ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5NY30 | MPIDPARLAFTDDGTPCSAAFGDVYHARGGGLEQARFVFIAGNGLPARWQGREHFAILETGFGFGLNFLATWDAWRADPKRCERLHFVSVERHPFTREDLATLHARWPELAPLAAELADHWPTLTPGMHRLHLNRGRVVLTLLFGDARELLPRLECGADAFFLDGFSPACNPELWSAALLAELGRLAASGATLATWSVSGDVRRALAAAGFDCEKAPGFDGKRQMCRGRHRDVGTGPAPAAAAARHALVIGAGLAGSSTAERLAARGWHVDVIDAADGPGEGASGNLTGVLRPLPSLDDNRLARITRAGALYGLHHLRQLTEAGLPVRWDACGVLHLARDPVHEDKQRRVVEAHRPPSDYLRFVERDEASTLAGWPLPVGGWWFPQGAWVSPPSLCAANLMTHPDLIRCHFGRAMQRLEASADGWTAFDADGKAIASAPVAVLANGVGIRAVPQAAALPVRSARGQVTHFPAAAGSPPNVVVCRLGYVAPALDGVRSAGATFSVDDDEPALRDADQRENLAKLEFILPGYAAAVDTAALAGRVGFRPASPDRLPMVGEVPAVLRADRATPLAQIPRHPGLYAVAGFGARGLVWASLAAELLASHIAGEPLPLERELVDALDPARYLLRPARGMTREG | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 67972
Sequence Length: 637
Subcellular Location: Cytoplasm
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Q2KVJ9 | MSSAYQPLTPALTEVNEAGHLASRQYGDVYNSPADAYGQAVDVFLHGNDLPQRWRGRRHFTVCETGFGLGTNFLALWRAWREDPGRCGRLHMLSIEGHPLTREAYEAVLDTQVPEPLRAGARELLAQWPKLLPGLHRLEFEHGAVTLTLALGDIGQVAPRLSACVDAFFLDGFAPSKNPAMWDTYVLRRLLRLGAADATLATWTSAGFVRRGLQEAGFDIQRLTGARGKRHITVGRRSAWAGKHAPRRTDAPDAPVLVVGAGLAGAGMAQALALRGLSVRVIAESAQPHGGHLAAALTPLVARDDNARARLARAGSQRAWHRWQGLDAVRKVGALQLERDAGRSAALADTLAALHFPRDWVRWVESDEAEQLAGLPVARGGLYFADGLLVRPQPLIDALLAWPGIERVRGRVSRLVQCSAGQWQALDALGQVLGEARQVVLANAAGTPLVLEASGLLGPLPRVAQMHALAGEVSHVPAAALGGGPHCMIGGEGYVLPAVDGWCVVGSTYAPGVAQSEVSLAGQQRNLEKAAGLLGAPLDAVAGPLPGWAGWRAVMPGRLPVLGELPGVSGVWLASAYGSRGLSWSALAGDVIAARLCGEPLPLETDLLASVGPR | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 65006
Sequence Length: 614
Subcellular Location: Cytoplasm
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A9I518 | MSSYSPLVPPAAGFDADGRFRSVAYGDVYHSLSGALGQAEHVFLRGNGLPQRWRGRQAFTVCETGFGLGLNFLALWDAWRNDPARPRCLHMVSIEAHPFARDALRDWLRQLAPDILQGLAGQLADQWPACLPGLHRLEFEGGAVTLTLAFGAASALAPHLRARVDAYFLDGFAPDRNPELWQPALMRDLARMAAPDATLATWACAGSVRQALRDAGFRVRKQPGYGGKWHMTVGVRESAQPEAPADAWALARAADGEGQDEVVVVGGGLAGAGIAQALALRGRPVCVIDAAGPASAHAGHVAAALTPVIARDDNPRARLSRAGSQRALARWAGLRPGAAPRRCGTLQLERDAGRSAALAETLQQLQFPADWVRAVDRDEAAGLAGVPLARGGVFFADGLLVQPAALIPALLGMPGVRRVAGCAAVLRRVAHGWQVLDDAGQLLGQGATVVLANAFGAQALLRDSGLLDPLPRVAQMHALAGEITLLPGQGLGGGPRCIVGGEGYLLPPVDGWCVAGSTYEHGAATARVGPAGQQTNLGKAAGLLGGLPAAWAALAPGQLPGWAGWRAVLPGRLPAVGPLGHAPGVWLAAGYASRGLSWSALAGDLIAACLHGEPLPLPADLLAAVAPR | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 65133
Sequence Length: 628
Subcellular Location: Cytoplasm
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P25811 | MDTIAAISTPMGEGAIAIVRLSGPEAIQIADKIYKGPKGKTLSSVESHTIHYGHIVDRPSDRVVEEVMVSVLKAPRTFTREDVIEINCHGGIVTVNQVLQLALREGARLAEPGEFTKRAFLNGRIDLSQAEAVMDLIRAKTDRAMNVAMNQMEGRLSALVRRLRSEILETLAHVEVNIDYPEYDDVEEMTHQILVEKATAVKKEIETLLRTSEQGKILREGLSTVIIGRPNVGKSSLLNSLVHEAKAIVTDIPGTTRDVIEEYVNVRGVPLRLVDTAGIRETEDIVERIGVERSRQVLKEADLILLVLNYSEELSEEDVKLFEAVEGMDVIVILNKTDLEPKIDTERVRELANGRPVVTTSLLKEEGINDLEEAIQSLFYTGAIESGDLTYVSNTRHITILQQAKRAIEDALSGIEQDVPIDMVQIDLTRCWELLGEIIGDSVHESLIDQLFSQFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50974
Sequence Length: 459
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q89Z26 | MNQDTICAIATAQGGAIGSIRVSGPEAISITSRIFQPAKAGKLLSEQKPYTLTFGRIYNGEEVIDEVLVSLFRAPHSYTGEDSTEITCHGSSYILQQVMQLLIKNGCRMAQPGEYTQRAFLNGKMDLSQAEAVADLIASSSAATHRLAMSQMRGGFSKELTDLRSKLLNFTSMIELELDFSEEDVEFADRSALRKLADEIEQVISRLVHSFNVGNAIKNGVPVAIIGETNAGKSTLLNVLLNEDKAIVSDIHGTTRDVIEDTINIGGITFRFIDTAGIRETNDTIESLGIERTFQKLDQAEIVLWMVDSSDASSQIKQLSEKIIPRCEEKQLIVVFNKADLIEEMQKEELSALLKNFPKEYTKSIFISAKERRQTDELQKMLINAAHLPTVTQNDIIVTNVRHYEALSKALDAIHRVQDGLDSHISGDFLSQDIRECIFFISDIAGEVTNDMVLQNIFQHFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51612
Sequence Length: 465
