ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5I085 | MADGELNVDSLISRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRT... | 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 ... |
Q8MJ46 | MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECVSINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGETDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPLRGMITKQ... | 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 glycog... |
P36873 | MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQ... | 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 glycog... |
P63087 | MADIDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAEKKKPNATRPVTPPRGMITKQ... | 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 glycog... |
Q8SRZ0 | MDIREMDLKRQEANALFKKQMIDEALEIYKTSFLEATKSVVPGTRNDLLEEQLSLLAYNISVVYYKRKNFPKSLAFGLESLKHRKSDKVLCKICAIYLRLGMLREYKEMYDQMVTRSSGPEVAFLLKRMKLSEVIVEKHLEKRVTLESLHELSKEISGGRSIPADTLESILEQGESILLGCENVVHTESSGEVLIFGDTHGQYFDVVSILNKVFDKDRMVIFNGDYVDRGSHSVENFALLLSLKILFPGRVHLTRGNHELSDINRVYGFYDEVKRKYPFSSDSVYRRFQDAFRALPISIIVNEKVFITHGGLPEAPVKVD... | 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
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Q7YSW8 | MSTNNNKAPTSQSSDKSATTESKLNDNENTETETKTDENNEEKPKMTLKPPQPKIENKVSTIDRVVPSVKYPKSLPLPHDVLFNEDKTINLPKLQEHFFAEGRLNHDDVIEIVKMAAEILEKEPTLIQVEAPITVCGDTHGQFYDLIKIFENDIGGNPANTNYLFLGDYVDRGYFSMEVIIYLYACKINYPNTFFLLRGNHECRHLTEYFTFKEECLHKYSEEVYDFITESFNALPLAALMNGKFLCIHGGLSPDIKTLDDIANIDRFKEPPSSGPMCDLLWSDPMEEFSPEIREHFVPNDVRGCSYLYSYRAVCSFLQK... | 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-[pr... |
Q08209 | MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAA... | 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, dephos... |
P16298 | MAAPEPARAAPPPPPPPPPPPGADRVVKAVPFPPTHRLTSEEVFDLDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNY... | 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 stimula... |
P48453 | MAAPEPARAAPPPPPPPPPPLGADRVVKAVPFPPTHRLTSEEVFDMDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNY... | 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 translocat... |
P48454 | MSGRRFHLSTTDRVIKAVPFPPTQRLTFKEVFENGKPKVDVLKNHLVKEGRLEEEVALKIINDGAAILRQEKTMIEVDAPITVCGDIHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTDYFTFKQECRIKYSEQVYDACMETFDCLPLAALLNQQFLCVHGGMSPEITSLDDIRKLDRFTEPPAFGPVCDLLWSDPSEDYGNEKTLEHYTHNTVRGCSYFYSYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQATGFPSLITIFSAPNYLDVYNNKAAVLKY... | 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 E... |
P48455 | MSVRRPQFSTTERVIKAVPFPPTRRLTLKEVFENGKPKMDLLKNHLVKEGRVEEEVALKIINDGAAILKQEKTMIEVEAPITVCGDVHGQFFDLMKLFEVGGSPSNTRYLFLGDYVDRGYFSIECVLYLWSLKINHPKTLFLLRGNHECRHLTEYFTFKQECRIKYSEMVYDACMHTFDCLPLAALLNQQFLCVHGGMSPEITCLEDIRKLDRFSEPPAFGPVCDLLWSDPLEDYGSEKTLEHYTHNTVRGCSYFFSYPAVCEFLQNNSLLSIIRAHEAQDAGYRMYRKNQATGFPSLITIFSAPNYLDVYNNKAAVLKY... | 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 E... |
Q0G819 | MASTSAGQNSAAKPDTTNTTTTASNNNRERERDLKQFTERFVKTVQFPVSERLTVDQVYDRRTGKPRHEVLRDHFIKEGRIEEEAAIRVIQECSSLFRNEKTMLEIEAPVTVCGDIHGQFYDLMKLFEVGGSPATTKYLFLGDYVDRGYFSIECVLYLWALKICYPTTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDVCMESFDALPLAALMNQQFLCVHGGLSPEIHTLEDIRRIDRFKEPPAFGPMCDLLWSDPLEDFGNERNSEQFSHNSVRGCSYFYSYAACCDFLQHNNLLSIIRAHEAQDAGYRMYRKSQ... | 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 b... |
