ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q893G4 | MSKGVFITATGTDVGKTYISALLVKKLKQQGINAGYYKAALSGGVMIDGNIVAKDAEYVLKMSKIDKNPNDYVSYIFKLSASPHLAAQFENTEILMSKIVNDFEGIKNEFDYVTIEGSGGIICPIFIGEKPIMLIDIIKQLNLDIIIVSNSELGTINSTMLTVEYAKQNHINIKAIILNNFDSNNIIHIDNKRVIKELSRLTVYTCGTNVKDCEISLEDILNFYTDV | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
Q6NHE6 | MAIVVVTGTNTDVGKTIASAAVCQHYSRQGFRVVPVKPVQTGEPKGSGDAQTIEKLTGIVGKCFARFPEPLAPNLSAQRAGMQQLNLEEIVNKIRELDGPQTVVVVEGAGGLLVRLADSFTIADVAAQLDAPLIVVTNMALGSLNAAELTVEAAQRRGLKVLGLIGGSMPKNPDLATSLNVAEMEKVTGIPLWGSIAEGAGQLSKEAFCQLVEDLHLPTMWP | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
Q8FPS0 | MSILFISGTGTDVGKTIATAALASAFHHRGDRVIPVKPVQTGEPDGRGDIHTVEKLSGIRGVEFTRYPDPLAPNLAARRAGLPQVTLPDLAREIRDLDAPDRIVLVEGAGGVLVRLADDLTLLDVAAELDAPLVLVTSLGLGSLNAAELSVQAARTAGVEVLGLIGGSASPDPGLAEQLNHGELTRICRVPLLGVLPAGAGDLLPDDFQAMAQSCLTLPL | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
P46397 | MPFLFVSGTGTGVGKTFSTAVLVRYLADQGHDVLPVKLVQTGELPGEGDIFNIERLTGIAGEEFARFKDPLAPNLAARREGVEPIQFDQIISWLRGFDDPDRIIVVEGAGGLLVRLGEDFTLADVASALNAPLVIVTSTGLGSLNAAELSVEAANRRGLTVLGVLGGSIPQNPDLATMLNLEEFERVTGVPFWGALPEGLSRVEGFVEKQSFPALDAFKKPPAR | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
C4LIG1 | MSIVIMTGTGTDVGKTVATGAVACVLQKEGYEPFIVKPAQTGEPEGEGDAPRVTALTGIDNAETLYRFPEPLAPATSARRANMPYPELTTVAEEIKSFDKPGRVVLVEGAGGLLVRIGQDWTIADLARELGAPIIVVCSTGLGSLNEAELTVEAATRRGLTVLGLIGGSIPDSPDLATRCNKEDLPVVTGTDVLGYIPEGAGGWSQQRFVQEAPGFFVPDVVGRVTRESD | Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 ... |
Q47C04 | MIEDHLNTELAEIASAGLTRRRRVLETPCGRMATVDGTNLLNFASNDYLGLAGNADIARVLADGALQWGAGSGASHLVSGHLGPHELLEKEIAEFTGFPRTLTFSTGYLANLAVTPTLAGRGDAVFADKLNHASLIDAMQLAKANGAEVQRYPHNDVAALEKMLAASTAAHKIIVTDAVFSMDGDLAPLPLIFALAERYDAWLVIDDAHGFGVLGPHGEGSLGHFNLPASPRILLMGTLGKAAGVGGAFVAGSETAIEYLLQKGRSYIFTTAQPPAIACALAKSLQLIRDGDALRANLMDRIGQLRDGLAGLPMKLLPSP... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
B1I4F9 | MREFLEETLQKIEAAGLRRSLRPLEPLGPTRALFNGREVTLFCTNNYLGLTHHPRVTARAQEALRKYGTGSGAARLVSGHNPLLQALEEALARCKGSPRALVFPTGYTANLAVIGTLAGREDVIFCDRLCHASLLDGCLLSGAKLVRFSHNDADSLRRLLNQHTGRRRFIVTEGLFSMDGDIPPLPEFYTLAQEFEAILIVDDAHGTGVLGPNGRGTVADAGIPAERIVISGTLSKALASLGGFVTGPGLLSEFLLNRARSFIFTTALPPVSAAAALAALEVLEAEPAILEGLWENVMRFRQGLNARGLPASGNSPIIPL... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
B8J3V0 | MSDVAARLETIRAAHLYRRLRTLSTPQDREVVIDGRRVLLFSSNSYLGLGINAHIRRSAVRALEKFGTGAGGSRLVTGNMTPHMQLESALAAFKGSESALAFTSGYTANMGVISALCHKDTVIFSDALNHASIIDGCRLARGRTVVYAHNDMDDLLEKIRQLRPRQGFIITDGVFSMDGDLARLPELAHIARSYGLTLMVDDAHATGVLGATGRGTLEHFGLSHEDVPVVTGTLSKAIPSEGGFVCGSEILCELLRNTARPFIFTTAPSPAAVAAATAGIGHIAAHPGLVRRLQDNVAYFTGSLAEQGMHVPGQSPIIPI... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
A8ZUS7 | MSKLDFVEAELEKRRAASRLRTLRPVAPADGAAVTINGARLLNVCSNDYLGLSCHPLLVERAQAFAAQWGAGATASRLVCGNYTCFDRVEEKLARLKQTPAALVLNSGYQANTTLLPALCDRDSLILSDRLNHNSIIMGCRLARCAVTLFDHNDPAHLEKLLVETANRGFSRRLIVTESVFSMDGDCCDMDALAGLAQAHDALLMVDEAHATGVFGEQGMGLTCGKPVDVVMGTFGKGCGSFGAYVACSSALRDFFVNRCAGFIYSTGLPPAVLGSIDAALDLVPAMDAERQTLLDNAAHLRVRLATFGFDTGASSSQIL... | Function: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]
Sequence Mass (Da): 4... |
B3PI89 | MTRPVLVLVHGWGCDSRTWQPVLDGLRELVPVQLVDLPGFGNTPALETFSLPAVLAAIESQLPERCVLLGWSLGAMLAVQLAARLPQQVLGVISLAANARFVASDDYPHAMAPDVNRQFNSRFAEQPQAALKMFTGLLAQGDVQERALLKQLRTQVPDAINHNWAQALQLLAELDNRAALVQLSQPLLHLLAEQDALVPIAAAESLRGLNSQHQIHVIAGSAHAVHWSQPQQLISAVQDFYETLATAVDKKRVAQSFGKAAATYDSVAGLQRAVGAQLLDYLPAQLDRTRLLDIGSGTGFFTAQLATRGAEVIALDIAQG... | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway (By similarity).
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H... |
Q21FY5 | MSNIEPSNVKPSNIELGTIPLAEAPATKLEAAYIAKKIAPNNSNPNAPVWVFVHGWGASANTWAPLVDELKSQCEIWLLDLPSFGGNTQAVNSPSAVAADIAKILPANTVLVGWSLGGMLLPLIAQQIEQHWPTKTISHCIGLAANAKFAQGDNYTAAMPAETFQTFCANFNVDPTTTWSRFGLLQAQGDSNRKLVSRQIKALHNAPMPEQFTAWQQALTWLGAIDNRVLLCEITTPFLHLFGEGDALVPADAAVAMAGINPLHQTLVVASAGHVLHFSQPAKIAQIMLARVHAKRNKARVAKSFSNAATEYDSVAYLQQ... | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway (By similarity).
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H... |
C5BMZ8 | MTEVNVRAAATPEEKPFLNRTRHEPANPQPNRSVLVFLHGWGSDKRQWQSFVPTLLEALGDEREMVFIDLPGFGDNSDFRCDDLEHMLKQLARIIPGNATLIGWSLGGMIATQLASRHPEKIGRLITIATNPLFVKNDAEIAAGKAPWKHAMERETFSDFVNGFADDPEATLKRFIALQSMGDSERRQVTDTLKNLLSFSAHSQQTCWANALSYLDQLDNRTALRNLTQPALHIYGKSDALVPVRAGRALQGLAPSHWVESITAAGHAPHISHPREVATMINSFLRQQAPRLSQRKRRIANSFSSAAQEYDTLARLQKRV... | Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway (By similarity).