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A1UQU6 | MDTIFAVSSGLLPSGVAVIRVSGPRVVDIVKTLCGCLPKARFMHHGDLIARDGSFLDSALTVFFPRPHSFTGEDCAEFHLHGGKAVVNRFLDELSTFTGCRLAEAGEFSRRAFIEGKIDLVQAEGLADLIEAETESQRRLAVMGANGHLTELYRHWRNKLMTARALIEAELDFSDEADVSNFSSDKVWQNMQELSDSLCEHIAEGERANILRDGIKVVIVGVPNSGKSSIINRLAGRPVAIVTEEEGTTRDALEVRLILGGLPVLVMDTAGFRETESKIEQLGIDIAKQHVLDADLVILVDDMKNPQKISLPNTSAEIWRVGNKLDICEGDKTRWPIQFSALNGLNFDYFLKEIESFCLHRIAEIGNIFPARKRQIQLLKEAVKEIDSSINYTFLDLSLRAEHLRRASDALGRITGDIDVEDLLDIIFSQFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48261
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q6MGL5 | MGPMIRGDRDKDTICAISTPHGVGGISVIRVSGPQTLNIVSKICQFLPAHPESHKVYFGNLKNSQTGDEIDEVLATYFKEGRSFTGEEVIEISCHGSPLICQTILNQLVNLGARPADRGEFTFRAFMNGKLDLVQAESVLSLIESQSQQAAKLALRQLKGTLSHKLEEIEDDMTWILAHAEASIDFSTEGIEVIEENVIQVRLKKIEAGLKELVATFKVGRLLKDGFRIVLTGLPNVGKSSLLNLFLEDERAIVTDIPGTTRDVIHGDTTFEGVKFTFVDTAGLRDEATDLVERIGIQKSYEAQNESDVVFFVYDIEKGLGAEELQILESLDPAKTYILANKTDKIGGSKPLETVEKTLKNSKFFQKLADPAAFFTRRVFFVSALDKKVRSEVLKDLVKEFADLQVENTVLISNARHFENLTRALENTQRSQSVVAQGLGAEFLALEFKEALIAIHETLGKRFDDQIMDRVFKEFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 53216
Sequence Length: 479
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q7VQV3 | MKNNEIDTIAAISTPIGRGGIGIIRVSGKLVPEVAMKLFNKIPKPRTAEYLTCIDHNGSIMEKVITLFFPEPHSFTGENILEIHGHGGQMILDLLLDRILNISSRIRLANPGEFTERAFLNEKIDLIQAESIADIINATSYQAAKSACNSLQGHFSNQIRIILNKITNFRTYIESTLDFSDQEISDISYQHIYNTLQNIIDNTNQICKLTHSGVLLRDGIKVVIAGKPNAGKSSLFNSLINKDRAIISNISGTTRDILHEYIQLNGIAFHIIDTAGFKKNSTNEIELIGMQKSKYELSKADHILWVIDSTDYSHNNSYNNIINSLKKELSSNNIEAVFITIIRNKSDLSFEHNGIDTTNKYACITLSALLNHGIDLLKKHLYDSAMLQIHKNSNFSSVEENQGNFIARKRHLKILQKVFQYLLSAKTQLQYNMTVNDCFAEDLKKAHEELAQIFGKLTPDDLLEEIFRAFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 53355
Sequence Length: 474
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q494C0 | MNYTIDTVVAISTPPGRGGIGIIRISGKSVPEIAPKLLGKIPNPRKAEYLPFLDTDGSILERVIALFFPEPNSFTGENILEIHGHGGQIILDILLERILKTSSDIRIAHPGEFTKRAFLNNKIDLVQAEAIADIIDATSYQAAKSASNSLQGIFSRKIYIILEQLTNLRMYAESSIDFSEDEISIIPYEDIKKKLRNIISDVQKMYKSTYHGVLLREGIKIVIAGKPNAGKSSLFNALVGIDRAIISTISGTTRDTLHEYIQLNGIAFHITDTAGLQKKSDNEIEQIGMKRTWEELSNADHILWVIDPNDVTNKENDITLKHVEKVLFCKNKKTPITIIHNKSDLTKNQIGISIINNYTIITLSALFNDGTDLLQEYLSNNIKSKIQQDCKSNLSENQGNFIARRRHLNALEKSSKYLFSAQTQLLSTMSINELFAEDLGLAHKELSKIFGKFTPDDLLKRIFSTFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52560
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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P53364 | MSKFFERDDDIVALATPFLSSALCVIRSSGASSISKFSKIFSNHSALNSASGNTIHYGYILDSENGCKVDEVVVCLYRAPKSFTGQDAIEVMAHGSVIGIKKIIDLFLKSGFRMAEPGEFTLRAFLAKKIDLTKAEAIHEIIFAKTNKTYSLAVNKLSGALFVKIDAIKKSILNFLSAVSVYLDYEVDDHEISIPFDLILSSKAELKKLINSYKVYEKIDNGVALVLAGSVNAGKSSLFNLFLKKDRSIVSSYPGTTRDYIEASFELDGILFNLFDTAGLRDADNFVERLGIEKSNSLIKEASLVIYVIDVSSNLTKDDFLFIDSNKSNSKILFVLNKIDLKINKSTEEFVRSKVLNSSNLIMISTKNLEGIDILYDKIRALISYERVEIGLDDIIISSNRQMQLLEKAYALILDLLSKIDRQVSYDMLAFDAYEIINCLGEITGEVSSEDVLDNMFKNFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51606
Sequence Length: 464
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q7VJY2 | MKNTLSSMILDDSTIVAIATPIGVGAISIVRLSGEKAYHIALALTHKESLKPRYAHLCHIYDAQQMPIDEALVLYFPKPYSYTTQDVCEVQCHGGIVSARAIVQLCLKLGARMAQAGEFAKRAFLGGRLDLAQVQAVAGLIQSQSLEANKILMRQLKGDLGTFVNRTRENLLEILAFSEVHIDYSEEVEESYIRDIQQKLAYVENELSHIYHISLTRQSIIEGYTLSIIGKPNVGKSSLLNALLRYERAIVSEIEGTTRDTIEEMLTIKGSLLRIVDTAGIRESDDKIEQIGILKTKEALMRSNIIVAIFDGSRPFDAEDKAIMEILKTQCQNKYILVIINKSDLPLQCEEELLHNLLRLHNKALLCMPLHLSTKYEGVQKVLECLEEVVSTHNGDESMILTSSYQLDCIKKALECIVKAHNVLDIGQLELFSYQIQDCIESICKITHPYENAELLDRLFATFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52356
Sequence Length: 467