Q12705 | MTSGPHNLEDPIVRAIRQKNQAPSHDFTIFVQEDGSSVSTLDRVVKNVQAPATYIPTDVEFFDINEPDKPDLHFLRNHFIREGRLSEEQTLYIIKKATEILKSEDNLIEVDAPVTVCGDIHGQYYDLMKLFEVGGNPANTQYLFLGDYVDRGYFSIECLLYLWALKIWYPKTLWLLRGNHECAHLTDYFTFKLECTHKYNIKVYEACLQSFNALPLAAIMNKQFLCVHGGLSPELHTLNDIRMINRFCEPPTHGLMCDLLWSDPLEDFGSEKSNKHFIHNNVRGCSYFYSYQAVCTFLENNNLLSVIRAHEAQDVGYRMY... | 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 Activ... |
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
Subcel... |
P40371 | MKGSHPNAGSLLEPLHKLNPFSENSTSGHRKNASDHSADGETRPIAIEMKDSKGNTVPVGNSRPSKASNWLAGLMEDKNQRWRRSMEDTHICLYDFGGNQDDGFVAVYDGHAGIQASDYCQKNLHKVLLEKVRNEPDRLVTDLMDETFVEVNSKIAKATHNDICGCTAAVAFFRYEKNRTRRVLYTANAGDARIVLCRDGKAIRLSYDHKGSDANESRRVTQLGGLMVQNRINGVLAVTRALGDTYLKELVSAHPFTTETRIWNGHDEFFIIACDGLWDVVSDQEAVDFVRNFVSPREAAVRLVEFALKRLSTDNITCIV... | 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... |
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 Celsiu... |
P49596 | MGQTLSEPVTKKESASCANENYLVGSSCMQGWRVDMEDAHTHLLSLPDDPKCAFFAVYDGHGGSKVSQYSGINLHKKVVAQKEFSEGNMKEAIEKGFLELDQQMRVDEETKDDVSGTTAVVVLIKEGDVYCGNAGDSRAVSSVVGEARPLSFDHKPSHETEARRIIAAGGWVEFNRVNGNLALSRALGDFAFKNCDTKPAEEQIVTAFPDVITDKLTPDHEFIVLACDGIWDVMTNQEVVDFVREKLAEKRDPQSICEELLTRCLAPDCQMGGLGCDNMTVVLVGLLHGQSPDTLFTKCARPAVFTGVNNEDGDQNQIQQ... | 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
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Q09172 | MGQTLSEPVLDKHSSSGGDRWLHFGVSHMQGWRISMEDAHCALLNFTDSNSSNPPTSFFGVFDGHGGDRVAKYCRQHLPDIIKSQPSFWKGNYDEALKSGFLAADNALMQDRDMQEDPSGCTATTALIVDHQVIYCANAGDSRTVLGRKGTAEPLSFDHKPNNDVEKARITAAGGFIDFGRVNGSLALSRAIGDFEYKKDSSLPPEKQIVTAFPDVVIHNIDPDDEFLILACDGIWDCKSSQQVVEFVRRGIVARQSLEVICENLMDRCIASNSESCGIGCDNMTICIVAFLHGRGLEDWYNWITQRVNSGEGPCAPPSY... | 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 Ma... |
Q9SFU3 | MTFLLLLLFCFLSPAISSAHSIPSTLDGPFVPVTVPLDTSLRGQAIDLPDTDPRVRRRVIGFEPEQISLSLSSDHDSIWVSWITGEFQIGKKVKPLDPTSINSVVQFGTLRHSLSHEAKGHSLVYSQLYPFDGLLNYTSGIIHHVRITGLKPSTIYYYRCGDPSRRAMSKIHHFRTMPVSSPSSYPGRIAVVGDLGLTYNTTDTISHLIHNSPDLILLIGDVSYANLYLTNGTSSDCYSCSFPETPIHETYQPRWDYWGRFMENLTSKVPLMVIEGNHEIELQAENKTFEAYSSRFAFPFNESGSSSTLYYSFNAGGIHF... | 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, an... |
Q9SCX8 | MNSGRRSLMSATASLSLLLCIFTTFVVVSNGELQRFIEPAKSDGSVSFIVIGDWGRRGSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFYDNGLFSEHDPNFEQSFSNIYTAPSLQKQWYSVLGNHDYRGDAEAQLSSVLREIDSRWICLRSFVVDAELVEMFFVDTTPFVKEYYTEADGHSYDWRAVPSRNSYVKALLRDLEVSLKSSKARWKIVVGHHAMRSIGHHGDTKELNEELLPILKENGVDLYMNGHDHCLQHMSDEDSPIQFLTSGAGSKAWRGDINPVTINPKLLKFYYDGQGFMSARFTHSDAEIVFYDVF... | 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
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Q9LJU7 | MEKWGILLLVTLSVSIIFTSAAADDYVRPKPRETLQFPWKQKSSSVPEQVHISLAGDKHMRVTWVTNDKSSPSFVEYGTSPGKYSYLGQGESTSYSYIMYRSGKIHHTVIGPLEADTVYYYRCGGEGPEFHLKTPPAQFPITFAVAGDLGQTGWTKSTLDHIDQCKYAVHLLPGDLSYADYMQHKWDTFGELVQPLASVRPWMVTQGNHEKESIPFIVDEFVSFNSRWKMPYEESGSNSNLYYSFEVAGVHAIMLGSYTDYDRYSDQYSWLKADLSKVDRERTPWLIVLFHVPWYNSNNAHQHEGDEMMAEMEPLLYASG... | 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
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Q9LX83 | MGLNHLTLVCSAIALLSIFVVSQAGVTSTHVRVSEPSEEMPLETFPPPACYNAPEQVHITQGDHAGRGMIISWVTPLNEDGSNVVTYWIANSDGSDNKSALATTSSYRYFNYTSGYLYHATIKGLETLYNYMSNPKGQAVLFAGDLSYADDHPNHDQRKWDSYGRFVEPSAAYQPWIWAAGNHEIDYAESIPHKVHLHFGTKSNELQLTSSYSPLTQLMDELKKVNRSETPWLIVLVHAPWYNSNNYHYMEGESMRVTFEPWFVENKVDIVFAGHVHAYERSERISNIQYNITDGMSTPVKDQNAPVYITIGDGGNIEGI... | 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