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H... |
A0KF11 | MSVSVERFGQGPDLVLLHGWGMNGAVWHGIVPALASRYRVHLVDLPGFGNSPLAGEVEYSLPWLAEEVAAILPEQCHLLGWSLGGLVASQLALSHPERLHSLITVASSPCFMARDEWPGIAPKVLAGFNQMLAGDFKQTIERFLAIQAMGSEHARDDIRQLRHWLAERPAPQLAALEAGLGLLAEVDLRDELTPLSLPWLRVYGRLDSLVPKASIPLLDERYPSSRSVVLEKASHAPFISHPQQFIEIIEHFVG | Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl e... |
Q9WZQ6 | MRQLIKAGIFTALIVVGAWISIPLGPVPFTLQVFFVFLSAYVLGKKYGTLAVATYVLLGAMGLPVFANFKGGAQVLVGPTGGYLFGFILGAFVIGLLAEKKESFAWYLASGVAGLGIIYALGVFVLNFYVHDIRKAISVGFVPFVWFDLIKLVVAALIALRLKKLEVER | Function: Substrate-binding (S) component of an energy-coupling factor (ECF) ABC-transporter complex. Probably a biotin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number o... |
O83256 | MHRTEPTINCVHDGTRSLHLSIDTTRALPAHSGNEPTRTHLAAVRVSLLKTIPVAPPKILKDSSFRVTLRIDPSEEYCTMHRSKSLAFVALFAALISSSALVSIPLKPVPLVLQNAAAVLTGLLLGPRDGALAVLSFLGAGLLGLPVFSGGRGGYTALFAPTGGFLLGYILAATLAGAIAQHHRLSCTPPRGGGRALLLWIRLTVATLVGFLSIYSIGLPVLGYVLGLRTGELMLGVFLPFFLADTLKIALVVLLAHHLAPTVRRHLYRHG | Function: Probable biotin transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28773
Sequence Length: 271
Subcellular Location: Cell membrane
|
Q7CTU0 | MQTRSSRMAGFGHAVPARCVDNAEIEASLGLEAGWIERRTGIRSRYWAEAGDTLSGLAERAGRMALEDAKINADDIALTLLATSTPDHLLPPSAPLLAHRLGLTRSGAIDLAGACSGFLYALTLADGFVRTYGRAVLVVAANILSRRINPAERASAVLFADAAGAVVLTPCPEVKRGVLSADLVADGSGYDLIQIAAGGSSQPFSAGMIAEDALMTMRDGREVFSRAVALMTNTSQRVLHEAELTAADISRFVPHQANARMSDAVCGNLGIEREKTVRTIGSFGNSSAATIPLSLSITNAERPLAGGETLLLTAAGAGMT... | Function: Involved in the formation of the biotin precursor pimeloyl-ACP . Catalyzes the condensation of glutaryl-CoA, an intermediate in lysine degradation, with malonyl-ACP to produce 3-oxopimeloyl-ACP .
Catalytic Activity: an acyl-CoA + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34135
S... |
D0MCQ4 | MLPEQSLTTPLPATATAAPARRAAVLGVGAALPAHREPSTETERRLGLPPGWIARRTGIRERPLVGPDEATSDLAVRAGAAALAQAELSPERIGLLLLATSTPDHLLPPTAPVVAHRLGLKHAGAVDLAGACSGFLYALALADGYVRLQRTCVLVIGANVLSRRTNPDDPKTSALFADGAGAVVLGPSEGSRGIVACWLGADGSCWDDLYIPAGGSRRPLTPERVARGEHLMYMKDGRALFRRAATGMAEAGRRVLQQAGLDLDDVAWWIPHQANHRLIEEARRQLGMPEARTVNLVDRIGNSSAATIPLALALEAHRFA... | Function: Involved in the formation of the biotin precursor pimeloyl-ACP . Catalyzes the condensation of glutaryl-CoA, an intermediate in lysine degradation, with malonyl-ACP to produce 3-oxopimeloyl-ACP .
Catalytic Activity: an acyl-CoA + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 36075
S... |
Q6J2K6 | MDEEARAAGCSPAPPRAPAASCGAAAELCLCSPTGVEGIEQVPGCPCFEDAGAVVVSGEAPEGPGVLCSGDGAELKLAEQGALDVRLGSPAVGIHEQQLLHRGTSGSDEAGAINEISPVEVSPSEASSNLDTAGAIGGSPLMLESLPETSDTRGCEQEVMPGVVVGSSNRDASSEVGVESECGSDADGRNGLGEGELVSSVDGGGAEKSSKVTGVLSEEGVDGMETALEPCVASVGSITQVEEGVDRMETSLDDSEASDGSTTQDFDTDVETESSGSSIEEQDMGYGVHIPHTEQAICEVARGNKSSEVKSSDRMSSVTL... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: May play a role in responses to biotic and abiotic stresses.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 58675
Sequence Length: 569
EC: 3.1.3.16
|
Q46036 | MRILPVVAAVTAAFLVVACSSPTPPKGVTVVNNFDAKRYLGTWYEIARFDHRFERGLDKVTATYSLRDDGGINVINKGYNPDREMWQKTEGKAYFTGDPSTAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEMKQQMLAIATREGFEVNKLIWVKQPGA | Function: Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 19921
Sequence Length: 177
Subcellular Location: Cell outer membrane
|
P0A902 | MRLLPLVAAATAAFLVVACSSPTPPRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKVTATYSLRDDGGLNVINKGYNPDRGMWQQSEGKAYFTGAPTRAALKVSFFGPFYGGYNVIALDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWVQQPGS | Function: Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 19852
Sequence Length: 177
Subcellular Location: Cell outer membrane
|
Q08790 | MRAIFLILCSVLLNGCLGMPESVKPVSDFELNNYLGKWYEVARLDHSFERGLSQVTAEYRVRNDGGISVLNRGYSEEKGEWKEAEGKAYFVNGSTDGYLKVSFFGPFYGSYVVFELDRENYSYAFVSGPNTEYLWLLSRTPTVERGILDKFIEMSKERGFDTNRLIYVQQQ | Function: Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 19686
Sequence Length: 171
Subcellular Location: Cell outer membrane
|
A2Y2B7 | MAKVHRLMNAVLRLAAAAAAATAAVVMVTSRETTSFFGIQMEAKYSYTPSFIFFVVAYAVAAAYSLLVLAVPAGSALSRLALTTDVVLGMVLAGAVASAGAISDIAKNGNSHAGWLPVCGQIHAYCNHVMAALIAGFVALAVHFVVVMYSLHIVTDVICPCH | Function: Involved in cell elongation in rice through dual regulation by brassinolide and auxin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16798
Sequence Length: 162
Subcellular Location: Cell membrane
|
B3LP78 | MLPTSVSRSLYLKTFRSHLLRAPQIVLKRMSSSIDISKINSWNKEFQSDLTHQLATTVLKNYNADDALLNKTRLQKQDNRVFNTVVSTDSTPVTNQKSSGRCWLFAATNQLRLNVLSELNLKEFELSQAYLFFYDKLEKANYFLDQIVSSADQDIDSRLVQYLLAAPTEDGGQYSMFLNLVKKYGLIPKDLYGDLPYSTTASRKWNSLLTTKLREFAETLRTALKERSADDSIIVTLREQMQREIFRLMSLFMDIPPVQPNEQFTWEYVDKDKKIHTIKSTPLEFASKYAKLDPSTPVSLINDPRHPYGKLIKIDRLGNV... | Function: The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homoc... |
P13497 | MPGVARLPLLLGLLLLPRPGRPLDLADYTYDLAEEDDSEPLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAVDLRRHTARKSSIKAAVPGNTSTPSCQSTNGQPQRGACGRWRGRSRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins . Thereby participates in several developmental and physiological proces... |
P98063 | MPGVARPPLPLLSLPLLLLLLLLPRAGRPLDLADYTYDLGEEDAPELLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAAVLRQQTARRPSIKAAGNSSALGGQGTSGQPQRESRGRWRGRPRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPSIGQRTRLSKGDIAQARK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins. Thereby participates in several developmental and physiological process... |
P98070 | MDYSYDLEEVVEETIDYKDPCKAAAFWGDIALDEEDLANFKIDRIVDLTKHTIHTVSGAATNISRPEKGRRTRKERRRSREKRASTSRPERVWPDGVIPYVISGNFSGSQRAIFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDDHVSIIRENIQPGQEYNFLKMEPEEVESLGETYDFDSIMHYARNTFSRGIFLDTILPKYDVNGVRPPIGQRTRLSSGDVAQARKLYKCPACGETLQDSQGNFSSPGFPNGYSAYMHCVWRLSVTPG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease involved in pattern formation in gastrula and later differentiation of developing organs. Able to cleave chordin (chrd), suggesting that it may act in dorsoventral patterning during early development by regulating the chordin (chrd) activity.
PTM: Proteo... |
P08558 | MSNTVTLRADGRLFTGWTSVSVTRSIESVAGYFELGVNVPPGTDLSGLAPGKKFTLEIGGQIVCTGYIDSRRRQMTADSMKITVAGRDKTADLIDCAAVYSGGQWKNRTLEQIARDLCAPYGVTVRWELSDKESSAAFPGFTLDHSETVYEALVRASRARGVLMTSNAAGELVFSRAASTATDELVLGENLLTLDFEEDFRDRFSEYTVKGYARANGAEGDDIDAKSIVSRKGTATDSDVTRYRPMIIIADSKITAKDAQARALREQRRRLAKSITFEAEIDGWTRKDGQLWMPNLLVTIDASKYAIKTTELLVSKVTLI... | Function: Forms the central cylindrical hub of the baseplate and plays an important role in baseplate and tail assembly (Probable). Core component of the initiator complex that triggers the tail tube polymerization during tail assembly (Probable). Forms a conduit that probably functions as an extension of the tail tube... |
Q9T1V4 | MERVNDSALNRLLTPLMRRVRLMLARAVVNVINDGRKVQNLQVGLLDDEESDEVERLQNYGHFSVPLPGAEALIACVGAQRDQGIAVVVEDRRYRPTNLEPGDAGIYHHEGHRIRLTKDGRCIITCKTVEVYADESMTVDTPRTTFTGDVEIQKGLGVKGKSQFDSNITAPDAIINGKSTDKHIHRGDSGGTTGPMQ | Cofactor: Binds 1 Ca(2+) cation per trimer. Ca(2+) plays an important role in interaction with the host cell membrane.