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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B0TAB6 | MVGDTIAAVATPPGEGGIGIVRVSGPGARDVLKAVFRPRYGRGVDDWASHTLHLGTIIHPDDHRVIDEALVAWMVAPRTFTTEDVVEFHCHGGSVPVRETLGAVLRAGARLAEPGEFTRRAFLGGRLDLAQAEAIIEVIRAKTRDGLGAAVSQLEGQLSRRIRKVRDDLLALLAHLEAMIDFPEEDLPDIGSERICTDLMQIQRQIGDMLERSRTGRVLREGWRTVIVGRPNVGKSSLMNALLDEQRAIVTEIPGTTRDAIEEYIDLGGIPLRIVDTAGIRETEDVVERIGVEKTREYLEKADLALVVLDGSDSLTAEDETLLLSLAGRPAVVLVNKSDLAVRRLDEKRLRSLVGEMPIISVSAKEGWGLKELTELIRRMVYGDDGLGYAPDGGRLALVTQARHREALERSYAHLRQALDAVAHGASPDFLTIDLKAAWEALGEITGDTVGEDILDKIFSSFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50851
Sequence Length: 466
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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O25991 | MKNTSSSTTLTMNDTIAAIATPLGKGAISIIKISGHNALNILKQLTQKQDFTPRYAYVHDIFSNGVLLDKALVIYFKAPYSFTGEDVCEIQCHGSPLLAQNILQACLNLGARLAKAGEFSKKAFLNHKMDLSEIEASVQLILCEDESVLNALARQLKGELKIFIEEARGNLLKLLASSEVLIDYSEEDIPSDFLDGVSLNLEKQIASFKDLLDFSNAQKQRNKGHALSIVGKPNAGKSSLLNAMLLEERALVSDIKGTTRDTIEEVIELKGHKVRLIDTAGIRESADKIERLGIEKSLKSLENCDIILGVFDLSKPLEKEDFNLIDTLNRAKKPCIVVLNKNDLAPKLELEILKSYLKIPYTLLETNTLNSKACLKDLSQKISAFFPKLDTQNKLLLTSLAQKIALENAITELQNAKNHLETLELFSYHILSAIENLNLLTRPYETSQMLDSMFSEFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51170
Sequence Length: 461
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q28VZ6 | MQTIFAQATARGKAGVAIIRISGPDAFEVGRCLLGSLPDAGRFALRDVRTPLGELLDRGLVLVFKAPASFTGEDTVELQLHGSVAVVRAVEGAIRSTGLARLADAGEFTQRALLNDMLDLTQVEGLGRLIDSETEAQRKVAQASFEGGLSDKAERWRHLMIRAAALLEASIDFVDEDVPVDVVPEVQSILMGLDTDLAKEVTGAVVAERLHDGFEVAILGAPNAGKSTLLNVLADREIAITSDVPGTTRDVIEARLDVSGLPVTFLDTAGIRDTVDVIEKIGVQRAIDRALAADVRILLEIDDWILPDVLSDTIDFRYRAKADLSDGEGISGRTGVGIDRLLTDIEGVLSEKMSAVRSAVTDRQRGGIEAARVSLDAGVTVLSGTAELELAAEHIRHAQRSLDSVIGRVDVENLLGEIFSRFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 45517
Sequence Length: 426
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A8Z5X0 | MLKNDDTIVAIATPSGYGAIAVIRISGNNSIKIIKKIFCSFSKNQIETNYIHLGYIKYKKQIIDKVLIFLFKKPKSYTGEDIVEISCHGSIYIQNKLLSIIIDQGARLANPGEFTLRAFLNGKIDLCQAESILDIVNSETFFSHKFAINQMRGNISLLIRKLSKEIINLLSLIEFELDFSEENCNFINYLEFKKMLYNIIKKLKTLIRSFKIGNALKNGISVSIIGCPNVGKSTLFNKLLKYERSIVSNIAGTTRNYIEDSLIINGIKFRFIDTAGINNNTKDYIEKLGIKKTYSKINKSDLILYVFDDLNEKFILKKVKSLQEKYPKKKIFIIINKYDLIKKKIKEFNYKKIFKISAKYGYGVNNLLSEITFFSKKITSLKENTIVITQTRHYESFKKAIFYLYKVKKNLYSISPEFLSIDIRTALDYLGKVTGEVTNEDILSNIFSKFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52174
Sequence Length: 454
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q1IHC2 | MNLDDTIVAIATPPGRGGIGVVRLAGPEARTVALLMLRLANGKAELEAQRAHFAELVDPESGERLDEVVVAYFAKPHSYTTDDIVEISCHGSPVLLARVVELALAKGVRMADPGEFTMRAFLNGRIDLTQAEAVRDLIESQTLYQARVAAQQLGGSVSRRLQPTKQKLVNLIAVLEAGIDFADDDVSVLPAKEAIARIAEVHEPLAKLKEGFAFGKVVHEGLTLAIVGRPNVGKSSLFNRLVERDRAIVTAIPGTTRDLVTETVSLGGIPVHLVDTAGIRESHDEAESIGIQKSREAMADADLVLVVVDAHAETGHELDHQLISAAAERSAILVENKIDLGRHSVANGKSIPVVRTSAVSGEGIAELREQILRMVSGESGREESGFLTNIRQHQLVTDSLAALEAATNALEVRVPHEMVLMDLYNALRPLDDITGATTADDILNLIFSTFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48692
Sequence Length: 454
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q9ZCI1 | METIFAQSSAFGKAGVAVFRISGPKSLEVLQLLTGRKDFKPRLMYYQQIIVPETNELIDNAMVVYFKLPNSFTGEDVVEIHTHGSKAISIMLINTLLNIADIRLAEAGEFTKRAFLNNKFDLTAAEGIADLINAETIMQHRQAVRQANGGLKELYNKWRNQLLKIISLLEAYIDFPDEDIPESILNDVNNTHKNIVNEISNYLNDNRRGELLNNGLKLAIIGPPNTGKSSLLNFLMQRNIAIVSNIAGTTRDIIEGHLDIGGYPIILQDTAGIRTESTDIIEQEGIKRAINSAKTANIKIVMFDAEKLDSSINNDITGLIDENTIVIINKIDLIEPNKTFAIENRYKCLRVSVKNNIALSNILKNIENIAENLAGVTETPYITNQRHRHYLKQALSHLIDFNLDNDLVLATEDIRMTVRCIGLITGVINVEEILNEIFKNFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49813