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Q9LXI7 | MVKVLGLVAILLIVLAGNVLSYDRQGTRKNLVIHPTNEDDPTFPDQVHISLVGPDKMRISWITQSSISPSVVYGTVSGKYEGSANGTSSSYHYLLIYRSGQINDVVIGPLKPNTVYYYKCGGPSSTQEFSFRTPPSKFPIKFAVSGDLGTSEWSKSTLEHVSKWDYDVFILPGDLSYANMYQPLWDTFGRLVQPLASQRPWMVTHGNHELEKIPILHSNPFTAYNKRWRMPFEESGSSSNLYYSFNVYGVHIIMLGSYTDFEPGSEQYQWLENNLKKIDRKTTPWVVAVVHAPWYNSNEAHQGEKESVEMKESMETLLYK... | 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
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Q8S340 | MKLFGLFLSFTLLFLCPFISQADVPELSRQPPRPIVFVHNDRSKSDPQQVHISLAGKDHMRVTFITEDNKVESVVEYGKQPGKYDGKATGECTSYKYFFYKSGKIHHVKIGPLQANTTYYYRCGGNGPEFSFKTPPSTFPVEFAIVGDLGQTEWTAATLSHINSQDYDVFLLPGDLSYADTHQPLWDSFGRLVEPLASKRPWMVTEGNHEIEFFPIIEHTTFKSYNARWLMPHTESFSTSNLYYSFDVAGVHTVMLGSYTDFDCESDQYQWLQADLAKVDRKTTPWVVVLLHAPWYNTNEAHEGEGESMREAMESLLFNA... | 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
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Q6TPH1 | MTLLIMITLTSISLLLAAAETIPTTLDGPFKPLTRRFEPSLRRGSDDLPMDHPRLRKRNVSSDFPEQIALALSTPTSMWVSWVTGDAIVGKDVKPLDPSSIASEVWYGKEKGNYMLKKKGNATVYSQLYPSDGLLNYTSGIIHHVLIDGLEPETRYYYRCGDSSVPAMSEEISFETLPLPSKDAYPHRIAFVGDLGLTSNTTTTIDHLMENDPSLVIIVGDLTYANQYRTIGGKGVPCFSCSFPDAPIRETYQPRWDAWGRFMEPLTSKVPTMVIEGNHEIEPQASGITFKSYSERFAVPASESGSNSNLYYSFDAGGVH... | 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... |
Q949Y3 | MNHLVIISVFLSSVLLLYRGESGITSSFIRSEWPAVDIPLDHHVFKVPKGYNAPQQVHITQGDYDGKAVIISWVTPDEPGSSQVHYGAVQGKYEFVAQGTYHNYTFYKYKSGFIHHCLVSDLEHDTKYYYKIESGESSREFWFVTPPHVHPDASYKFGIIGDMGQTFNSLSTLEHYMESGAQAVLFLGDLSYADRYQYNDVGVRWDSWGRFVERSTAYQPWLWSAGNHEVDYMPYMGEVTPFRNYLQRYTTPYLASKSSSPLWYAVRRASAHIIVLSSYSPFVKYTPQWHWLSEELTRVDREKTPWLIVLMHVPIYNSNE... | 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-n... |
P08371 | MPVKEQGFSLLEVLIAMAISSVLLLGAARFLPALQRESLTSTRKLALEDEIWLRVFTVAKHLQRAGYCHGICTGEGLEIVGQGDCVIVQWDANSNGIWDREPVKESDQIGFRLKEHVLETLRGATSCEGKGWDKVTNPDAIIIDTFQVVRQDVSGFSPVLTVNMRAASKSEPQTVVNASYSVTGFNL | Function: Not yet known.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20520
Sequence Length: 187
Subcellular Location: Membrane
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P08372 | MSASLKNQQGFSLPEVMLAMVLMVMIVTALSGFQRTLMNSLASRNQYQQLWRHGWQQTQLRAISPPANWQVNRMQTSQAGCVSISVTLVSPGGREGEMTRLHCPNRQ | Function: Not yet known.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12004
Sequence Length: 107
Subcellular Location: Membrane
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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
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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'-cGM... |
P11155 | MAASVSRAICVQKPGSKCTRDREATSFARRSVAAPRPPHAKAAGVIRSDSGAGRGQHCSPLRAVVDAAPIQTTKKRVFHFGKGKSEGNKTMKELLGGKGANLAEMASIGLSVPPGFTVSTEACQQYQDAGCALPAGLWAEIVDGLQWVEEYMGATLGDPQRPLLLSVRSGAAVSMPGMMDTVLNLGLNDEVAAGLAAKSGERFAYDSFRRFLDMFGNVVMDIPRSLFEEKLEHMKESKGLKNDTDLTASDLKELVGQYKEVYLSAKGEPFPSDPKKQLELAVLAVFNSWESPRAKKYRSINQITGLRGTAVNVQCMVFGN... | 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 ra... |
Q6AVA8 | MPSVSRAVCVQRASGNNGRRCRDGAAAAGRRSVVAQRARHGKPEVAIRSGSGGSARGGHCSPLRAVAAPIPTTKKRVFHFGKGKSEGNKAMKDLLGGKGANLAEMASIGLSVPPGFTVSTEACQQYQAAGKTLPAGLWEEIVEGLQWVEEYMAARLGDPARPLLLSVRSGAAVSMPGMMDTVLNLGLNDEVAAGLAAKSGDRFAYDSYRRFLDMFGNVVMDIPHALFEEKLEAMKAVKGLHNDTDLTATDLKELVAQYKDVYVEAKGEPFPSDPKKQLQLAVLAVFNSWDSPRAIKYRSINKITGLKGTAVNVQTMVFGN... | 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 r... |
