By similarity).
Sequence Mass (Da): 110840
Sequence Length: 990
Subcellular Location: Mitochondrion intermembrane space
EC: 3.4.24.-
|
P32898 | MLRFQRFASSYAQAQAVRKYPVGGIFHGYEVRRILPVPELRLTAVDLVHSQTGAEHLHIDRDDKNNVFSIAFKTNPPDSTGVPHILEHTTLCGSVKYPVRDPFFKMLNKSLANFMNAMTGPDYTFFPFSTTNPQDFANLRGVYLDSTLNPLLKQEDFDQEGWRLEHKNITDPESNIVFKGVVYNEMKGQISNANYYFWSKFQQSIYPSLNNSGGDPMKITDLRYGDLLDFHHKNYHPSNAKTFTYGNLPLVDTLKQLNEQFSGYGKRARKDKLLMPIDLKKDIDVKLLGQIDTMLPPEKQTKASMTWICGAPQDTYDTFLLKVLGNLLMDGHSSVMYQKLIESGIGLEFSVNSGVEPTTAVNLLTVGIQGVSDIEIFKDTVNNIFQNLLETEHPFDRKRIDAIIEQLELSKKDQKADFGLQLLYSILPGWTNKIDPFESLLFEDVLQRFRGDLETKGDTLFQDLIRKYIVHKPCFTFSIQGSEEFSKSLDDEEQTRLREKITALDEQDKKNIFKRGILLQEKQNEKEDLSCLPTLQIKDIPRAGDKYSIEQKNNTMSRITDTNGITYVRGKRLLNDIIPFELFPYLPLFAESLTNLGTTTESFSEIEDQIKLHTGGISTHVEVTSDPNTTEPRLIFGFDGWSLNSKTDHIFEFWSKILLETDFHKNSDKLKVLIRLLASSNTSSVADAGHAFARGYSAAHYRSSGAINETLNGIEQLQFINRLHSLLDNEETFQREVVDKLTELQKYIVDTNNMNFFITSDSDVQAKTVESQISKFMERLPHGSCLPNGPKTSDYPLIGSKCKHTLIKFPFQVHYTSQALLGVPYTHKDGSALQVMSNMLTFKHLHREVREKGGAYGGGASYSALAGIFSFYSYRDPQPLKSLETFKNSGRYILNDAKWGVTDLDEAKLTIFQQVDAPKSPKGEGVTYFMSGVTDDMKQARREQLLDVSLLDVHRVAEKYLLNKEGVSTVIGPGIEGKTVSPNWEVKEL | Cofactor: Binds 1 zinc ion per subunit.
Function: Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running . Preferentially cleaves the N-terminal side of paired basic amino acid residues . Also degrades other unstructured peptides . May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase .
Sequence Mass (Da): 112180
Sequence Length: 989
Subcellular Location: Mitochondrion intermembrane space
EC: 3.4.24.-
|
P76440 | MPQQNYLDELTPAFTSLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQSGCTRAGVDAPIDIGRLQRFVTDFEQQTGMEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVGLSSGSGLPLFEHSDVEIAVDFLQRARQAQGDISIPQSALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFTSARELGVSIIDGFTPVAVEGNKVTFKHVRLSGELTMAADKIILAVGQHARLDAFAELEPQRNTIKTQNYQTRDPQVFAAGDIVEGDKTVVYAVKTGKEAAEAIHHYLEGACSC | Function: Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT).