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q16CZ5 | MDTVFALGSAQGRAGVSVIRLSGPAAWAVAETICGSLPDPRKSAVRVLRAQDGSVIDQALVLAFKAPHSFTGEDVVEFHVHGSIAVVRTVLDALSDQDVARLAEAGEFTRRALENGKLDLSQVEGLADLIDAETEAQRRQAVRVLTGALGEKVEVWRSKLIRAAALIEATIDFADEDVPVDVTPEVTSLLEDVSSDVRTEVAGTHVAERIRSGFEIALVGAPNAGKSTLLNKLAGRDAAITSEIAGTTRDVIEVRMDLGGLPVTFLDTAGLRQSADEIETIGIERAIKRAQEADLRVFLSGPDERLLIEPLEDDIRLTPKVDLAPGSQTGISGKTGQGIPELLEKIRSVFSERVSAVGLATHERHRLAMQRALEDLDNSFEALLRGPEFYDITAQELRSAIRALETLVGRIDAENLLDEIFSSFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 46025
Sequence Length: 428
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q8CPM6 | MGVILLNSNNNNHEQQRSLDEINNTINFNHNDSASQKFLAFLGPGLLVAVGYMDPGNWITSMQGGAQYGYTLLFIILISSLSAMLLQSMTVRLGIATGMDLAQMTRHFLNKPVAIMFWIIAELAIIATDIAEVIGSAIALDLIFGIPLIVGALITVFDVFLLLFIMKFGFRKIEAIVGTLIFTVLAIFVFEVYISSPHIIDMLNGFVPHKEIITNQGILYIALGIIGATIMPHNLYLHSSIVQSRKYDRHSIHEKAQAIKYATIDSNIQLSIAFVVNCLLLTLGAALFFGTKTEDLGGFYDLYLALKTEPALGATLGGIMSTLFAVALLASGQNSTITGTLAGQIVMEGFLKLSIPNWLRRLITRSLAVIPVIICLIVFKGNTEKIEQLLVFSQVFLSIALPFSLIPLQLATSNQNLMGPFKNKTWINIISWLLIIVLSGLNVYLIIQTFQEL | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49783
Sequence Length: 453
Subcellular Location: Cell membrane
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Q4L5B9 | MGVIDNKEQRSLDEINSTIEFNDSQRTSQKFLAFLGPGLLVAVGYMDPGNWITSMQGGAQFGYTLLFVILISSLSAMLLQSMTVRLGIATDKDLAQMTRHYLNKPTAIIFWVIAELAIIATDIAEVIGSAIALDLLFNIPLIIGALITVFDVFLLLFIMKFGFRKIEAIVGTLIFTVLMIFVFEVYISSPNLIEILNGFVPHYQIIANHSILYIALGIIGATIMPHNLYLHSSIVQSRKYNRHSFTEKAQAIKFATIDSNIQLSIAFIVNCLLLVLGAALFYGVNSNNIGGFYDLYQALRTQPVLGVVMGSIMSTLFAIALLASGQNSTITGTLAGQIVMEGFLKLSIPNWMRRLVTRSLAVIPVLLCLVIFRGNESKMEQLLVFSQVFLSIALPFSLIPLQLATSNEKLMGPFKNKKWVNICAWGLIIILSFLNIYLIIETFKEL | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49423
Sequence Length: 446
Subcellular Location: Cell membrane
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P54512 | MTTPSMEDYIEQIYMLIEEKGYARVSDIAEALAVHPSSVTKMVQKLDKDEYLIYEKYRGLVLTSKGKKIGKRLVYRHELLEQFLRIIGVDEEKIYNDVEGIEHHLSWNSIDRIGDLVQYFEEDDARKKDLKSIQKKTEHHNQ | Function: Central regulator of manganese homeostasis that regulates the expression of both manganese uptake and efflux systems . In the presence of high levels of manganese, it mediates repression of the manganese uptake systems MntH and MntABCD and activation of the efflux systems MneP and MneS. Binds with high affinity to the regulatory regions of its target genes . The manganese concentration required for activation of efflux is higher than that for repression of uptake .
Sequence Mass (Da): 16759
Sequence Length: 142
Domain: Contains an N-terminal DNA-binding domain and a C-terminal dimerization domain . Contains two metal binding sites per subunit, site A (corresponding to metal ion 2) and site C (corresponding to metal ion 1), which both contribute to the metal selectivity of MntR. A large metal cation is needed at the A site to correctly orient and position the C site ligands. Smaller, non-cognate metal cations bind at the A site, but disrupt the C site, blocking the full activation of MntR. Binding at the C site also favors Mn(2+) and Cd(2+) over other metals .
Subcellular Location: Cytoplasm
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Q8X7U4 | MSRRAGTPTAKKVTQLVNEEEHVEGFRQVREAHRRELIDDYVELISDLIREVGEARQVDMAARLGVSQPTVAKMLKRLATMGLIEMIPWRGVFLTAEGEKLAQESRERHQIVENFLLVLGVSPEIARRDAEGMEHHVSEETLDAFRLFTQKHGAK | Function: In the presence of manganese, represses expression of mntH and mntS. Up-regulates expression of mntP (By similarity).
Sequence Mass (Da): 17670
Sequence Length: 155
Domain: It contains an N-terminal DNA-binding domain and a metal-binding domain.