Q75KR1 | MAPAAHRDGAAEAVGQRVFHFGKGRSDGNKTMKDLLGGKGANLAEMASIGLSVPPGFTVSTEACQQYQAQKAMPAGLWDEILAALTWVEGNMGAVLGDPRRPLLLSVRSGAAVSMPGMMDTVLNLGLNDHVVAGLAHRSGERFAYDSYRRFLDMFGNVVMDIPHSLFEEKIEAMKAALGLRNDTELTARDLKELVAQYKNVYVEAKGEEFPSDPKKQLHLSVLAVFNSWDSARAKKYRSINQITGLKGTAVNVQCMVFGNMGDTSGTGVLFTRNPSTGERKLYGEFLVNAQGEDVVAGIRTPQDLDTMKDCMPEPYAELV... | 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 | MAKWVYKFEEGNASMRNLLGGKGCNLAEMTILGMPIPQGFTVTTEACTEYYNSGKQITQEIQDQIFEAITWLEELNGKKFGDTEDPLLVSVRSGARASMPGMMDTILNLGLNDVAVEGFAKKTGNPRFAYDSYRRFIQMYSDVVMEVPKSHFEKIIDAMKEEKGVHFDTDLTADDLKELAEKFKAVYKEAMNGEEFPQEPKDQLMGAVKAVFRSWDNPRAIVYRRMNDIPGDWGTAVNVQTMVFGNKGETSGTGVAFTRNPSTGEKGIYGEYLINAQGEDVVAGVRTPQPITQLENDMPDCYKQFMDLAMKLEKHFRDMQ... | 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... |
P37213 | MQRVYAFEDGDGTNKKLLGGKGAGLCTMTKIGLPVPQGFVITTEMCKQFIANGNKMPEGLMEEVKKNMQLVEKKSGKVFGGEENPLLVSVRSGAAMSMPGMMDTILNLGLNDKTVVALAKLTNNERFAYDSYRRFVSLFGKIALNVDDEVYDKTLENKKVEKGVKLDTELDANDMKELAQVFIKKTEEFTKQPFPVDPYAQLEFAICAVFRSWMGKRAVDYRREFKITPEQADGTAVSVVSMVYGNMGNDSATGVCFTRDPGTGENMFFGEYLKNAQGEDVVAGIRTPQIISKMAEDADLPGCYEQLLDIRKKLEGYFHE... | 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 domai... |
P51776 | MSTRRVYFFGETPENQPANSELCRKVLGGKGISLAAMIKLGMPVPLGFTITCQTCVEYQKTASWPKGLKEEVASNLKLLEEKMGKTFGDNTNPLLVSVRSGAAVSMPGMMDTILNLGLNDESVKGLAAVTGNARFAYDSYRRFMQMFGDVCLGIDHDKFEHALDAVKTRYGRKTDPELTADELEEVCEAYRKICVAATGKTFPQCPHEQLELAINAVFKSWTNPRAQAYRTLNKLDHNMGTAVNVQSMVFGNTGDDSGTGVGFTRCPKTGEKFSYLYGEFLQNAQGEDVVAGIRTPVNLKEMPTINASWKACYDELSLIY... | 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(+) + phosphoenolpyruva... |
Q59754 | MAKWVYTFGAGQAEGSAEDRDRLGGKGANLAEMCNLGLPVPPGLTIVTAACNSYLEKGRSMPEGLREQVREGITRMEKITGRVFGDTNRPLLLSVRSGARASMPGMMDTVLNLGLNDQSVHALGHDAGDARFAWDSYRRFIQMYGDVVMGVDHEVFEEVLEDEKARLGHEQDTELSAVEWQHVISRYKEAIEEVLGLPFPQDPEVQLWGAIGAVFSSWMNPRAITYRHLHGIPAGWGTAVNVQAMVFGNLGNSSATGVAFTRNPSTGEKELYGEFLVNAQGEDVVAGIRTPQNITEAARIASGSDKPSLEKLMPEAFAEF... | 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(+) + phosphoenolpyruva... |
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 isom... |
Q4G338 | MAASNFPHNKKRTLYVGGFGEEVTEKVLMAAFITFGDIVAISIPMDYETGKHRGFGFVEFELAEDAAAAIDNMNESELFGRTIRCNFARPPKATERSSRPVWADDEWLKRYGKGSGIADAKESNGSASTAKGLPRVYLGVKIGIRYIGRIVIELRSDVVPRTAENFRCLCTGEKGFGYEGSSFHRIIPKFMLQGGDFTKGDGTGGKSIYGPKFEDENFKLKHLMPGTVSMANCGPNTNGSQFFICAEKTDWLDGKHVVFGHVVEGMNVVRQVEQQGTPSGKPQMVVKIVECGELDPVPQTEPQENEENSDPQTPMDVEPQ... | 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 ... |
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 i... |
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 isom... |
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):... |
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
... |
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
... |
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 inhibiti... |
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 inhibi... |
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 ... |
Q13427 | MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPKSKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRKHKKEKKKRKKSKKSASSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERKNRERERERECNPPNSQPASY... | 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]-... |
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 Loca... |
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 Loca... |