Function: Component of the baseplate that forms a central needlelike spike used to puncture the host cell membrane for tube insertion during virus entry. Probably involved in baseplate and tail assembl... |
A9BME3 | MTHPNDLPLQALQFYATAAYPCSYLDGRLARSQVATPSHLIQNSAYSELVSLGFRRSGMFTYRPYCDGCRACVPMRILVHDFRPDRSQRRAAARHADLTASIQRLHYSNEHYQLYLRYQQSRHSGGGMDHDSVDQYTQFLLQSRVNSRLVEFRTPAADGGIGTLKMVSILDVLEDGLSAVYTFYEPNDPASYGTFNVLWQIDQARSMSLPYVYLGYWIADSQKMNYKARFLPHEVRVDERWQRVDQLPR | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
Q0BTF8 | MNDSKPLYRPQFFYTTGASPCPYLDGRMERKVVTEITGPDAETLHNRLSRAGFRRSHNIAYAPVCQGCNACVPIRIAVNDFRLTRTRRRINRTNAGVEMFDVPAQATHEQFMLFQRYQKSRHGDGDMAAMGFTDYRAMVEDTPIQTSILEFRDQDDVLLCACLTDRLNDGLSAVYSFYDPDLPQRSLGSYAILSMVAQTKAEGLPYLYLGYWVANSRKMAYKSAYQPAEILSRGAWRPLTQADIEEQEEQTRPLFRPSATGFSTGQE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
A1WWV3 | MSRSRITLLRTHCHECAYVSGRTARLEFLSPTLRLNDHRYQLLLEQGFRRSGPYVYRPHCPGCKACQSLRIPVARFRPRRRHRRCQRANANLHVTACPPVMTQEHLALYRRYIDHRHPRSSMANPDHAEAEGFLAAPWCTTVFYELRTEAQGSLLAVAVTDVLPDALSAVYTFYAPEAEHRGLGNLAVLWQLSEARRLGAQHLYLGYWIADAPAMAYKASFRPHEIFDGRGWRAQE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
P59794 | MRLVEFYSEKKVCSYIDSKQSIFRYFHIQNVTPSFYYGLLERGWRRFGNYFFTPMCEGCTDCISIRTLIDDFTFSRNHKRLLKKAQNIDIYIQKPTITQAHIELYNRYHRVMRDKKGWEYTPTTPESYMDMFVEGHQDFGYEILYFIDSQLVGVGLVDALFDSITAVYFYYDHTFAHHSLGTLNILKQIQIGKENGLKYFYPGYWIKDHYCMGYKQRFTPFEVLKNIPDVFEAPIWEMYNG | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
Q0C3S3 | MKFSDPHLLPAGLERSLRFYVTNPSPCPYLPDRKERKAFTNLAIPEADALHNVLSQSGFRRSQSIAYRPACTRCNACKSVRVATREYDISRNDRRVIARNAHLVRRPVAAQATREQFRLLKSYVVTRHDNGGMSDMTYRDYVAMVGGSPVQSLIFEYRDGPEPDAPLVAAAITDVLRDGLSMVYTFFDPAKTSQSLGHYLILDHIRHAHDLGLPHLYLGYWVKGSPKMDYKRRYKPLEVLDGDRWRPLRDDE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
Q72R21 | MIQNKLQNFVDTLPISPEKSCSYYPERLSQIQYFPFPEEISKEVLQFFFDSGFRRNGNILYRTSCCGCKDCLSYRIPLDQFVPSRNRKKLLKKNSDLKICFESPNLTLEKEILYLRYQRSRYQNFVIEESDQELLEGMRWNLFEYKENSLEMTLSLDGKILCFMILDFASDSLSAVYSVYDPDYPDRSLGSFAILSSILYAKELGMKYFHLGYFLPGHPNMDYKKYWTPAQIREPVSNENRWIETDDFQKRYSDFSW | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-glutamyl-[protein] = H(+) + N-terminal L-leucyl-L-glutamyl-[protein] + ... |
F1QW93 | MSDVKPPQHFTMNGNPPPPEFKNPKKPGRLTNHLQYIEKVVIRALWKHHFSWPFRQPVDAVRLNLPDYYTIIKNPMDLTTIRKRLENNYYWKAMECVEDFNTMFTNCYVYNRPGDDIVLMAQVLEKLFLEKVAEMPEEEYEISALTTKGPVKGARKSTIGLKKRPPSPMSEVVFQQTVTVIPPDALHTIPSAPLSAQLTAKLKNGVKRKADTTTPSASSIPSCESSSCVTEPKVLKLFSRRGSGRPIKPPCKDLPESPPQHQVGRRTKLSERLKYCNAILKEMFSKKHSAYAWPFYKPVDAETLGLLDYHEIIHQPMDMS... | Function: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the pr... |
Q58F21 | MSLPSRQTAIIVNPPPPEYINTKKNGRLTNQLQYLQKVVLKDLWKHSFSWPFQRPVDAVKLQLPDYYTIIKNPMDLNTIKKRLENKYYAKASECIEDFNTMFSNCYLYNKPGDDIVLMAQALEKLFMQKLSQMPQEEQVVGVKERIKKGTQQNIAVSSAKEKSSPSATEKVFKQQEIPSVFPKTSISPLNVVQGASVNSSSQTAAQVTKGVKRKADTTTPATSAVKASSEFSPTFTEKSVALPPIKENMPKNVLPDSQQQYNVVKTVKVTEQLRHCSEILKEMLAKKHFSYAWPFYNPVDVNALGLHNYYDVVKNPMDLG... | Function: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis . Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the p... |
F7DRV9 | MSMSSRHLHSSIVNPPPPEYINRKKTGRLTNQLQYLEKVVLKALWRHHFSWPFQQPVDAAKLNLPDYYQIIKNPMDLSTIRKRLEYNYYSKALDCIQDFNTMFTNCYIYNKPGDDIVVMSQELEKVFMEKIAEMPHEEIELSVVGNRGVKSRIKISAVAAEVCKKKMVSQKMHRRTFPCPVIAMMPKRTTLVPLSVIRSSTSSHSASSVSKVNKGIKRKADTTTPAVSLIATSCESSPTLSEPKPNKILSGTEKTRSAETSAVDLPDSQHHIHFIKSNQICEQLKHCNNILNEMMSKKHAEYAWPFYKTVIPTSLLDCSD... | Function: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the pr... |
Q8RXD6 | MASTGEPDRKRRHFSSISPSEAAAAVKKQPFFWPSSEDKLDTAVLQFQNLKLSQKLEAQQVECSILEDKLSQIKEKQLPYNSSLKTVHKSWEKLTASVESCSVRVSDSSSGAHRFVNKEDGSSPAVKNDFINRLLETGATESSSSNICSNQMEENGVNTSSQMTQTLYNLVAATEDLRCLKDELYPTVLRTNLGKDLCGQLALSELESEIKSFRGDLDDVLVKFKSLSRELQSHRDADAKVRVDLKRIRGELEDEVVELQQCNGDLSALRAERDATAGAFFPVLSLGNKLATSDRERDKQRDLQDMETVLKELTVLASGR... | Function: E3 ubiquitin-protein ligase that monoubiquitinates H2B to form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and maybe H3K79me. It thereby plays a central role in histone code and gene regulation. Forms a ubiquitin ligase complex in c... |
Q5ZLS3 | MSGAGNKRAAGEPGPSAPPEKKAGVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIINRYWNQFDENIRIILKRFDLDQGLGDLLSERKALVVPEPEPDSDSNQERKDERERGEGLEPAFSFLATLASSTSEEIESQLQERVESSRRAVAQIVTMYDKLQEKVDVLSHKLNSGDISLMEEAVLELNSYLSHENGRLQELADTLQEKHRIMSQEFSKLQEKVETAESRVSVLETMIDDLQWNIDKIRKREQRLNRHLADVLERVNSKGYKVYGAGSSLYGGTITI... | Function: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respe... |
Q5VTR2 | MSGIGNKRAAGEPGTSMPPEKKAAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDNLIVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITI... | Function: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respe... |
Q5DTM8 | MSGIGNKRAAGEPGTSMPPEKKTAVEDSGTTVETIKLGGVSSTEELDIRTLQSKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLDQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGDGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVDLLSRKLNSGDNLIVEEAVQELNSFLAQENVRLQELTDLLQEKHHTMSQEFCKLQGKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITI... | Function: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1) . H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, resp... |
Q7XU27 | MGSTGEPDRKRRLSSSVAPGGGAPVSPAKRLAVAPTSEDKKLDFTVLKYKNQKLSEQLEAHKFEYRALENKFAGLKEKQRTHNETLSLVNSSWEQLVADLKSRSFCKSGSPNSSPGSGHNNVQKDGTCAPIERDTLRSLVESGATESSGCLPGCHLGSDAPPLHLSTANALGDIFFPSSDLLQANEECALAALTKLPENDRSKQLQSTSSNLLSSLNNVVQALSNLQLKHKQLAEDYQNQRDSSARKRAEHRRLKEELASAASELEETNYKLAALKAQRDNTQGARIPYPTLGNKNMPEDKVRDKQREMQDLEATHKELS... | Function: E3 ubiquitin-protein ligase that monoubiquitinates H2B to form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic transcriptional activation and is a prerequisite for H3 Lys-4 methylation (H3K4me). It thereby plays a central role in histone code and gene regulation. H2B monoubiquitination (H2BK143ub1)... |
Q9C895 | MENQESDEPMQKKPHLLDSVSPNSMARNSSPSHPIAKSVSFFDCDFSLLCLRLVDYEIDVDATVLQLQNQKLVQQLDLQKKQLYDVESKIQELQLNQTSYDDELISVNQLWNQLVDDLILLGVRAGANQEALNYLDIVDKKRVPPCAADETFLCRLLQVDSLDTSKSDEVVRKVEEALALRHSSTMELMGLFENTIDTQKTKAESISQSLHAVKSTEDATIQLSSINDLMKEESKNLREMIDALHVRHKEHSEQIQAYISSHSTDQSELKHLKGQLEEIKAELEENRRKLITLKMQKDAACEGHVTSPAIANGSLSPEKP... | Function: E3 ubiquitin-protein ligase that monoubiquitinates H2B to form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and maybe H3K79me. It thereby plays a central role in histone code and gene regulation. Forms a ubiquitin ligase complex in c... |