Subcellular Location: Cytoplasm
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A0R443 | MTVTALGLPTVARSTGDGSAGASPAPADGPLVDTYGRAATDLRVSLTDRCNLRCTYCMPAEGLNWLPGDALLSPTELARLLRIAVARLGITSVRFTGGEPLVVRHLEEVVAAAAALEPRPEITLTTNGLGLARRAEGLKKAGLNRINVSLDSVDAAHFARITRRDRLPDVLAGLAAAKAAGLEPVKVNAVLDPVSGLDDAVELLRYCLQHGYQLRIIEQMPLDASHSWQRDNVIDADRILQTLQQHFELTPDSRPRGSAPAELWQVAEGPTHAAGTVGVIASVSHAFCSACDRTRLTADGQIRSCLFSREETDLRHLLRGGADDAEIEAAWRAAMWSKPAGHGINDPDFVQPVRPMSAIGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 38499
Sequence Length: 361
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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A0PKZ7 | MTVTALGVPTVRGRSEGSAVASDAPGDGPLLDRFGRSATDLRVSLTDRCNLRCGYCMPAEGLNWLPGEQLLGPAELARLPRIAVTPLGITSVRFTGGEPLLARHLEEVVAAAAQLRPRPEISLTTNGVGLAKRAAALAEAGLDRVNVSLDTVDRAHFAAVTRRDRLTDVLDGLAGARAAGLTPVKVNAVLDPETGRQDVVELLRFCLEQGYQLRVIEQMPLDAGHQWRRNALLGSDDVLAALQPHFRLRPDPAPRGSAPAELWLVDAGPDTPAGKFGVIASVSHAFCSTCDRTRLTADGQVRSCLFSTEETDLRGLLRAGAGDEAIEAAWRGAMWAKPAGHGINNPDFLQPQRPMSAIGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 38245
Sequence Length: 360
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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A6Q5D0 | MLIDGHGRKVDYLRISLTERCNFRCQYCMPEKPFSWVPKENLLNFEDLFKFVKAAIDEGITKIRLTGGEPTLRADLDKFIKMIYDYKPDIDLAMTTNGYLLKDIAQDLKKAGLKRLNISLDSLKPEVAAKIASKDVLKNVLEGIDAALEAGLKVKINMVPLKGVNEDEIVDVMEYCKDRGMQIRFIEYMENVHAHSDLVGMHGKEILDKIKQKYEIEKIGRQGSSPAFLYKLKEDGYIFGLIDPHKHDFCETCNRIRLTAEGYLIPCLYFDEAMSIKEAVQAGDIDRAVEILKTVLANKPKENRWSEDANEASNRAFYETGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 36684
Sequence Length: 322
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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Q44118 | MPAARPAGAGVGLVDRYGRRATDMRLSLTDKCNLRCTYCMPAEGLEWLSKQAVMSASEIVRIVGIGVGRLGVRELRLTGGEPLVRHDLVDIIAELRRNHPELPISMTTNGVGLAKKVAPLKAAGLTRINVSLDSLHEETFTKLTRRPFLDQVLAGVDAAWAAGLGPVKLNAVLMRGINDAEAPSLLAWAVERGYELRFIEQMPLDADHGWTRRNMITAAEIRDLLSTDFVLTPDPRARDGAPAERFEVRRRVAGSGAGLGPVLGTVGIIASVTEPFCSDCRRTRITAEGRIMSCLFSREEFDLLVLLRSGASDDDLARRWQDAMWLKPKAHGMDHVGLDAPDFVQPDRSMSAIGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 38712
Sequence Length: 355
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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A1B4A2 | MPAHAYLCAMDAHAPLIDPFARPITYLRVSVTDRCDFRCTYCMAEHMQFLPKRDLLTLEELDRLCSAFVGLGVRKLRVTGGEPLVRRNIMEFFRAMSRHLGAGLDELTLTTNGSQLARFATELADCGVRRVNVSLDTLDEDRFARITRWGRLPQVLQGIEAAKAAGMRVKINTVALKGFNEDELFRLVGWCADQGHDLTFIEVMPMGEMGEEERLDQYWALSDLRDRLGERFTLTPLAERTGGPARYVRLDETGQKIGFITPLTHNFCESCNRVRITCTGELFMCLGQEDRADLRAPLRAGAEDAPLRAAIRDAIARKPKGHDFDYSRRHVAGQVSRYMSHTGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 38771
Sequence Length: 344
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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Q7U3H2 | MTPASALVDQRSRPLRVLRLSLTARCNLACPYCCPDLEDPPDLLSLEQQLRLIRVACRLGIHSLRLTGGEPLLSARLLPLLQAIAAARATPGDPLQGLQQVALTTNGTLLSDQRACDLRQAGLDRITVSLDGVDGAVVARMAGRPTATAGDSLARKVLGGLASARSAGFDPLAGELKLNAVIQRGVNEDQLLPLADLARDQGVELRLIEYMDVGNRNQWRLDQVLSAAEMVTRIRARWPLQAVGRPTGGTAQRWRYVDGGGHLGVIASISEPFCGDCNRLRVTADGQAFRCLFASVGTDLKPALHCEAELLRLVADLWRRRDDRYSDERQQTTGSMPHAEMAYLGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 37484
Sequence Length: 346
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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A5CYZ0 | MQDTYQREINYLRISVTDRCNLRCVYCMPEEGVRSLPHGEILRLEEIETVVRAAALTGVKKIRLTGGEPLVRKGLEELVRRVSGIPGIDDIALTTNGLLLPSRAKALKEAGVKRVNVSLDTLRADRYAEITRGGNLAGAWEGIQSALDAGLHPVKLNTVIIRGFNEDEVVAMAMLTINRPLHVRFIELMPIGSSSSWAAGRYVPAAEVMDAISAKLGPLVPARQPAGGGPAKYYRLKDAAGTVGFITSMSEHFCHRCNRLRLTASGGLRPCLYDGREIDLKAPLREGAGTREIAALIMEAIALKPDRHHMLEGWRDRRQMSQIGG | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 35623
Sequence Length: 325
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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Q3ADX7 | MELTHFNEEGRARMVEVTEKQETVRTAVAAGEITMRPETLELILDKKVAKGDVLAVAQVAGIMAAKKTGDLIPMCHPLNLTGVDISFTIKVPDTIEAKAKVTCVGKTGVEMEALTAVSVTLLTIYDMVKAVEKGMVIKNIRLLEKTGGKSGDYRREE | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17060
Sequence Length: 157
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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B0T229 | MTRLTHIDDQGRARMVDVSDKAETVREAIAVGFVRMTPETLALAITGAGRKGDVRAVAEIAGVMAAKKTADLIPLCHPLALSKVEVSVEVAEGGLAVMARVKLKGQTGVEMEALTAVSVACLTIYDMLKAAEKGMVIETVRLVEKTGGKSGAWRAE | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16447
Sequence Length: 156
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q9AC52 | MSKLTHIDDQGRARMVDVSEKPATAREAVAAGFVRMSAETLALAISGSGRKGDVRAVAELAGVMAAKKTSDLIPLCHPLALSKVEVAVEPADGGLSVTARVKTTGPTGVEMEALTAASVACLTIYDMLKAAEKGMVIEAVRLLEKTGGKSGDWKADQP | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16362
Sequence Length: 158
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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B3PDN1 | MSDSLTHIDASGQASMVDVSTKAVTVREAWAQACVRMQPDTLLQVKYNQLQKGDVLAVARIAGIQAAKKCADLIPLCHPLALSKVSVDFELDETNSTVLITSYCKLSGQTGVEMEALTAASVAALTIYDMCKAVDMGMVIEQVCLLEKSGGRRGHYRRGDTVS | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17495
Sequence Length: 163
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q9ZFA6 | MSGLTHFDESGRAHMVDVSEKPVTARVAVARGAVKMSAETLALVTEGRAEKGDVLGVARLAGIMGAKRTADLIPLCHPLPITKVALELTADPALPGVVVEATVKTGGQTGVEMEALTAVSVACLTIYDMVKAVEKGMEITGIRLLLKEGGKSGRFEASA | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16453
Sequence Length: 159
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q4L8D8 | MSKFTHINEQGNAKMVDVSNKNITKRTAQAHSSITVNETIYQQIIDNTNKKGNVLNTAQIAGIMAAKNTSTIIPMCHPLPLTGIDVQFNWQINDNTTYTLNITAIVSTTGKTGVEMEALTAASATALTVYDMTKAVDKGMIIGETYLESKSGGKSGDYRR | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17333