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 = ... |
Q9V521 | MADKKNLLLLFDHPTEPVFMDKGKRVTVFDVPDSFLTDRYRPISNEVQSRVGDKVEQRVPVREISIPDLRIPMSLGRDEQFSLFLPKHRRIAGRLIDIFMNMRSVDDLQSVAVYARDRVNPVLFNYALSVALLHRPDTQGLDLPSFSQTFPDRFIDSQVIRKMREESFVVQPGSRMPITIPRDYTASDLDPEHRLWYFREDLGINLHHWHWHLVYPFEASDRSIVAKDRRGELFYYMHQQVIARYNAERFSNNLARVLPFNNLRDPIAEGYFPKMDSLVASRAWPPRFESTRLSDLNRESDQLNVEIGDLERWRDRIYEA... | 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... |
Q8I6K2 | MSNTAVLNDLVALYDRPTEPMFRVKAKKSFKVPKEYVTDRFKNVAVEISNRFGEDDSETVTIDSVPLPDLADILTLGREENFSLFIPKHRNLSAKLINIFLQAENPKHLLSIACYAHDRVNPYLFIYALSVALIHRKDTKSLKIPNQIQTFPDKYFDSQVFSQGKEEMTVVPQGLRRPIEIPRDYTASDLEEEHRVAYWREDLGINLHHWHWHLVYPTDGGEIVTKKDRRGELFYYSHQQIVARYNFERFCNALKRVERLTDWQGPIKEAYFPKLDSLVAKRAYPARVQDMTMQDLDIPGQNIKVDVDDMIRWRDRIYRA... | 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 an... |
Q9MB14 | MASFTTSPCTSAAPKTPKSLSSSATISSPLPKPSQIHIATAKRTHHFKVSCNAPNGDSQPKLDRRDVLLGLGGLAGAASLINNPLAFAEPIHAPEISKCVVPPKDLPPDAIVDNCCPPLATNVIPYKVPKTSPSAMKIRPAIHRMDKEYIAKFEKAIRLMKELPADDPRNFYQQALVHCAYCNGGYVQTDYPDKEIQVHNSWLFFPFHRWYLYFYERILGKLIGDPTFGLPFWNWDTPAGMLIPQYFRNQNSPLYDENRNQSHLPLVMDLGYAGTDTDVTDQERISNNLALMYKSMVTNAGTAELFLGKPYKAGDDPVNK... | 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 | MSDKKSLMPLVGIPGEIKNRLNILDFVKNDKFFTLYVRALQVLQARDQSDYSSFFQLGGIHGLPYTEWAKAQPQLHLYKANYCTHGTVLFPTWHRAYESTWEQTLWEAAGTVAQRFTTSDQAEWIQAAKDLRQPFWDWGYWPNDPDFIGLPDQVIRDKQVEITDYNGTKIEVENPILHYKFHPIEPTFEGDFAQWQTTMRYPDVQKQENIEGMIAGIKAAAPGFREWTFNMLTKNYTWELFSNHGAVVGAHANSLEMVHNTVHFLIGRDPTLDPLVPGHMGSVPHAAFDPIFWMHHCNVDRLLALWQTMNYDVYVSEGMN... | 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 ... |
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... |
Q8MZM3 | MATLTQKFHGLLQHPLEPLFLPKNDGTLFYDLPERFLTSRYSPIGQNLANRFGPNSPASSQVSNDTGVPPTVVTIKDLDELPDLTFATWIKRRDSFSLFNPEHRKAAGKLTKLFLDQPNADRLVDVAAYARDRLNAPLFQYALSVALLHRPDTKSVSVPSLLHLFPDQFIDPAAQVRMMEEGSIVLDENRMPIPIPMNYTATDAEPEQRMAFFREDIGVNLHHWHWHLVYPASGPPDVVRKDRRGELFYYMHQQLLARYQIDRYAQGLGRIEPLANLREPVREAYYPKLLRTSNNRTFCPRYPGMTISDVARSADRLEVR... | 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, ... |
Q08303 | MASLCSNSSSTSLKTPFTSSTTCLSSTPTASQLFLHGKRNKTFKVSCKVTNTNGNQDETNSVDRRNVLLGLGGLYGVANAIPLAASAAPTPPPDLSSCNKPKINATTEVPYFCCAPKPDDMSKVPYYKFPSVTKLRIRPPAHALDEAYIAKYNLAISRMKDLDKTQPDNPIGFKQQANIHCAYCNGGYSIDGKVLQVHNSWLFFPFHRWYLYFYERILGSLIDDPTFGLPFWNWDHPKGMRFPPMFDVPGTALYDERRGDQIHNGNGIDLGYFGDQVETTQLQLMTNNLTLMYRQLVTNSPCPLMSLVDLTLFGSTVEDA... | 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 | MASGAVADHQIEAVSGKRVAVVGAGVSGLAAAYKLKSRGLNVTVFEADGRVGGKLRSVMQNGLIWDEGANTMTEAEPEVGSLLDDLGLREKQQFPISQKKRYIVRNGVPVMLPTNPIELVTSSVLSTQSKFQILLEPFLWKKKSSKVSDASAEESVSEFFQRHFGQEVVDYLIDPFVGGTSAADPDSLSMKHSFPDLWNVEKSFGSIIVGAIRTKFAAKGGKSRDTKSSPGTKKGSRGSFSFKGGMQILPDTLCKSLSHDEINLDSKVLSLSYNSGSRQENWSLSCVSHNETQRQNPHYDAVIMTAPLCNVKEMKVMKGG... | 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; protoporphyr... |
P55826 | MELSLLRPTTQSLLPSFSKPNLRLNVYKPLRLRCSVAGGPTVGSSKIEGGGGTTITTDCVIVGGGISGLCIAQALATKHPDAAPNLIVTEAKDRVGGNIITREENGFLWEEGPNSFQPSDPMLTMVVDSGLKDDLVLGDPTAPRFVLWNGKLRPVPSKLTDLPFFDLMSIGGKIRAGFGALGIRPSPPGREESVEEFVRRNLGDEVFERLIEPFCSGVYAGDPSKLSMKAAFGKVWKLEQNGGSIIGGTFKAIQERKNAPKAERDPRLPKPQGQTVGSFRKGLRMLPEAISARLGSKVKLSWKLSGITKLESGGYNLTYE... | 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; protoporphyr... |
P0AFL8 | MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTAS... | 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 Locat... |