Catalytic Activity: 5,6-dihydrouracil + NAD(+) = H(+) + NADH + uracil
Sequence Mass (Da): 44329
Sequence Length: 412
EC: 1.3.1.1
|
Q85228 | MPPSMIRVLYATDGCAITYSLMLLTGQEPSGAVYVVSYAWDGAGLDEAFSLPGERAEAELLARRPGVTFCLTGHVASVRVRPVFVAAATPAVVRALCRGEPLAARDVLEAMDEAATFALHDGLIAALTMVLEQVRPRTGNAEYAPERPLRSIAVGRRGLTSLFVHHETQTLAAFRRLYGNHNTPFWYVARFGPEEKTLVLATRLHLFHPRPAYDLRALKDLLLTYNPRVDPNPSGLDPAGLLSFAALSRFCCLSGYARGPAAAHAARYVDERVRADRAEMGVLRDYISHDRGSLKLPDREFVTYVYLAHFESFNRARLREHLDAVNVTDPAAPVGRSPLGERAAAAFFRHVRAQLNIRDYVAQNVTPSVARLAPAMGAGYVEDRTYAALAADAPRGLCDAAAGLARRVTAVEERLAPHGWVRAPDEEQQQPGADGAVLRRLLELAAAPGGGRARTALGALLGLPDACPPAPVYRVELAHRRQAFAVLAGDAWGRATARRDAAPEMAAHEPAAQMYVSRHEVFNARLAVTNIVLDVDFRLARPVPAGTLEAAMRGFRRAVLDALALLFPEADGDWAAHPCYVYKSACPPGGALAAAAGSASAASSDDGLEEAPWDDDAALADFGAAPGDEDWADWDAGVPAEVYTCDDDEVGVGIGGAGGDPGASALVRAPVPADERPPCGCRAKMGFRVCTPVPSPYAVAGADTVRGLARVLQQAVLLERDFIEPMGPYLQDFTFVDTGVYAHGRSLRLPFFAKVDGGGCHGRLLPFGDAPPGFDDPRNFHFHARPAHAVTRVLHSLGGEYESFFERKAARNREAFFARRTPLADMLRGLAVDAEDRRALEAFVADVAMAPVLRHLDAHFNGRAHEYAGATAQRVVAKPDWVLFQLCGSARFSCLRARHARSPPARTFVALSVDAHDRLCISLSQQCFATKCGSNATRTIFTAEVGQSCSSAGARCTSSSSG | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.
Sequence Mass (Da): 103329
Sequence Length: 962
Subcellular Location: Host nucleus
EC: 2.7.7.-
|
Q08501 | MSSALAYMLLVLSISLLNGQSPPGKPEIHKCRSPDKETFTCWWNPGSDGGLPTNYSLTYSKEGEKNTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNEMGSSTSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWLPPTITDVKTGWFTMEYEIRLKSEEADEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWGQEKSIEIPNDFTLKDTTVWIIVAVLSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERLMPSHSKEYPGQGVKPTHLDPDSDSGHGSYDSHSLLSEKCEEPQAYPPAFHIPEITEKPENPEANIPPTPNPQNNTPNCHTDTSKSTTWPLPPGQHTRRSPYHSIADVCKLAGSPGDTLDSFLDKAEENVLKLSEDAGEEEVAVQEGAKSFPSDKQNTSWPPLQEKGPIVYAKPPDYVEIHKVNKDGVLSLLPKQRENHQTENPGVPETSKEYAKVSGVTDNNILVLVPDSRAQNTALLEESAKKVPPSLEQNQSEKDLASFTATSSNCRLQLGRLDYLDPTCFMHSFH | Function: This is a receptor for the anterior pituitary hormone prolactin.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68241
Sequence Length: 608
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Membrane
|
Q91513 | MMTKVGEVLLLLLLPAFVPHTDGTHYSLPGKPTEIKCRSPEKETFTCWWKPGSDGGLPTTYALYYRKEGSDVVHECPDYHTAGKNSCFFNKNNTLIWVSYNITVVATNALGKTYSDPQDIDVVYIVQPHPPEKLEVTVMKDQGWPFLRVSWEPPRKADTRSGWITLIYELRVKLEDEESEWENHAAGQQKMFNIFSLRSGGTYLIQVRCKPDHGFWSEWSSTSYVKVPEYLHREKSVWILVLVFSAFILLLLTWLIHMNSHSLKHCMLPPVPGPKIKGFDKQLLKSGKSDEVFSALVVSDFPPTTSNYEDLLVEYLEVYMPEQQELMVDKGKDHDGCLKSIGSASDSDSGRGSCDSDNLLMDKSGAPKEEQQQQNQEGDQIGKETQGPKEAWEKEAMPCANEDVVSPDASSEKVKTWPSVFSPVTPYSPLDPHNSLEMHKQHCLSNTQFPPGSPSSDHYIKEALQSSYWEVCFNNNQPYPQTEVHPQLQAHSDRNISAVNDRNAPTGLLLPTRMTEYVEVQRVNEENKVLLHPIPSGHSREKACPWVGQRDDYSKVKGVDSDNGLLLQREVVEEESMEMAGAAESCYTSSIAFTTPKQTACSPVALPVQDERVLAVSGYVDTATVFSVHT | Function: This is a receptor for the anterior pituitary hormone prolactin.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70811