Sequence Length: 160
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q82H75 | MTVPSRGETPGPPAQDRLTHIDEAGAARMVDVSGKDVTARTARASGRVLVSPRVVELLRGEGVPKGDALATARIAGIMGAKRTPDLIPLCHPLSVSGVKLDLSVADDAVEILATVKTTDRTGVEMEALTAVSVAALTVIDMVKAVDKGAVITDVRVEEKTGGKSGDWSRS | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17620
Sequence Length: 170
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q9RKA8 | MSTQDRPSGSGQDPQDRLTHIDEAGAARMVDVSGKDVTARTARASGRVLVAPRVVELLRGEGVPKGDALATARIAGIMGAKRTPDLIPLCHPLSVSGVKLDLSVADDAVEITATVRTTDRTGVEMEALTAVSVAALTVVDMVKAVDKGAVITDVRVEQKTGGKSGDWTRS | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17685
Sequence Length: 170
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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B1VTN7 | MTGAPSARRSELSTQNRLTHIDETGAARMVDVSQKDVTTRLARASGRVLVSPRVIELLRGEGVPKGDALATARIAGIMGAKRTPDLIPLCHPLAVSGVEVELGVADDAVEITATVKTTDRTGVEMEALTAVSVAALTVIDMVKAVDKSAVITDVRVEAKSGGKSGDYRRTAPEGPDA | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 18442
Sequence Length: 177
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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A4VIR7 | MLTHLDSLGRASMVDVTDKAVTAREAVAEARVRMLPQTLQLIQQGGHPKGDVFAVARIAGIQAAKKTHELIPLCHPLLLTSIKVELQADGEDSVLIRAVCKLAGQTGVEMEALTAASVAALTIYDMCKAVDRGMVIEGVRLLEKLGGKSGHWQVQA | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16632
Sequence Length: 156
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q4JAB2 | MIDISGKDIVLREAIAEGFIKLKKDTIEKITKREIEKGDVIATAKVAGILAAKKTHELLPMCHPIPLEYINVEIEIENDGLKVVSTVRAHYRTGVEMEALTATSIALLTIWDMVKKYEKDEEGQYPLTEISKIRVVSKIKSYG | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16040
Sequence Length: 143
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q975D5 | MTEAKIVDISSKDIVLREAVVEGYIKLRKETIEKIKNKEVEKGDVITVAKTAGILAAKKTPELIPMCHPIPLEFVDVEIKIEEEGLRVISTVKAHYKTGVEMEALTATSVALLTIWDMVKKYEKDENGQYPYTEIKSIRVINKIKTYDDMK | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17125
Sequence Length: 151
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q3AVP2 | MQSDRNLSHLNSKGDVHMVDVGDRPSTFREAHAQGSIQMDRETFDLILRGETPKGDVLAVARIAAIQAAKRTWELIPLCHPISLSGMDVDIQPAEHLPGLRLNCRCRTTGPTGVEMEAMVAVSVGLLTLYDMLKAVDPAMTIGSIQLIHKSGGRNGVWNR | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17466
Sequence Length: 160
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q9HKV1 | MINISEKAISARTATATGRIHLRRSTIQAIREKKVKKGDVLEVSRVVGTQHAKNTFLQIPYCHNIPIEGVDVDFNVGEDYVEVSCTLTTTYKTGIEMEAISCVSGALINIWDMVKYLEKDESGNYPETRIDGIHVVEKRKTPV | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 15994
Sequence Length: 143
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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B9L0K8 | MAELTHLDERGQARMVDVAEKPETHRVAVARGRVSLRPETLQLVREGRAAKGDVLAVARVAGIMAAKRTAELIPLCHPLPLTKVEVDVRTNEQDTCLEIEARVETVSRTGVEMEALTAVAVAALTVYDMLKAVDRGMTIDRIQLIEKAGGRSGTWRREDDEARHAR | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 18301
Sequence Length: 166
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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Q977Y1 | MIDFDGNMINISRKDVVARKATAVGRIYLRKETITAIKNNQVKKGNVIEISRAVGTMYAKNTFLQIPYCHNIPIEGVDVDFSLGENYVEVTCSTTTSYKTGIEMEAINCVNGALLNIWDMVKYLEKDETGNYPETRIEGVHVIKKTKSQE | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16884
Sequence Length: 150
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.6.1.17
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A9IFD9 | MIDKTDITGLILAGGRGSRMGGIDKGLQNYQGMPMAMHALLRLAPQVGQAMVNANRNLGAYEAMGVPVWPDNLPDFAGPLAGLAVGLERCETPYLATVPCDCPRFPLDLVERLAGELARQDADIAMAATLQNGQLRTQPVFCLMKTSLLPSLLAFLQSGQRKIDAWTAMHRCVEVRFDDAAAFAGANTLAELQQLP | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21065
Sequence Length: 196
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q7VY88 | MIDKNDITGLILAGGRASRMGSVDKGLQNFHGMPLAMHTLLRLGPQVGDIMINANRNLAAYEAMGAPVWPDALPDFPGPLAGFAAGLERCETPYMVTAPCDTPNFPADMVSRLADALIAEGAQIAMAATTADGALRTQPVFCLMRIDLLDSLLEFLHSGQRKTEIWANQHRCAIVRFDDAQAFAGANTLAELRQLQS | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21179
Sequence Length: 197
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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A4Z027 | MTSSTTTAVPGLLLAGGLARRMGGGDKPMRVIAGRTLLAHVITRLAPQCEPLVLNANGDPARFAAYGLTVVPDDVPGFAGPLAGILAGLDWVASHRPAAQRMISVAADCPFLPRDLVARLTAACMAEDTDLALAASGGHTHPVIGLWPVRLREDLRHALVSEDIRKVTRFTARYKVATVTWPVVPRDPFFNANTAEDLAEAERLAAMEDRDA | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22565
Sequence Length: 212
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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C0RIT3 | MRAGQPKITGAKITGAIIAGGQSSRMQAGGVSGDKFLQPLGSAPVIAHVIARLQPQVDTLFINSKGDLSRFAAFGLPAVKDIAMNHGGPLVGLLTCLAHASPCRLLLTSAADTPFLPCDLASNLIRKQAETGARIILACSNERVHPIVGLWHTDLVPDLEKWLQYAEKASIFWFAKHIGFEVVNIPLAHAPRLAESYDPFFNINLPDDLLKAREINEALQA | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23761
Sequence Length: 221
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q0BH30 | MSASPSPSITGLLLAGGRATRMDGADKGLQLLDGTPLALHVLRRLSPQVDETLISANRNADRYAELGAPFDARIVADETADFPGPLAGLLAGMRAARAPLVACAPCDTPYLPADVVARLHAALDAQQADIAMAVTVDAQHARSPQPTFALLRTSLADDLAAALAAGERKVRAWYARHKTVEVEFRDERAFYNANSWHELAALARR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21874
Sequence Length: 205
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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Q39I98 | MPASASPSIAGLLLAGGRATRMDGVDKGLQLLDGTPLALHVLSRLSPQVDETLISANRHADRYAELGAPFDARIVADETPDFPGPLAGLLAGMRAARAPLVACSPCDTPYLPADLVARLQAALDAQQADIAMAVTVDAQHVRSPQPTFALLRTSLADDLAARLAAGDRKVRAWYARHKTVEVEFHDERAFYNANSWQELAALARR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21928