P44828 | MNDSILEPKHRGNVREIAAIDLGSNSFHMIVARIVNGSIQVLSRLKQKVKLAEGLDENAVLNQEAITRGVNCLALFAERLQGFPMENVNVVGTYTLRRAVNNDEFLRQAAKVFPYPINIISGQTEAKTIYAGVCHTQPEKGRKLVIDIGGGSTEMIIGDDFTPLMAESRHMGCVSFATQFFTDGIISPENFQRARQSAVNKIEDLGLEYRKLGWQSVLGSSGTIKTVAQVIATNLDPNGTITAERLNALIEQTLQAKHFTELNINGLNQDRVDVFVPGLAILSAVFDVFHIQQMRYSDGALREGVIYSLEKNFQVADIRA... | 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 Locat... |
Q9ZN70 | MDLQSMPQKPAEAFPLIAALDLGSNSFHLCLAKANIHGEVRILERLGEKVQLAAGLDEERNLSEEATQRGLDCLRRFAQFISGMPQGSVRVVATNALREARNRSDFIRRAEEVLGHPVEVISGREEARLIYLGVANSMPDSGGRRLVSDIGGGSTEFIIGQGFESELRESLQMGCVSYTQRYFRDGKITPARYAQAYTAARLELMGIENSLRRLGWQQAVGASGTIRAVALAIKAGGHGNGEISPDGLAWLKRKVLKLGDVEKLDLEGIKPDRRTIFPAGLAILEAIFDALELEQMVHSEGALREGVLYDLVGRHQHEDV... | 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
... |
Q9KU08 | MTTVVSNAREIAAIDLGSNSFHMVVAKVVDQDLQLISRHKQRVRLAAGLDEQKNLDEESIQRGLECLAMFAERLQGFEPRNVRIAATHTLRQARNANLFIQRALDVLPFPIEIIPGSEEARLIYLGVAHTQPQADSMLVVDIGGGSTEMIIGKGFEAELLNSKQMGCVNFTERYFANGKLSRKNFAQAIVASEQKLESIASKYRKKGWQMAFGSSGTIKAIHEVLIGQGHEDGLITFERLSKLIEKLCEWDSIDDLQLPGLTDDRKPVFAAGVAILSAIFHGLNIKEMHFSDGALREGLLYEMEDRFKYSDIRLRTTENL... | 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 Locat... |
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
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P26570 | MGNSSSKSSKKDSHSNSSSRNPRPQVSRTETSHSVKSAKSNKSSRSRRSLPSSSTTNTNSNVPDPSTPSKPNLEVNHQRHSSHTNRYHFPSSSHSHSNSQNELLTTPSSSSTKRPSTSRRSSYNTKAAADLPPSMIQMEPKSPILKTNNSSTHVSKHKSSYSSTYYENALTDDDNDDKDNDISHTKRFSRSSNSRPSSIRSGSVSRRKSDVTHEEPNNGSYSSNNQENYLVQALTRSNSHASSLHSRKSSFGSDGNTAYSTPLNSPGLSKLTDHSGEYFTSNSTSSLNHHSSRDIYPSKHISNDDDIENSSQLSNIHASM... | 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
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B0XUR7 | MGQSHSKGNSGPGDSLQSYPSFSRSDTKESLRSLRGSIRSKIRSSDSPRGSTAGLSDDKSDAASVKSTTSRRSSTNQSVQSPDDTPSQPDAPEPPPSPSLSSSLKRGHKDVNAMQQSGEVDHVSDVPPTGAAPTGPSTQKVGESILIKRENQLNPILDFIMNAPLETSGSPGMGMGALKSIDLDDMISRLLDAGYSTKVTKTVCLKNAEIMAICSAARELFLSQPALLELSAPVKIVGDVHGQYTDLIRLFEMCGFPPASNYLFLGDYVDRGKQSLETILLLLCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCN... | 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 pathoge... |
A0A166Z003 | MPDNHGPWGLRWRAKPSFILTTVAMGLFTDLVLYGILLPALPFTMRNRFDIPNAEIQHYTSAFLATYAGASVFFSVPAGWAASKLGSRQLFLGGLMFLVVATAIFAFSTSLVLLVVSRLLQGMSTAVVWTAGLDMVQDTVEPSQVGETIGTIFATISVGELAAPVLGGVLYERGGISAVFAVSAVLLAIDLALRALVIDKKTAVKYESPRLIRFPVERNMSDDHVASAPTVMEAQESVHEGTRLLPQVDDDGDHYKIDRELGSIVRAIPLLYCFREPRLHLAMLLSFVQALFIGTFDATVPTVAESLFHFSSLQVGLVFI... | 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): 5173... |
A0A166YZY9 | MATDTAVTGAPETTELRLASGNGPVTRTVLRTPVRDALPSEVPLIDISPIFSTCVADRKAVARKIHDAATNIGFFYIQNHRVPSQDIDLAYSASQDFFRQEMEVKVEADAKDGPFDSGYRGPGTQRVNPTEGADLRETYSILYDPMLDPTVPDPANIPEPASRFLHLGRAPFESTATLPHFKDAFVRYFQACLVLARALTRAFALSLDLPESAFDGKVQYPDASLEINFYPPISTGHAVSAPGDADTRVSIGSHTDFLLFTILWQDSNGGLQVLNREGQWIRAIPVEGTFVVNIGDYLQRVTNDKYVSTVHRAQNFSGRE... | 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 con... |
A0A166YZY4 | MARTPERRVRTLDFAQFCHGEPSSSHGFCRELVDCLRSLGFVKIRNHGISGEEIEKVFVMNKLFFSLPQAAKAKAAHPPEANPHRGYSYVGQEKLSRVKDYEKGKRSIVDVYDIKESYDQGPAVDKLYPNRWPDKQDIPGFRVVMEKFYERCHQVHQDVLRAIATGFDLSPSFLTDLCCENTSELRLNHYPGVHPSSLRKGAKRISEHTDFGTVTLLFQDSVGGLEIEDQNSPGTYFPVSSERKSDMIVNVGDCIQRWTNDKILSTSHRVVLPEDRDALIKDRYSVAYFGKPSRSQLVSPLREFVKEGEKPKYSAISAWQ... | 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 con... |