Sequence Length: 630
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Membrane
|
P05710 | MPSALAFVLLVLNISLLKGQSPPGKPEIHKCRSPDKETFTCWWNPGTDGGLPTNYSLTYSKEGEKTTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNQMGSSSSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWSPPTITDVKTGWFTMEYEIRLKPEEAEEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWSQESSVEMPNDFTLKDTTVWIIVAILSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERLMPSHSKEYPGQGVKPTHLDPDSDSGHGSYDSHSLLSEKCEEPQAYPPTLHIPEITEKPENPEANIPPTVDPQSTNPNFHVDAPKSSTWPLLPGQHMPRSPYHSVADVCKLAGSPVNTLDSFLDKAEENVLKLSKALETGEEEVAEQKGAKSFPSDKQNTPWPLLQEKSPTVYVKPPDYVEIHKVNKDGVLSLFPKQRENNQTEKPGVPETSKEYAKVSGITDNNILVLVPDSRAQNTALLEESAKKAPPSFEADQSEKDLASFTATSSNRRLQLGRLDYLDPTCFMHSFH | Function: This is a receptor for the anterior pituitary hormone prolactin.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68599
Sequence Length: 610
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Subcellular Location: Membrane
|
A7GT06 | MKWSEISIHTTEEAVEAVSHILHEAGASGVAIEDPAELTKEREQQYGEIYALNPAEYPADGVVIKAYFPQTDSLQETIASLKSSIDVLPSYDIEIGTGNITINEVDEEDWATAWKKYYHPVQISDTFTIVPTWEEYTPSSPDEKIIELDPGMAFGTGTHPTTTMCIRALEKTVKPGDTVIDVGTGSGVLSIAAAKLGAASVQAYDLDPVAVESAEMNVRLNKTDDVVSVGQNSLLEGIEGPVDLIVANLLAEIILMFPEDAARVVKQGGLFITSGIIAAKEKTISEALEKAGFTIKEVLRMEDWVAIIAQNA | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 33681
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P54460 | MKWSELSIHTTHEAVEPISNILHEAGASGVVIEDPLDLIKERENVYGEIYQLDPNDYPDEGVIVKAYLPVNSFLGETVDGIKETINNLLLYNIDLGRNHITISEVNEEEWATAWKKYYHPVKISEKFTIVPTWEEYTPVHTDELIIEMDPGMAFGTGTHPTTVLCIQALERFVQKGDKVIDVGTGSGILSIAAAMLEAESVHAYDLDPVAVESARLNLKLNKVSDIAQVKQNNLLDGIEGEHDVIVANILAEVILRFTSQAYSLLKEGGHFITSGIIGHKKQEVKEALEQAGFTIVEILSMEDWVSIIAKK | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 34531
Sequence Length: 311
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q8AAZ8 | MKYFEFTFHTSPCTETVNDVLAAVLGEAGFESFVESEGGLTAYIQQALCDENTIKNAITEFPLPDTEITYTYVEAEDKDWNEEWEKNFFQPIVIDNRCVIHSTFHKDVPQATYDIVINPQMAFGTGHHETTSLIIGELLDNELKDKSLLDMGCGTSILAILARMRGARPCIAIDIDEWCVRNSIENIELNHVDDIAVSQGDASSLVGKGPFDIIIANINRNILLNDMKQYVACMHPGSELYMSGFYVDDIPFIRREAEKNGLTFVHHKEKNRWAAVKFTY | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31658
Sequence Length: 280