Sequence Length: 205
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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B1JY88 | MPAPASPSIAGLLLAGGRATRMDGVDKGLQLLDGTPLALHVLRRLAPQVDETLISANRHADRYAELGAPFDARIIADETPDFPGPLAGLLAGMRAARAPLVACSPCDTPYLPVDLVARLRAALDAQQAAIAMAVTVDAQQVRSPQPTFALLRTSLADDLAARLAAGDRKVRAWYARHKTVEVEFRDERAFYNANSWQELAALARR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22027
Sequence Length: 205
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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D4GQ17 | MSHRQPNRRERGVTRLLPETWRGLTLLLAGVLLLYYLLPIGALVFAQSPASLATDVTNEVVLTAATNSVVAATLSTLVAVAFGVPLAYWLSRTSFRGRDVILALVMLPLVLPPVVSGMLLLRLVGPAGLGQLTSVPLTRSLFGVVLAQTYVASPFLVVTAKTAFDGVDRQLEAAARSLGEDRVGSVRRVTLPLAKQGILAGVTLTFARAIGEFGATLMLAYYPRTLPVQIWVSYLSTGLDAAFPVALVLVGIAVGAILLVHALGTNPWE | Function: Part of an ABC transporter complex involved in molybdenum import (Probable). Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28536
Sequence Length: 269
Subcellular Location: Cell membrane
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Q84MM9 | MLRSLHSSSSSDTDNNSGGCKNNGGGGGEAAAAVEGGGDQRAVAAAAPSTRDLLLACADLLQRGDLPAARRAAEIVLAAAASPRGDAADRLAYHFARALALRVDAKAGHGHVVVGGGAARPASSGAYLAFNQIAPFLRFAHLTANQAILEAVDGARRVHILDLDAVHGVQWPPLLQAIAERADPALGPPEVRVTGAGADRDTLLRTGNRLRAFARSIHLPFHFTPLLLSCATTAPHHVAGTSTGAAAAASTAAAATGLEFHPDETLAVNCVMFLHNLAGHDELAAFLKWVKAMSPAVVTIAEREAGGGGGGGDHIDDLPRRVGVAMDHYSAVFEALEATVPPGSRERLAVEQEVLGREIEAAVGPSGGRWWRGIERWGGAARAAGFAARPLSAFAVSQARLLLRLHYPSEGYLVQEARGACFLGWQTRPLLSVSAWQPSSS | Function: Putative transcription regulator that controls rice tillering by initiating axillary buds and promoting their outgrowth. Rice tiller is a specialized grain-bearing branch that is formed on the unelongated basal internode and grows independently of the mother stem (culm) by means of its own adventitious roots.
Sequence Mass (Da): 45750
Sequence Length: 441
Domain: The C-terminal part of the protein is important for tillering. Mutant moc1, in which the last 124 amino acids are missing, is mono culm.
Subcellular Location: Nucleus
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Q9GQ00 | MKFIPEITLLLLLFVHSTQAKGKRRKCPEGAWSEGKIMNTIMSNYTKMLPDAEDSVQVNIEIHVQDMGSLNEISSDFEIDILFTQLWHDSALSFAHLPACKRNITMETRLLPKIWSPNTCMINSKRTTVHASPSENVMVILYENGTVWINHRLSVKSPCNLDLRQFPFDTQTCILIFESYSHNSEEVELHWMEEAVTLMKPIQLPDFDMVHYSTKKETLLYPNGYWDQLQVTFTFKRRYGFYIIQAYVPTYLTIIVSWVSFCMEPKALPARTTVGISSLLALTFQFGNILKNLPRVSYVKAMDVWMLGCISFVFGTMVELAFVCYISRCQNSVRNAERRRERMRNSQVWANGSCRTRSNGYANGGSVISHYHPTSNGNGNNNRHDTPQVTGRGSLHRNGPPSPLNLQMTTFDSEIPLTFDQLPVSMESDRPLIEEMRSTSPPPPSGCLARFHPEAVDKFSIVAFPLAFTMFNLVYWWHYLSQTFDQNYQ | Function: Functions as a 5-hydroxytryptamine (serotonin) receptor . This receptor is a ligand-gated anion-specific ion channel, selective for chloride ions . Relays a long-range endocrine signal from the body cavity neurons to modulate distal adipose triglyceride lipase atgl-1 function, via the nuclear receptor nhr-76 . Together with the G-protein coupled serotonin receptor ser-1 involved in male mating behavior . May mediate an inhibitory effect of serotonin on egg laying . Involved in regulating locomotory behavior, perhaps by modulating interneuronal signaling, acting in concert with G-protein coupled serotonin receptor ser-4 . In the presence of food, plays a role in initiating and extending dwelling behavior, perhaps acting in AIY, RIF and ASI neurons, in opposition to neuropeptide PDF-mediated signaling . Plays a role in aversive learning upon exposure to pathogens such as Gram-negative bacterium P.aeruginosa strain PA14; perhaps acting in interneurons in response to serotonin released by the serotonergic ADF neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56143
Sequence Length: 489
Subcellular Location: Membrane
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O59740 | MSALSESPAIPSFWRPETSEISKKPRPNTTVGFQFDNRNVGTSAPSTPAIRRNNTDSFERGLSLPLPSSKQDTGSSVLDPDGDAYVNRYARPVTAGSIYIPSNYHKSFSPNTFSGFNVKRSASKSPKRSANGSTSEDISIEGSPSETAKGARSSFNSNFRTFDIGSERRRRILEASQDSSRPGRYSYRTKSASPALIDTSTLDSRLNFTMGRLERSIAQLSKNTMRAVSHLENPPKDITLPKLNVKNSAWPLQPYSPPANETPASSSSSAKARPVSVPDMSSPVPASSVEYESLKAAVTYSPSQNPKKVAETDSESRKSSFQSSYNDADRPFQVGAQTQSTPNRISRSDSPIVYDVDTHSEDNASTASSEAISQSMRSFQPQPNTGSPFPRFTSTNTEDEQESDIPQSDANDSTVNLNQPNYANLTPTPQVSPKRPTYSRSSPLPSASVPALGDGSPDPPAAPSIQNSLSVHESEMPPHVTRDYTQPAASATPVPKEKPSEKSEKPPKKKGSKLEKFCCILM | Function: With tea1, acts in a positive-feedback loop in the microtubule-mediated regulation of cell polarity. Involved in the anchoring of tea1 at the cortex as well as the correct localization of tea3.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56542
Sequence Length: 522
Subcellular Location: Cell membrane
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Q9H3H1 | MASVAAARAVPVGSGLRGLQRTLPLVVILGATGTGKSTLALQLGQRLGGEIVSADSMQVYEGLDIITNKVSAQEQRICRHHMISFVDPLVTNYTVVDFRNRATALIEDIFARDKIPIVVGGTNYYIESLLWKVLVNTKPQEMGTEKVIDRKVELEKEDGLVLHKRLSQVDPEMAAKLHPHDKRKVARSLQVFEETGISHSEFLHRQHTEEGGGPLGGPLKFSNPCILWLHADQAVLDERLDKRVDDMLAAGLLEELRDFHRRYNQKNVSENSQDYQHGIFQSIGFKEFHEYLITEGKCTLETSNQLLKKGIEALKQVTKRYARKQNRWVKNRFLSRPGPIVPPVYGLEVSDVSKWEESVLEPALEIVQSFIQGHKPTATPIKMPYNEAENKRSYHLCDLCDRIIIGDREWAAHIKSKSHLNQLKKRRRLDSDAVNTIESQSVSPDHNKEPKEKGSPGQNDQELKCSV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i6A37) . Mediates modification of a limited subset of tRNAs: tRNA(Ser)(AGA), tRNA(Ser)(CGA), tRNA(Ser)(UGA), as well as partial modification of the selenocysteine tRNA(Ser)(UCA) . TRIT1 is therefore required for selenoprotein expression .