A0A166YZU9 | MLSIIHVGWLELVWFVALYPFACWTLFAVLKSVYRITLHPLAKFPGPKLAGASYCYEFWYEIVCGIQYTQKIIKLHEQYGPIVRINPDELHFNDIDFVDVVYTAGARKRDKSRHYLAGFEGSIIRFVSSDFHSFLIDTRVKKPERLKRVVLGAERHHDAKDCPMFLELLNSNLPAQEKSKQRLMYEANGATLAGSGSTAIALSNIVYNLVANPRIGHKLRSELMRKVSASKNLPTWSTLEELPYLTAVIHEGLRSMYDPSKERLPYDPSQERLPRVATEEELIYEGGSALGKSKYVIPRGYAISTSAHVVHSDESIFPNA... | 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 forma... |
Q89FG1 | MLEKQRSTAETFGIPLAVLLEITHRCPLQCPYCSNPVELDRSGKELTTDEWKKVLSELAEIGVLQVHFSGGEPTARKDLVELVKHASDVGLYTNLITSAVLLTRERLSELADAGLCHVQISFQGVEEGLADRVAGYRNAHRKKLEVAKWTRELDLPLTVNAVMHRQNLHQLPDIIQMSIDLDADRLEVANVQYYGWALKNRAALMPTVAQLDECTRLVEEARERLKGRLSIDYVVPDYYALRPKKCMGGWGRQFFNISPAGKVLPCHAAESITGLDFESVRSNHSIAWIWQNSEAFNRYRGTGWMKEPCKSCEFREIDFG... | 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 pre... |
Q9L3B0 | MTLPSPPMSLLAELTHRCPLSCPYCSNPLELERKAAELDTATWTAVLEQAAELGVLQVHFSGGEPMARPDLVELVSVARRLNLYSNLITSGVLLDEPKLEALDRAGLDHIQLSFQDVTEAGAERIGGLKGAQARKVAAARLIRASGIPMTLNFVVHRENVARIPEMFALARELGAGRVEIAHTQYYGWGLKNREALLPSRDQLEESTRAVEAERAKGGLSVDYVTPDYHADRPKPCMGGWGQRFVNVTPSGRVLPCHAAEIIPDVAFPNVQDVTLSEIWNISPLFNMFRGTDWMPEPCRSCERKERDWGGCRCQAMALTG... | 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 pre... |
P27507 | MSQSKPTVNPPLWLLAELTYRCPLQCPYCSNPLDFARQDKELTTEQWIEVFRQARAMGSVQLGFSGGEPLTRKDLPELIRAARDLGFYTNLITSGIGLTESKLDAFSEAGLDHIQISFQASDEVLNAALAGNKKAFQQKLAMAKAVKARDYPMVLNFVLHRHNIDQLDKIIELCIELEADDVELATCQFYGWAFLNREGLLPTREQIARAEQVVADYRQKMAASGNLTNLLFVTPDYYEERPKGCMGGWGSIFLSVTPEGTALPCHSARQLPVAFPSVLEQSLESIWYDSFGFNRYRGYDWMPEPCRSCDEKEKDFGGCR... | 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 pre... |
Q608P0 | MAGSEKSSLTKPRWLLAELTYACPLQCPYCSNPLDYARLGDELSTEEWKRVLSEARALGAVQLGLSGGEPLTRRDLAEIVTHARQLGYYTNLITSGYGLDEVRIAELKSAGLDHIQVSIQSPEKLLNDELAGTESFEHKLKVARWVKQHGYPMVLCVVIHRQNIHQMQQILEMADELGADYLELANTQYYGWALLNRDHLLPTREQFAEAEAIAQSYKEKVKGRMKIYYVVPDYYEDRPKACMNGWGTTFLTIAPDGMALPCHAARELPGLNCPSVRDFSIREIWYESAAFNRFRSYGWMKEPCRSCPEKEKDFGGCRCQ... | 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 pre... |
P71517 | MNAPTPAPSPVDVIPAPVGLLAELTHRCPLRCPYCSNPLELDRRSAELDTQTWLRVLTEAAGLGVLHVHLSGGEPTARPDIVEITAKCAELGLYSNLITSGVGGALAKLDALYDVGLDHVQLSVQGVDAANAEKIGGLKNAQPQKMQFAARVTELGLPLTLNSVIHRGNIHEVPGFIDLAVKLGAKRLEVAHTQYYGWAYVNRAALMPDKSQVDESIRIVEAARERLKGQLVIDLVVPDYYAKYPKACAGGWGRKLMNVTPQGKVLPCHAAETIPGLEFWYVTDHALGEIWTKSPAFAAYRGTSWMKEPCRSCDRREKDW... | 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 pre... |
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 corre... |
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
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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
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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
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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 +... |
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: [thior... |
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 ... |
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 +... |
Q6C0U8 | MLRLKSLKKPVQAVVRRFATTSAPTLSVGDNIHGFNVLRTKEIPEFDLQATLLEHSTGAQHLHIARDDSNNVFSIGFKTNPPDRTGVPHILEHTTLCGSEKYQVRDPFFKMLNRSLANFMNAMTAQDYTFYPFATTNATDMKNLRDVYLDATLKPLLRELDFSQEGWRLENEDSKDKTSPIILKGVVFNEMKGQMSNAAYAFYIRYLEKIYPSLNNSGGDPLVIPELTYEGLKKFHADHYNPSNAKTFSYGDISVADHLEALNAKFENCEISKTPGNTERLPLEFSSAAENTRIVEEGPIDTLLDTSKQHKMSMSWLMGS... | 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... |