A2ZAC2 | MDAAALQYENQKLVQQLEAQKSKMRALEGKFKELRDEQCSYDNTLICLNKMWNQLIDDLVLLGVRAGGDLNGLQALDHEEMSEESLESCPSEEIFLFRLLNSRNFRNNDDSSLSKLVEEALALRYSTTVTLMKSLQEAFAVQQARSESLSLALNGQNSSEDVIVALENHNDYLKEVVDNLRQAVSIINRKHEKYLDEIEAFKNNQSRELHEVKCLSGELEESMAELEESRRKLAVLQLQTGGGSLMNTSAPNGVNGSVSTDKSSDKGMGWRDLKDAVEEAKTLAANRLFELHETQEDNLILSKQLEDIQDQLKDENYIVT... | Function: E3 ubiquitin-protein ligase that monoubiquitinates H2B to form H2BK143ub1. H2BK143ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and maybe H3K79me. It thereby plays a central role in histone code and gene regulation. Forms a ubiquitin ligase complex in c... |
B0R5N7 | MSNRSQFVPSWLVPEAAGDLPLTVSRLSLLALAAAFAVGYGAGFAVPLEVQAGVYLLGMVAMNLPHGGYEHFENLRRRAASFQGKYIVAYLVGIAAFGALFFVAPVAGLGLAVTVAVAKGGFGGVQSMDALYGTDHLRTRPQRWLAAVVRGGAVMVVPMLFWTDVFYAFSSVMISIFDPSAVSALGGDIATRRLVLGGGYGALVVAHLGLGYRRAAGTGSFLADAAETLLLIAYFALVPVVIAVGLYFPLWYSARQVARSSAVDDTAMTQADATGMLDALDADDPARATLASWAVLIVGSVATFGLAAVLWLLSPQPLGG... | Function: Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal.
Catalytic Activity: all-trans-beta-carotene + O2 = 2 all-trans-retinal
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37569
Sequence Length: 359
Subcellular Location: Ce... |
Q9UT30 | MEMYVEDVPMPDIGPDSVLNTPIRPKYEILKSKKKTQNENDPEPMDISMSPDEKNLKKSTVRRKLRKSKPNSSSNQVSSRTRALTKRSNSSNAIIKANNQDSVYVSDWTNVHRDIPIVVSGYLQLMFNACVASIFLYFLFKIVFGIQNDVRNRVEYHKILQEEQAADCQREYLSINCDSPGPAIFEVCQKLKQCKMESSNNVGSTKLAALVFAEIIDAFISHISYKTMVFSLILVFGSLLTSNYAFGLYRARHSQNIHDYAANAIPAMIPSSRFLPSNLSDISNRNLIEAASQEEEI | Function: Involved in mRNA and protein export from nucleus.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33574
Sequence Length: 297
Subcellular Location: Endoplasmic reticulum membrane
|
P53062 | MELRSFSRQPDGILANPRLGREEVLEGEHPQDARLARQSIWLSPSLIAEYIQLFFNFIIGTIGLSLAIKFILMIRNDVNLKLEHNVREELDKIATCKSRYFENQCEPHMRVPALEVRCNEWSKCMNKEIVSGSDYQWAKAWARTLAEVINAFFEAFSIRSFLFILISIIGIIFVTNTSFGSYRVYLNNKDTKSVRHA | Function: Required for mRNA nuclear export. Involved in the nuclear pore complex (NPC) distribution and nuclear envelope morphology.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22807
Sequence Length: 197
Subcellular Location: Nucleus membrane
|
C0HJG8 | YSLQNDPEITLIDSTIEWDEGYDVTARFLDYLNSLDAGFVAELENKTVEQLWSEYKASYGPNGQ | Function: Metalloprotease, digests gelatin and azocasein (in vitro).
PTM: Glycosylated.
Sequence Mass (Da): 7324
Sequence Length: 64
EC: 3.4.24.-
|
A0A2K4Z9J5 | MSTFQALMLMLAIGSFIIALLTYIEKIDLP | Function: Toxic component of a type I toxin-antitoxin (TA) system; overexpression in the absence of cognate antisense antitoxin SR5 RNA leads to cell lysis . Base pairing occurs between the 3' UTRs of bsrE mRNA and SR5 RNA which leads to bsrE mRNA degradation initiated by RNase III (rnc) and RNase J1 (rnjA) . Genetic e... |
L8EAY0 | MTVYESLMIMINFGGLILNTVLLIFNIMMIVTSSQKKK | Function: Toxic component of a type I toxin-antitoxin (TA) system; expression in the absence of cognate antisense antitoxin SR4 RNA leads to cell lysis . Induced expression causes membrane invaginations that dislocate the cell wall synthesis machinery, leading to eventual death. Unlike many type I TA systems it does no... |
A0A2K4Z9K4 | MHVSTFQALMLMLAFGSFIIALLTYIKKK | Function: Possible toxic component of a type I toxin-antitoxin (TA) system; an overlapping antisense RNA has been identified.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3317
Sequence Length: 29
Subcellular Location: Cell membrane
|
A0KLG5 | MHKKTLLATLILGLLAGQAVAAPYLPLASDHRNGEVQTASNAWLEVDLGAFEHNIQTLKDRLGDKGPKICAIMKADAYGHGIDLLVPSVVKAGIPCIGIASNEEARVAREKGFTGRLMRVRAATPAEVEQALPYKMEELIGSLVSAQGIADIAQRHHTNIPVHIALNSAGMSRNGIDLRLADSKEDALAMLKLKGITPVGIMTHFPVEEKEDVKMGLAQFKLDSQWLLEAGKLDRSKITIHAANSFATLEVPDAYFDMVRPGGLLYGDSIPSYTEYKRVMAFKTQVASVNHYPAGNTVGYDRTFTLKRDSWLANLPLGYS... | Function: Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Is not active on negatively... |
P33967 | MKTFNISQQDLELVEVATEKITMLYEDNKHHVGAAIRTKTGEIISAVHIEAYIGRVTVCAEAIAIGSAVSNGQKDFDTIVAVRHPYSDEVDRSIRVVSPCGMCRELISDYAPDCFVLIEMNGKLVKTTIEELIPLKYTRN | Function: Catalyzes the deamination of the cytosine moiety of the antibiotics blasticidin S, cytomycin and acetylblasticidin S.
Catalytic Activity: blasticidin S + H(+) + H2O = deaminohydroxyblasticidin S + NH4(+)
Sequence Mass (Da): 15573
Sequence Length: 140
EC: 3.5.4.23
|
I0J1I6 | MPFSRTLLALSLGMALLQNPAFAAPPLSMTDGVAQVNTQDSNAWVEINKAAFEHNIRTLQTALAGKSQICAVLKADAYGHGIGLLMPSVIAMGVPCVGVASNEEARVVRESGFKGQLIRVRTAALSELEAALPYNMEELVGNLDFAVKASLIAEDHGRPLVVHLGLNSSGMSRNGVDMTTAQGRRDAVAITKVPNLEVRAIMTHFAVEDAADVRAGLKAFNQQAQWLMNVAQLDRSKITLHAANSFATLEVPESHLDMVRPGGALFGDTVPSHTEYKRVMQFKSHVASVNSYPKGNTVGYGRTYTLGRDSRLANITVGYS... | Function: Amino-acid racemase able to utilize a broad range of substrates. Is mostly active with lysine and arginine and, to a lesser extent, with ornithine, whereas is about 10 times less active with alanine, methionine and ethionine. With phenylalanine as substrate only a trace activity is detectable, and is inactive... |
Q9KSE5 | MHFKATLLSLSIAATLPSFSLSAAPLHIDTALPDAAQIQQSNSWLEISLGQFQSNIEQFKSHMNANTKICAIMKADAYGNGIRGLMPTIIAQGIPCVGVASNAEARAVRESGFKGELIRVRSASLSEMSSALDLNIEELIGTHQQALDLAELAKQSGKTLKVHIALNDGGMGRNGIDMTTEAGKKEAVSIATQPSLSVVGIMTHFPNYNADEVRAKLAQFKESSTWLMQQANLKREEITLHVANSYTALNVPEAQLDMVRPGGVLFGDLPTNPEYPSIVSFKTRVSSLHHLPKDSTVGYDSTFTTSRDSVLANLPVGYSD... | Function: Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Among these substrates, is ... |
O87943 | MSDVQTLEYKGKVVQFAPENPREAEIPADELHEHLQNPSTERTRRLKARCRWKHAAAGEFCEKGVTAGIERMRLLTESHWATRGEPEPIRRAHGLKNILDKSTLVLQTDEFIVGYHAEDPNMFPLYPELSYMAVQDYLKSKYSPQPAKEAQEIVDYWKPFSLQARCEPYFDPVDLHRGYQVSTIEGPVFATGYNSVIPPYETVLEDGLQARIALAEEKIEHARAEMEKFPWHAPSGLEWIDKIDNWKAMVIACKAVIAWARRHARLCKIVAEHFETDPKRKAELLEIADICQRMPAEPARGLKDAMQSKWFTFLICHAIE... | Function: Catalyzes the addition of fumarate to the methyl group of toluene, leading to the formation of benzylsuccinate.