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A1WYK5 | MAQLQVTLEVAAGDLDAVDGALELAGALSQTYQADDGTVLLEPGVGEHPLWEQVRVDALFPPETDPDALHTLLAGQLGERLRGWQAETLEDRAWEREWLDHFRPMAFGERLWIVPTGAEPELPAGAVPIHLDPGLAFGTGTHETTALCLEWLDGEPIAGRNGLDYGAGSGILAVAAVRLGAACCMAVDNDPQAVVASRENAERNGVAEDVPSYAVDQRPAYCADFLVANILASTLVDLADELRDGVRVGGRLALSGILRGQEQQVMDAFQGGIAWDAPRCCGDWVLVSGTRTA | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31158
Sequence Length: 293
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q7VHY7 | MDKQTYWEIIIHPSDFLDQFTDFIIQKTSCAIEFFDILPTPSHFAIIYDDASWQSVLGFDILKAKKSKQPTQIVSRIASNEINIQDFLESLQHFALMLAQNTQDSVGFCYHIEEKFNYDWIKAYQDSIEPVQCGRFYIRPSWEQEVKESYDEIIINPAFAFGSGHHASTAMCLEFLSEMNIQGKTLLDVGCGSGILSIASCKLGAQVYACDTDENAIKECNKNILLNGVMLNALWQGSIADSPMGAPQKYDVIVANIVAFIVKVLHNDFRTKLAKNGVLILSGILDEYKFDIIKAFNDFDMLDTCCKDGWVALKLTL | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 35781
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
B0TAD9 | MKWREIAITTRQENADAMAEIFEAVGAMGMVIEDPQLIASYIESNVWDLHDVEIPDVPEGMIRVKTYLAIDNTLEERLAALQEELSARERSEKWPAHAWTMTDLHEDDWAHAWKAFFKPEKVGRRVVIRPTWEEYVPKEDDLVISIDPGMAFGTGTHPTTVMCIRALEDYVHAEAHVLDVGTGSGVLSIAAALLGAKRVLAVDNDPVAVATAQENVILNQVDEIVEVRRNDLLSGLSEQADILVANIIADVIIRLAPQAAALLAPEGIMIASGIIQNRLDDVVAAMTEKGFSIEELISHGEWAAIVARRAGVSAEG | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 34642
Sequence Length: 316
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
O07678 | MLKPMYYEFFFIFPKERELFESFLLDATHLALEESSLENLKAFDDKETIGFISQSNWHYFATHDPLKKDLKENLKEKPPHLKNFVILRSQKDLNNSLIPALEAFCLNLKQNLQSEFDFFYLSRNLASKDWLEAYKQAILPVQCTKFYIHPSWHQKPSHVVTNDCIMIDPALAFGSGHHESTSMCLELLSDIDLKRKNALDVGCGSGILSIALKKQGVSALVACDTDSLAVEETLKNFSLNQIPLLVQDKVIYGSTQKIEGRFDVIVANLVADVIKSLYSEFVRLCNHTLILSGILETHLNSVLQIYYNGFEVLEQRQRNEWVALKLLKKQPIN | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 38160
Sequence Length: 333
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q31II5 | MAWIQINTTVSEALAEPLSDAFMEVNAASVTFADAKDQPIFEPEIGTTPIWSQTKVIGLFDAEADIPAVINQLATLIPDVPAERYNIEALEDKDWIRAWMDQFQPMQFGSRLWIVPSWCDTPDPKAVNLMLDPGMAFGTGTHPTTALCLTWLDQNPPTDLTVIDYGCGSGVLALAAEKLGAKHVKGTDIDPQAIIASQQNADRNNANIEFKLVKEFQSEPVDLLIANILAGPLKALAPEFIRLMKPNATLILSGLLTNQAADLIAFYQQQGFEFLAQNDLDEWSQLSFTKQVTS | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32277
Sequence Length: 294
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q4L6S8 | MNWTELSIVVNHEVEPLVTDILENYGSNGVVIEDSNDLINQPADKFGEIYELKQEDYPEKGVRLKAYFNELKFDDSLRNKIKTAVTNLENIDSTVLNFSEQTIAEVDWENEWKNYFHPFRASEKFTIVPSWEQYTKEDDSEMCIELDPGMAFGTGDHPTTSMCLKAIETYVDSDNSVIDVGTGSGILSIASHLLGVKRIKALDIDELAVNVAKENFAKNHCEDAIEAVPGNLLKNETEKFDIVIANILAHIIEDMIEDAYNTLNKDGYFITSGIIEEKHKQILNKMQNVGFDIKSVNHDNGWVCIVGQKVSE | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 35216
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.