P32898 | MLRFQRFASSYAQAQAVRKYPVGGIFHGYEVRRILPVPELRLTAVDLVHSQTGAEHLHIDRDDKNNVFSIAFKTNPPDSTGVPHILEHTTLCGSVKYPVRDPFFKMLNKSLANFMNAMTGPDYTFFPFSTTNPQDFANLRGVYLDSTLNPLLKQEDFDQEGWRLEHKNITDPESNIVFKGVVYNEMKGQISNANYYFWSKFQQSIYPSLNNSGGDPMKITDLRYGDLLDFHHKNYHPSNAKTFTYGNLPLVDTLKQLNEQFSGYGKRARKDKLLMPIDLKKDIDVKLLGQIDTMLPPEKQTKASMTWICGAPQDTYDTFL... | 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 ... |
P76440 | MPQQNYLDELTPAFTSLLAIKEASRCLLCHDAPCSQACPAQTDPGKFIRSIYFRNFKGAAETIRENNALGAVCARVCPTEKLCQSGCTRAGVDAPIDIGRLQRFVTDFEQQTGMEIYQPGTKTLGKVAIIGAGPAGLQASVTLTNQGYDVTIYEKEAHPGGWLRNGIPQFRLPQSVLDAEIARIEKMGVTIKCNNEVGNTLTLEQLKAENRAVLVTVGLSSGSGLPLFEHSDVEIAVDFLQRARQAQGDISIPQSALIIGGGDVAMDVASTLKVLGCQAVTCVAREELDEFPASEKEFTSARELGVSIIDGFTPVAVEGN... | 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(+) ... |
Q85228 | MPPSMIRVLYATDGCAITYSLMLLTGQEPSGAVYVVSYAWDGAGLDEAFSLPGERAEAELLARRPGVTFCLTGHVASVRVRPVFVAAATPAVVRALCRGEPLAARDVLEAMDEAATFALHDGLIAALTMVLEQVRPRTGNAEYAPERPLRSIAVGRRGLTSLFVHHETQTLAAFRRLYGNHNTPFWYVARFGPEEKTLVLATRLHLFHPRPAYDLRALKDLLLTYNPRVDPNPSGLDPAGLLSFAALSRFCCLSGYARGPAAAHAARYVDERVRADRAEMGVLRDYISHDRGSLKLPDREFVTYVYLAHFESFNRARLRE... | 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... |
Q08501 | MSSALAYMLLVLSISLLNGQSPPGKPEIHKCRSPDKETFTCWWNPGSDGGLPTNYSLTYSKEGEKNTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNEMGSSTSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWLPPTITDVKTGWFTMEYEIRLKSEEADEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWGQEKSIEIPNDFTLKDTTVWIIVAVLSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERL... | 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 recep... |
Q91513 | MMTKVGEVLLLLLLPAFVPHTDGTHYSLPGKPTEIKCRSPEKETFTCWWKPGSDGGLPTTYALYYRKEGSDVVHECPDYHTAGKNSCFFNKNNTLIWVSYNITVVATNALGKTYSDPQDIDVVYIVQPHPPEKLEVTVMKDQGWPFLRVSWEPPRKADTRSGWITLIYELRVKLEDEESEWENHAAGQQKMFNIFSLRSGGTYLIQVRCKPDHGFWSEWSSTSYVKVPEYLHREKSVWILVLVFSAFILLLLTWLIHMNSHSLKHCMLPPVPGPKIKGFDKQLLKSGKSDEVFSALVVSDFPPTTSNYEDLLVEYLEVYM... | 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 recep... |
P05710 | MPSALAFVLLVLNISLLKGQSPPGKPEIHKCRSPDKETFTCWWNPGTDGGLPTNYSLTYSKEGEKTTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNQMGSSSSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWSPPTITDVKTGWFTMEYEIRLKPEEAEEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWSQESSVEMPNDFTLKDTTVWIIVAILSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERL... | 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 recep... |
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.-
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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.-
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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.-
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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.-
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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 | MLKPMYYEFFFIFPKERELFESFLLDATHLALEESSLENLKAFDDKETIGFISQSNWHYFATHDPLKKDLKENLKEKPPHLKNFVILRSQKDLNNSLIPALEAFCLNLKQNLQSEFDFFYLSRNLASKDWLEAYKQAILPVQCTKFYIHPSWHQKPSHVVTNDCIMIDPALAFGSGHHESTSMCLELLSDIDLKRKNALDVGCGSGILSIALKKQGVSALVACDTDSLAVEETLKNFSLNQIPLLVQDKVIYGSTQKIEGRFDVIVANLVADVIKSLYSEFVRLCNHTLILSGILETHLNSVLQIYYNGFEVLEQRQRNE... | 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.-
|
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