Catalytic Activity: fumarate + toluene = 2-benzylsuccinate
Sequence Mass (Da): 97736
Sequence Length: 861
Pathway: Xenobiotic degradation; toluene degradation.
EC: 4.1.99.11
|
O87944 | MSATPHTQVHWEENTARPCRKCKWQTPDPTDPLRGQCTVNRHAMGGVWKRWIRDVEHMTCSRHEEGELSFRDHV | Function: Catalyzes the addition of fumarate to the methyl group of toluene, leading to the formation of benzylsuccinate.
Catalytic Activity: fumarate + toluene = 2-benzylsuccinate
Sequence Mass (Da): 8752
Sequence Length: 74
Pathway: Xenobiotic degradation; toluene degradation.
EC: 4.1.99.11
|
O87942 | MTTCKDCAFFFSIPEDADDFEKSKGDCVTQKDDEKGRYWLSKPVFENDQCCGAFHKR | Function: Catalyzes the addition of fumarate to the methyl group of toluene, leading to the formation of benzylsuccinate.
Catalytic Activity: fumarate + toluene = 2-benzylsuccinate
Sequence Mass (Da): 6619
Sequence Length: 57
Pathway: Xenobiotic degradation; toluene degradation.
EC: 4.1.99.11
|
O87941 | MKIPLITEIQRFSLQDGPGIRTTIFLKGCPLRCPWCHNPETQDARQEFYFYPDRCVGCGRCVAVCPAETSRLVRNSDGRTIVQIDRTNCQRCMRCVAACLTEARAIVGQHMSVDEILREALSDSAFYRNSGGGVTISGGDPLYFPDFTRQLASELHARGVHVAIETSCFPKQGKVVESMIGIVDLFIVDLKTLDAHKHLDVIGWPLAPILANLETLFAAGAKVRIHIPVIPGFNDSHADIDAYAEYLGKHAAAISGIDLLNFHCYGEGKYTFLGRAGSYQYSGVDETPAEKIVPLAQALKARGLAVTIGGIVGIANGKNE... | Cofactor: Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of benzylsuccinate synthase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce... |
Q9GZN4 | MVVSGAPPALGGGCLGTFTSLLLLASTAILNAARIPVPPACGKPQQLNRVVGGEDSTDSEWPWIVSIQKNGTHHCAGSLLTSRWVITAAHCFKDNLNKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEPHPVYSWKEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGSIQDGVPLPHPQTLQKLKVPIIDSEVCSHLYWRGAGQGPITEDMLCAGYLEGERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHRSWVEKIVQGVQLRGRAQGGGALRAPSQGSGAAARS | Function: Preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA.
Sequence Mass (Da): 33732
Sequence Length: 317
Subcellular Location: Secreted
EC: 3.4.21.-
|
P39988 | MPRLLATQSHVVHGYVGNKAATFPLQCLGWDVDCCNSVQFSNHTGYGLDKVFGTITRETDLKELLSGLFDNFSQDYQALLSGYLPNKNSVRCMGTYYAKFKEANPEMIWLMDPVMGDEGQLYVSEDVIPEYRKLALSPKQLVDIITPNQFELEILYGGEIKTKEHLKKALKKLHQTIPVIIVTSCDCKMFDDKDFIYCVASMEGKTPIVYRVPFIDSYFTGVGDLFSALLLDRVYKILSNPTTTLKFEDQVNNVLNVIQKVLKITRSYASGKMKAKMGSALEMKEMELRLIESRDIYETINIHQTDYIYARL | Function: Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection.
Catalytic Activity: ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 35559
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 2.7.1.35
|
P53727 | MTSTLHTTKKVLSIQSHVIHGYVGNKAATFPLQYRGWDVDVLNTVQFSNHSGYAHFTGFKCSTEELVDIVEKGLIGSLRIKYDAVLSGYLPNVQALQKVAGIVGQLCEGSENVKWILDPVLGDNGRLYVDRECVAVYQDILQNFKIFLATPNQFEMELLVGMSIRTLDDAKQAFKLFHKKYPRVSRIVVTSLELSEFLSNDTYVVAGFDCSASEEIFFYEIPKINAKFSGSGDLISAMLTDSLLGDRRCTQLSLSASLGQVLWLVTSILQKTYDLNIAERGPQDSTIDIKDLKLIQCRDILKQDLIPSIGKPKTIKI | Function: Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection.
Catalytic Activity: ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 35367
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 2.7.1.35
|
Q55DA6 | MSRPEHIAPPEIFYDDVESKKYSSNSRIIEIQTKMAERAYELLAIPETAEGLMLLDIGCGSGISGDVITDAGHYWIGCDISQHMLDVAIDREVEGDVMLRDIGQGFPFRAGSFDAAISISAIQWLCNAEKSHHNPRKRLHTFFQSLFNVLTRGGKAILQFYPENSAQIEMITASALRCGFSGGLLIDFPNSSKAKKYFLVLFTGNNNIMPSAKGVEGEEYEQQEEEDSNEVKYSNRKRDRRRVTKSKGSAQHKTKEWIMNKKDRQRKQGREIKNDSKFSGRKRGPKF | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (By similarity).
Catalytic Activity: a guanosine in 18S rRNA + S-adenosyl-... |
O43709 | MASRGRRPEHGGPPELFYDETEARKYVRNSRMIDIQTRMAGRALELLYLPENKPCYLLDIGCGTGLSGSYLSDEGHYWVGLDISPAMLDEAVDREIEGDLLLGDMGQGIPFKPGTFDGCISISAVQWLCNANKKSENPAKRLYCFFASLFSVLVRGSRAVLQLYPENSEQLELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDEVEPRESVFTNERFPLRMSRRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA . Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity . Involved in the pre-rRNA processing steps leading to small-subunit rRNA production inde... |
Q9CY21 | MASRSRRPEHSGPPELFYDQNEARKYVRNSRMIDIQTKMTERALELLCLPEGQPSYLLDIGCGSGLSGDYISEEGHYWVGIDISPAMLDAALDRDTEGDLLLGDMGQGVPFRPGSFDGCISISAVQWLCNANKKSDVPARRLYCFFSSLYSALVRGARAVLQLYPENSEQLELITTQATRAGFTGGVVVDFPNSAKAKKFYLCLFSGPSTSLPKGLTESQDADQASESMFTSERAPHKKARRDLVKKSREWVLEKKERRRRQGKEVRPDTQYTGRKRKPRF | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Involved in the pre-rRNA processing steps leading to small-subunit rRNA production indepe... |
Q10162 | MSRPEHIAPPEIFYNDVEAGKYSTNTRIQSIQTEMSERALELLDAEGPSFILDIGCGSGISTQIGESQGHVVVGMDISPSMLSVALESQEIEGDLLLCDMGTGVPFRPGTFDGVISISAIQWLLNADKTCNVPQRRLNRFFQTLYISMKRGGRAVMQYYPETEKSQQMIMDTARKAGFAGGIVVDHPESKRQKKYYLVLQAGGTRTLDISSMTLDQEGTNAKQRKLKKKQDMSTREYIIHKKELNRKRGRLHVPKDSKYSGRRRKAAF | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (By similarity).
Catalytic Activity: a guanosine in 18S rRNA + S-adenosyl-... |
P25627 | MSRPEELAPPEIFYNDSEAHKYTGSTRVQHIQAKMTLRALELLNLQPCSFILDIGCGSGLSGEILTQEGDHVWCGLDISPSMLATGLSRELEGDLMLQDMGTGIPFRAGSFDAAISISAIQWLCNADTSYNDPKQRLMRFFNTLYAALKKGGKFVAQFYPKNDDQVDDILQSAKVAGFSGGLVVDDPESKKNKKYYLVLSSGAPPQGEEQVNLDGVTMDEENVNLKKQLRQRLKGGKDKESAKSFILRKKELMKRRGRKVAKDSKFTGRKRRHRF | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of guanine 1575 (m7G1575) in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Important for biogenesis end export of the 40S ribosomal subunit independent... |
P51853 | MAMITGGELVVRTLIKAGVEHLFGLHGAHIDTIFQACLDHDVPIIDTRHEAAAGHAAEGYARAGAKLGVAGHGGRGIYQCGHAHCQRLAGSQGRCIPHPGSGALRDDETNTLQAGIDQVAMAAPITKWAHRVMATEHIPRLVMQAIRAALSAPRGPVLLDLPWDILMNQIDEDSVIIPDLVLSAHGARPDPADLDQALALLRKAERPVIVLGSEASRTARKTALSAFVAATGVPVFADYEGLSMLSGLPDAMRGGLVQNLYSFAKADAAPDLVLMLGARFGLNTGHGSGQLIPHSAQVIQVDPDACELGRLQGIALGIVA... | Cofactor: Binds 1 metal ion per subunit.
Function: Cleavage of benzoin-anisoin acyloin linkage.
Catalytic Activity: benzoin = 2 benzaldehyde
Sequence Mass (Da): 58957
Sequence Length: 563
EC: 4.1.2.38
|
Q501B2 | MASNEMEKSSKEKEPKTPPPSSTAPPSSQEPSSAVSAGMATPDWSGFQAYSPMPPPHGYVASSPQPHPYMWGVQHMMPPYGTPPHPYVAMYPPGGMYAHPSMPPGSYPYSPYAMPSPNGMTEVSGNTTGGTDGDAKQSEVKEKLPIKRSRGSLGSLNMITGKNNEPGKNSGASANGAYSKSGESASDGSSEGSDGNSQNDSGSGLDGKDAEAASENGGSANGPQNGSAGTPILPVSQTVPIMPMTAAGVPGPPTNLNIGMDYWGAPTSAGIPGMHGKVSTPVPGVVAPGSRDGGHSQPWLQDDRELKRQRRKQSNRESAR... | Function: Transcriptional activator that binds to the G-box motif (5'-CACGTG-3') and other cis-acting elements with 5'-ACGT-3' core, such as Hex, C-box and as-1 motifs. Possesses high binding affinity to G-box, much lower affinity to Hex and C-box, and little affinity to as-1 element . G-box and G-box-like motifs are c... |
O22208 | MAEPITKEQPPPPAPDPNSTYPPPSDFDSISIPPLDDHFSDQTPIGELMSDLGFPDGEFELTFDGMDDLYFPAENESFLIPINTSNQEQFGDFTPESESSGISGDCIVPKDADKTITTSGCINRESPRDSDDRCSGADHNLDLPTPLSSQGSGNCGSDVSEATNESSPKSRNVAVDQKVKVEEAATTTTSITKRKKEIDEDLTDESRNSKYRRSGEDADASAVTGEEDEKKRARLMRNRESAQLSRQRKKHYVEELEEKVRNMHSTITDLNGKISYFMAENATLRQQLGGNGMCPPHLPPPPMGMYPPMAPMPYPWMPCP... | Function: Transcriptional activator involved in salt and osmotic stress responses. Functions as a stress sensor and transducer in a signaling pathway that resembles an ER stress response. Following salt stress, BZIP17 is cleaved by SBT6.1 (S1P) and S2P at the C-terminus and the N-terminal bZIP component is translocated... |
Q50EK0 | MVWKEAVSVLQKAQELKEPPLMFTVFLASFIGLAFFFYLISNHRTKAWRGIPPGTFGWPLIGETLEFLGCQRKGNPRDFFDSRTQKYGNVFTTSLVGHPTVVFCSPEGNRFLFSNENKLVVNSWPSSVGNLFRSSLITTVGDDAKRLRRILMTFLRPEALREFVGRVDSMTKRHLAEHWIGKDEVTALPLLKRYTFSLACDLFASINNKDDLGRLWLHFMVFVKGVMQIPIDLPGTRYNKAKHAANAIRQQLGSIINERKIGLEAGNASPEQDLLSFLLSNVDEQGESLTDNEIQDNILLLLYAGHDTSSSTLTVLLKFL... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56458
Sequence Length: 497
Subcellular Location: Membrane
EC: 1.14.-.-
|
O42145 | MAGDLLQPCGMKPVRLGEAVVDLLIQRAHNGTERAQDNACGATATILLLLLCLLLAIRHHRPHKSHIPGPSFFFGLGPVVSYCRFIWSGIGTASNYYNSKYGDIVRVWINGEETLILSRSSAVYHVLRKSLYTSRFGSKLGLQCIGMHEQGIIFNSNVALWKKVRAFYAKALTGPGLQRTMEICTTSTNSHLDDLSQLTDAQGQLDILNLLRCIVVDVSNRLFLGVPLNEHDLLQKIHKYFDTWQTVLIKPDVYFRLDWLHRKHKRDAQELQDAITALIEQKKVQLAHAEKLDHLDFTAELIFAQSHGELSAENVRQCVL... | Function: Catalyzes the formation of aromatic C18 estrogens from C19 androgens.
Catalytic Activity: 3 O2 + 3 reduced [NADPH--hemoprotein reductase] + testosterone = 17beta-estradiol + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): ... |
Q1LX59 | MTLAHIFQTIWDFGTKDSVLQPIWDYVRLNHSETLRSPLFPVVLTVSSYFVLVLPYLSCDILGRKWPAIYRYKIQPDKLPTTAMLLHCSGVTLYNHILLVIPAAVAQWMWRPPIPLPEQAPTLLELVGGVTGNLLLFDLQYFIWHFLHHKIRWLYVTFHAIHHNYSAPFALATQCLGGWELVTVGFWTTLNPVLLRCHLLTTWMFMVVHVYVSVEDHCGYDFPWSTSRLIPFGVYGGPSKHDVHHQKPNTNFAPHFSHWDKMFGTHADFRFSKPRE | Function: May catalyze the formation of 25-hydroxycholesterol from cholesterol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32063
Sequence Length: 276
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.99.-
|
Q20027 | MLDLYPVQNLTVDQLEYEKNTRFLQPAWDWIKNGNEHILSSPLFPPFYALSIDYTWVAVFTFIDVFLCNVPFFKDAKIQKDRKVTWDLIKKSLKLQGWNQLLWIYPMALVQLIWVPDTELPILAPTVFEMLSQLAIFFLAFDFTYFWFHYINHKVKWLYRWCHSVHHMYSSPFAASAQHLHPFELFFVGTFITTIPWIFPTHCLTYWIWFFIAQSVSYEVHIGYDFPFALHRIFWFYSGAPAHDMHHLRPLTCFQPWFNYLDRLMGYHITYADLKKMTEAKFKKFGLYSAEDEKGLIKIN | Function: Probable sterol desaturase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36065
Sequence Length: 300
Subcellular Location: Membrane
EC: 1.14.99.-
|
Q567X1 | MWNISEVVFQLPTSSASDRVLQPLWDYLLLRHYTLISSPFFPVLLAFSSYIIFSVPFAVLDVLGEKAPLFKYKIQKDRRPTVGMMLRTLWTAVYNHLVFVLPAVLITNVVMPMPPLPTVAPTVWEMFSGGLGALLVFDTQYFLWHMVHHKNPHLYRWVHAIHHDYISPFSWSTQHLSGVELMTVGFWSNIDPILLKCHPLTVWTLTVYSIWMSVEDHIGYDLPFSPGHLVPFGLLGGAMAHDMHHQKPSSNFAPFFSHWDKIFGTAITVKLTQKSEKEKQVA | Function: May catalyze the formation of 25-hydroxycholesterol from cholesterol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32343
Sequence Length: 282
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.99.-
|
A8WGT1 | MLDISNTTWDLSNQSVLQPLWDYLQQNHESSLRSPLFPVILSVSMYLVLVFFYTVLDLLAPTWPSIRRYQIHQDRTVTWSNIGSTLALTTYNHLLYIFPAAVAQWLWRPPIPLPREAPTLTAFLLGIVGCTVVFDFQYYLWHLLHHRVGWLYRTFHALHHQYRQTFSLVTQYLSAWELFSVGFWTTVDPLLLQCHCLTAWAFMLFNIWVSTEDHCGYDFPWAMHRLVPFGLWGGALRHDAHHQLPGTNFAPFFAHWDWLGGTATMPAPVKTKKRDDKEA | Function: May catalyze the formation of 25-hydroxycholesterol from cholesterol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32605
Sequence Length: 279
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.99.-
|
Q4G0S4 | MQTSAMALLARILRAGLRPAPERGGLLGGGAPRRPQPAGARLPAGARAEDKGAGRPGSPPGGGRAEGPRSLAAMPGPRTLANLAEFFCRDGFSRIHEIQQKHTREYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWREYRDLRGRATGLISAEGEQWLKMRSVLRQRILKPKDVAIYSGEVNQVIADLIKRIYLLRSQAEDGETVTNVNDLFFKYSMEGVATILYESRLGCLENSIPQLTVEYIEALELMFSMFKTSMYAGAIPRWLRPFIPKPWREFCRSWDGLFKFSQIHVDNKLRDIQYQMDRGRR... | Function: A cytochrome P450 monooxygenase that catalyzes the 3,4 desaturation of all-trans-retinol (also called vitamin A1) to all-trans-3,4-didehydroretinol (also called vitamin A2) in the skin. Desaturates with lower efficiency all-trans retinal and all-trans retinoic acid. Forms minor amounts of 3-hydroxy and 4-hydr... |
P0DTX6 | MSGTGVLLLTLLLLVAMAASDMLSSLIQAHERDSEESCKSYGGGPCPSGEDCCCPPGRSTGTCKRTCNNGSVCA | Function: Probable neurotoxin.
PTM: May contain 4 disulfide bonds.
Sequence Mass (Da): 7543
Sequence Length: 74
Domain: The cysteine framework is C-C-CCC-C-C-C.
Subcellular Location: Secreted
|
Q9V419 | MVLITLTLVSLVVGLLYAVLVWNYDYWRKRGVPGPKPKLLCGNYPNMFTMKRHAIYDLDDIYRQYKNKYDAVGIFGSRSPQLLVINPALARRVFVSNFKNFHDNEIAKNIDEKTDFIFANNPFSLTGEKWKTRRADVTPGLTMGRIKTVYPVTNKVCQKLTEWVEKQLRLGSKDGIDAKHMSLCFTTEMVTDCVLGLGAESFSDKPTPIMSKINDLFNQPWTFVLFFILTSSFPSLSHLIKLRFVPVDVERFFVDLMGSAVETRRAQLAAGKQFERSDFLDYILQLGEKRNLDNRQLLAYSMTFLLDGFETTATVLAHIL... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57705
Sequence Length: 505
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
|
Q9VYT8 | MFGSLLLGIATLLGAIYAFLVSNFGHWRRRGVTEPRALPLFGSFPNMIWPRQHFTMDMRDIYMHYRNTHSYVGCYLLRAPKLLVLEPRLVYEIYVSAFSHFENNDASKMVDIAKDRLVALNPFVLEGEEWRHQRAVFSTLLTNGRIRTTHAIMQRVCLDLCQFIAIKSAGGKDLDCIDLGLRFTGESLFDCVLGIQARTFTDNPLPVVRQNHEMSAENRGLAIAGAVHGLFPNLPRWLRPKVFPRSHDRFYGQMISEALRLRRSKHQERNDFINHLLEMQRELDLSEEDMASHAMTFMFDGLDTTSNSIAHCLLLLGRNP... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57410
Sequence Length: 505
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
|
Q9VMT5 | MCPISTALFVIAAILALIYVFLTWNFSYWKKRGIPTAKSWPFVGSFPSVFTQKRNVVYDIDEIYEQYKNTDSIVGVFQTRIPQLMVTTPEYAHKIYVSDFRSFHDNEMAKFTDSKTDPILANNPFVLTGEAWKERRAEVTPGLSANRVKAAYPVSLRVCKKFVEYIRRQSLMAPAQGLNAKDLCLCYTTEVISDCVLGISAQSFTDNPTPMVGMTKRVFEQSFGFIFYTVVANLWPPITKFYSVSLFAKDVAAFFYDLMQKCIQVRRESPAAQQRDDFLNYMLQLQEKKGLNAAELTSHTMTFLTDGFETTAQVLTHTLL... | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57271
Sequence Length: 502
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.-.-
|
Q7NI47 | MTFGHCRRASTLRSAFVLGLCGLLLAGCSGADDDRDAAALKDKYVTVNLGVRGPVDLPADGVGNLQTFSPQQIYAGKKLFESNCQNCHVGGTTTPNPKVSLALAKLQGATPPRDNIQSLVQYMRLPMSYDGSEETFNCRKSDWIEDDEAQNLAAFILRASQKARGWGTARLEANQDSMTTAPP | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19725
Sequence Length: 183
Subcellular Location: Cell inner membrane
|
Q7NI46 | MFSRQFGRLATLALALAVAGCAGGEQSTTAEAPSEPAPVAKPDVVSAATGELSNFSTADLKQAKKLFQAECGRCHVGGQTYGTYNSTDVSLSYDALTNATPPRNTVAGLVDYMKKPTSYDGRTDLLKTGEHASFTGLGDEKLRLIAGHIIKEATSNPNWGQGKDTR | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17470
Sequence Length: 166
Subcellular Location: Cell inner membrane
|
Q76FB0 | MFVKMIGWLVLFLFAHQTWAIEVAKDTNGGILNIAPEQLKRGKRLFNSHCSSCHVGGITKTNPNIGLDLESLSLATPPRNNLDALVDYMKNPTTYDGSESIAQIHPSIASSDIFPKMRDLSEDDLYAIAAHILTQPQIQAEKWGGGKIYYTKRSM | Cofactor: Binds 1 heme c group covalently per subunit.
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Unlike Synechococcus vulcanus it does not bind by itself to PSII, but requires all extrinsic members of the OEC.
Location Topology: Peripheral membrane p... |
P24469 | MKWNPLIPFLLIAVLGIGLTFFLSVKGLDDSREIASGGESKSAEKKDANASPEEIYKANCIACHGENYEGVSGPSLKGVGDKKDVAEIKTKIEKGGNGMPSGLVPADKLDDMAEWVSKIK | Function: Not essential for growth on minimal or rich media.
PTM: Binds 1 heme c group covalently per subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12766
Sequence Length: 120
Subcellular Location: Cell membrane
|
P24037 | MKKTLMASAVGAVIAFGTHGAMAAAPADWSSVAATDVTLFYPGVSPVEWITKGTEHGGARALKKGETCAGCHSEEASDMGEKMASGKKLEPSPIAGKAPFINAKVQAANDGENLYLRFTWKQPAASGAAPMDADNPVKIAYMLEGGSKVELAEAGGCWGSCHGDARTMPGAADTKTKYVKDGSLANGVYYDLNQWRSGENKAFDGYVATERVMEGGQALVDAQGKLDGDTWTVVFTRKFAGGEGDVTLAPGNLYNFGFAIHDDSATGRYHHVSLGYSLGIDAQGDITAAKQ | Function: May play a role in nitrite reduction. Shows peroxidase activity on proteolytic modification.
PTM: Binds 2 heme c groups per subunit.
Sequence Mass (Da): 30426
Sequence Length: 291
Subcellular Location: Periplasm
|
Q54NY3 | MDLLLFIFFLILFYYSVKYYKADNQNSLSLSGPTPVPILGNIHQVGKDAHLTIPIISKKYHGIFRMWLGGTYYVVVSDYKLIREMYIENFENFKNRIATFKTMTGDDSRGIIGCNGDIWDSNKELIMKSYKKVLNKDMNDFILLKSKELFNFFEKNGIKNEEEEDDDDDGNKSIIINNTRFYFQSLTLTVMFKMIFNENKSFQLYSDSTEFKLIFKTILNLLNSLNVYNVIYDFLGIFQPILLKFTKILDKNSFLSKIATEKFNSRIKEIDFTSDDFKANDLLDSLIMTINEDENGLNEKQIENIKSICIDFLMAGTDTT... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58248
Sequence Length: 502
Subcellular Location: Membrane
EC: 1.14.-.-
|
Q3J2P2 | MRPIPALALTFSLVAMPALAQDARQIERMIEGRHGLMTLMAHELGKLGGMAKEETPYDAEVAGKAASNLSALASVISPELFPKGSAVGEAEDSEALPAIWEKPDDFAQKISGMEEAAAKMQAAAGTDLASLQGAMRDLGAACGSCHETYRQKD | Function: Monoheme c-type cytochrome, that is particularly expressed when cells generate energy via aerobic respiration.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 16073
Sequence Length: 153
Subcellular Location: Periplasm
|
P33325 | MQSSRPSDRQLAIVVSVAVGIVVAVITTATFWWVYDLTLGRAQREAAQTAGARWSPSDGIKVITSSPPVTPTDGRQNWMGTQAWNEGVQAGQAWIQQYPNTVNVQVLIGMSSAQIWTYMQQYVSGALGVGCQYCHNINNFASDEYPQKIAARNMLRLVRDVNAEFIVNLPNWQGNYVQCATCHNNAPNNLEGFGAQFINSVPPIKVTVDPLDANGMAILDPAQKPEAIREPVLLKDAILFYIYNYQVWKPFDPNDPESGRGSLALTYDGGRTQDQVTINQNVMNYQAWSLGVGCTFCHNSRNFVAYELNPAGDNVLNPLY... | Function: Serves as the immediate electron donor to the oxidized BChl2 (bacteriochlorophyll dimer) that is oxidized in the first step of light-induced charge separation. Can also oxidize low-potential substrates.
PTM: Binds 4 heme groups per subunit.
Sequence Mass (Da): 45594
Sequence Length: 414
Subcellular Location: ... |
Q57142 | MKIMIACGLVAAALFTLTSGQSLAADAPFEGRKKCSSCHKAQAQSWKDTAHAKAMESLKPNVKKEAKQKAKLDPAKDYTQDKDCVGCHVDGFGQKGGYTIESPKPMLTGVGCESCHGPGRNFRGDHRKSGQAFEKSGKKTPRKDLAKKGQDFHFEERCSACHLNYEGSPWKGAKAPYTPFTPEVDAKYTFKFDEMVKEVKAMHEHYKLEGVFEGEPKFKFHDEFQASAKPAKKGK | Function: Involved in ammonia oxidation; accepts electrons directly from hydroxylamine oxidoreductase (HAO).
PTM: Binds 4 heme groups per subunit.
Sequence Mass (Da): 25999
Sequence Length: 235
Subcellular Location: Periplasm
|
Q54LA8 | MIIIVIVVFLFYFSFLNLNLNPKKKRPPSPITLPVIGNLISLLNNQPQNILFNYYKKYGKIYQLQYGIVNTVVLSEFDILKEAFIENGEVFIERYNKITKKFKSSENIVNSNGLIWKKLQSISIQELSPNIKIKKYEPMIINETNKLIDSFNEHIKSNESIDPTLNIKICFLNIIISFLFNFRYNDYKDEKVIQLVDYIHSIFRMGSHPIPQDYIPILNKFYINKTTKIHQKIFENIYEYIENQVQKRLEILNKNNNNNNNNINECFVDLLLLKFKSNLLTWNEVIKTTTDLMIAGSDTNSLFTIHLIIALTNRENIQNK... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56886
Sequence Length: 484
Subcellular Location: Membrane
EC: 1.14.-.-
|
Q45234 | MKRTMIVVTTLLLGAGAVMAQQEVAVQQDNLMRSQARSLYTVILKMTKGDIPYDQKAADEAIANLETDVAKIAKTFEVNPKQDVVNATYGASPKVWKNKADFDSKIPPVQKAIAQVKGKITDVASLKAAYTAINDRCTDCHETYRLKLK | Function: Low-spin monoheme cytochrome.
PTM: Binds 1 heme c group covalently per subunit.
Sequence Mass (Da): 16402
Sequence Length: 149
Subcellular Location: Periplasm
|
P58051 | MIWWFIVGASFFFAFILIAKDTRTTKKNLPPGPPRLPIIGNLHQLGSKPQRSLFKLSEKYGSLMSLKFGNVSAVVASTPETVKDVLKTFDAECCSRPYMTYPARVTYNFNDLAFSPYSKYWREVRKMTVIELYTAKRVKSFQNVRQEEVASFVDFIKQHASLEKTVNMKQKLVKLSGSVICKVGFGISLEWSKLANTYEEVIQGTMEVVGRFAAADYFPIIGRIIDRITGLHSKCEKVFKEMDSFFDQSIKHHLEDTNIKDDIIGLLLKMEKGETGLGEFQLTRNHTKGILLNVLIAGVDTSGHTVTWVMTHLIKNPRVM... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56900
Sequence Length: 496
Subcellular Location: Membrane
EC: 1.14.-.-
|
A0A0N9HT29 | MEFLSFPLSSALLIILLFMLVKKAIQNKNSKLPPGPRKLPVIGSLHHLIGDGLPHHALRNLAKKHGPLMHLQLGENSTLVVSSSKMARAIMSTHDLMFANRTVQFATDILLYGGKGIGLAPYGDYWRQIRKICVLELLSAKRVQSFQTVREEEISNLIRSISAESSKVNFSEMITSLTNDIIARAAFGEKCKDKHAFLSLIEEGIQLAGGFDIAGLFPSLKLLHVITGKKRQLERVHNELDRILVDIIKENKEKRRASKLNEDKYEENLVDVLVRVQENTQLEVPLANDNLKAVILDIFVAGSETSSTTIEWAMSEMLKN... | Function: Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family . Catalyzes the conversion of deoxypodophyllotoxin to desmethyl-deoxypodophyllotoxin .
Catalytic Activity: (-)-deoxypodophyllotoxin + O2 + reduced [NADPH--hemoprotein reductase] = (-)-4... |
Q9LW27 | MSVFLCFLVLLPLILIFLNVLKPSKYKLPPGPKKLPIIGNLHQRRTLHPRNRRNLAEMYGPVALLQYGFVPVVAISSKEAAEEVLKINDLECCSRPEAAGMRATFYNFKDIGMAPFGDEWSLMRKLSVVELFSVKKLQSFKYIIEEENNLCVKKLSEFATRQSPVNLERAIFTLVGNIVCRIGYGINLYECDFFEADRVVDLVLKAEAVIRETVFSDFFPGRIGRFIDCISGQNRRLKNNFSVVDTFFQNVLNEHLKPGRESSTIVDLMIDMKKKQENDGDALKFTTDHLKGMISDIFVAGIGGVAGITLWGMTELIRNP... | Function: Multifunctional enzyme involved in the biosynthesis of the indole-derived phytoalexin camalexin. Catalyzes two reactions, the formation of dihydrocamalexate from indole-3-acetonitrile-cysteine conjugate and the oxidative decarboxylation of dihydrocamalexate which is the final step in camalexin biosynthesis. R... |
Q9LTM4 | MAISFLCVFLITFVSLIFFAKKIKRSKWNLPPSPPKFPVIGNLHQIGELPHRSLQHLAERYGPVMLLHFGFVPITVVSSREAAEEVLRTHDLDCCSRPKLVGTRLLSRDFKDIGFTPYGNEWKARRKFALRELFCLKKVQSFRHIREEECNFLVKQLSESAVDRSPVDLSKSLFWLTASILFRVALGQNFHESDFIDKEKIEELVFEAETALASFTCSDFFPVAGLGWLVDWFSGQHKRLNDVFYKLDALFQHVIDDHLNPGRSKEHEDIIDSMLDVIHKQGEDSSLELTIDHIKGFLANIFLAGIDTGAITMIWAVTEL... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57519
Sequence Length: 502
Subcellular Location: Membrane
EC: 1.14.-.-
|
Q9LTL8 | MSILLYFIALLSLIIIKKIKDSNRNLPPSPLKLPVIGNLYQLRGLFHKCLHDLSKKHGPVLLLRLGFLDMVVISSTEAAEEALKVHDLECCTRPITNVTSKLWRDGQDIGLAPYGESLRELRKLSFLKFFSTTKVRSFRYIREEENDLMVKKLKEAALKKSSVDLSQTLFGLVGSIIFRSAFGQRFDEGNHVNAEKIEDLMFEVQKLGALSNSDLFPGGLGWFVDFVSGHNKKLHKVFVEVDTLLNHIIDDHLKNSIEEITHDRPDIIDSLLDMIRKQEQGDSFKLTIDNLKGIIQDIYLAGVDTSAITMIWAMAELVKN... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56809
Sequence Length: 498
Subcellular Location: Membrane
EC: 1.14.-.-
|
Q9LTL0 | MDSIWILSLLFFIIFLLLAAFKRKNHGKHRRIPSPPGFPIIGNLHQLGELQHQSLWKLSKKYGPVMLLKLGKVPTLILSSSETAKQALRDYDLHCCSRPSLAGGRELSYNNLDMSSSPYNEYWKELRKLCSQELFSANKIQSIQPIKDEEVKKVIDSIAESSSLKNPVNLSKTFLALTTSVVCKAAFGVSFEGSVLNSDRFNKLVRDTFEMLGSFSASDFIPYVGWIIDKFNGLQGWRKKSFRDLDAFYEQIFDLHKEEKEVGSEDLVDVLLRLEKEEIVVGNGKLTRNHIKAILMNILLGGIDTSAITMTWAMAELAKN... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57080
Sequence Length: 500
Subcellular Location: Membrane
EC: 1.14.-.-
|
Q9LIP6 | MTNIWLLSLIFVICILVAVFNHKNRRNYQRTPPSPPGCPIIGNLHQLGELPHQSLWKLSKKYGPVMLLKLGRVPTVIVSSSETAKQALKIHDLHCCSRPGFAGARELSYNYLDIAFSPYDDYWKEVRKLAVQELFSSKQVHSIQPIKDEEVKKLIDSISESAAQKTPINLNKTLLALTVSVVCRTAFSVNFEGTVLNSERFNNIVREALEMLGSFSASDFIPYVGRIIDLLTGLQGRRERSMRDLDAFYEQMFDLHKQKKEEGSEDFVDLLLRLEKEEAVLGNDKLTRNHIKAILMDVLLAGMDTSAITMTWAMAELAKN... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57139
Sequence Length: 500
Subcellular Location: Membrane
EC: 1.14.-.-
|
O49396 | MDTSLFSLFVSILVFVFIALFKKSKKPKYVKAPAPSGAWPIIGHLHLLGGKEQLLYRTLGKMADHYGPAMSLRLGSSETFVGSSFEVAKDCFTVNDKALASLMTAAAKHMGYVFWLEMRKIAMIELLSNRRLQMLNNVRVSEISMGVKDLYSLWVKKGGSEPVMVDLKSWLEDMIANMIMRMVAGKRYFGGGGAESSEHTEEARQWRKGIAKFFHLVGIFTVSDAFPKLGWLDLQGHEKEMKQTRRELDVILERWIENHRQQRKVSGTKHNDSDFVDVMLSLAEQGKLSHLQYDANTCIKTTCLALILGGSETSPSTLTW... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57886
Sequence Length: 512
Subcellular Location: Membrane
EC: 1.14.-.-
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.