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 52725
Sequence Length: 467
Subcellular Location: Mitochondrion
EC: 2.5.1.75
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Q9UT75 | MLKPLCVVIGTTGAGKSDLAVQLAKRFGSQVINADSMQIYRGFDTITNKITVEEQENVHHRLMSFLNFDKEYSVPEFERDASRVIDEIHSQGKIPIVVGGTHYYLQSLLFEDTTLSAIDKLTNDSSPSKPPHPDSHILDDDPSAMLSYLKKIDPVMAEQWHPRDTRKIRRSLEIYFHTGRPPSEIYSEQKMKSSGSKLRYKSLIFWAFADSLVLMPRLDKRVDKMLSHGLVDEIKSMKSLAESEKFSPDFTRGIWQCIGFKEFMPWFEAPSDIVFNDCLERMKVSTRQYAKSQKKWIQSRFLPMCLAQQDLSPSSILFSTTNTTDLNNWEEQVEKACRVFQYFFYNGDAIAPSADDQHAFEKARDYLSIMNGRQSQKKKFVCEECLDKRGDPFTVIGEDAFNVHIKSRKHKTTVRRKKERAERQIRLKNIGILK | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 of both cytosolic and mitochondrial tRNAs, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 50121
Sequence Length: 434
Subcellular Location: Mitochondrion
EC: 2.5.1.75
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P07884 | MLKGPLKGCLNMSKKVIVIAGTTGVGKSQLSIQLAQKFNGEVINSDSMQVYKDIPIITNKHPLQEREGIPHHVMNHVDWSEEYYSHRFETECMNAIEDIHRRGKIPIVVGGTHYYLQTLFNKRVDTKSSERKLTRKQLDILESTDPDVIYNTLVKCDPDIATKYHPNDYRRVQRMLEIYYKTGKKPSETFNEQKITLKFDTLFLWLYSKPEPLFQRLDDRVDDMLERGALQEIKQLYEYYSQNKFTPEQCENGVWQVIGFKEFLPWLTGKTDDNTVKLEDCIERMKTRTRQYAKRQVKWIKKMLIPDIKGDIYLLDATDLSQWDTNASQRAIAISNDFISNRPIKQERAPKALEELLSKGETTMKKLDDWTHYTCNVCRNADGKNVVAIGEKYWKIHLGSRRHKSNLKRNTRQADFEKWKINKKETVE | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in the anticodon loop on a specific subset of tRNAs both in the cytosol and the mitochondrion, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). This modification optimizes the codon:anticodon fit in the ribosome and promotes translational fidelity. Competes with the farnesyl pyrophosphate synthase ERG20 for the common substrate dimethylallyl diphosphate (DMAPP).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 50237
Sequence Length: 428
Domain: The core aggregation region, although lacking the prion-typical Gln/Asn (Q/N)-rich domain, is required for the formation of the amyloid-like fibrillar aggregates.
Subcellular Location: Cytoplasm
EC: 2.5.1.75
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P39421 | MKYSVMQLKDFKIKSMDASVRASIREELLSEGFNLSEIELLIHCITNKPDDHSWLNEIIKSRLVPNDKPLWRGVPAETKQVLNQGIDIITFDKVVSASYDKNIALHFASGLEYNTQVIFEFKAPMVFNFQEYAIKALRCKEYNPNFKFPDSHRYRNMELVSDEQEVMIPAGSVFRIADRYEYKKCSTYTIYTLDFEGFNL | Function: ADP-ribosyltransferase that efficiently ADP-ribosylates both alpha subunits of host RNA polymerase RPOA . The ModA-induced ADP-ribosylation of RPOA alpha subunits inhibits transcription from viral early promoters .
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 23348
Sequence Length: 200
Subcellular Location: Virion
EC: 2.4.2.31
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P0A5Y1 | MRWIGLSTGLVSAMLVAGLVACGSNSPASSPAGPTQGARSIVVFAAASLQSAFTQIGEQFKAGNPGVNVNFAFAGSSELATQLTQGATADVFASADTAQMDSVAKAGLLAGHPTNFATNTMVIVAAAGNPKKIRSFADLTRPGLNVVVCQPSVPCGSATRRIEDATGIHLNPVSEELSVTDVLNKVITGQADAGLVYVSDALSVATKVTCVRFPEAAGVVNVYAIAVLKRTSQPALARQFVAMVTAAAGRRILDQSGFAKP | Function: Involved in the transport of molybdenum into the cell. Part of the binding-protein-dependent transport system ModABCD.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26576
Sequence Length: 261
Subcellular Location: Cell membrane
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P39423 | MIINLADVEQLSIKAESVDFQYDMYKKVCEKFTDFEQSVLWQCMEAKKNEALHKHLNEIIKKHLTKSPYQLYRGISKSTKELIKDLQVGEVFSTNRVDSFTTSLHTACSFSYAEYFTETILRLKTDKAFNYSDHISDIILSSPNTEFKYTYEDTDGLDSERTDNLMMIVREQEWMIPIGKYKITSISKEKLHDSFGTFKVYDIEVVE | Function: ADP-ribosyltransferase that regulates transcription by ADP-ribosylation of host ribosomal protein S1 . Additional identified targets include proteins involved in either translation or cellular metabolism such as elongation factor-Tu or trigger factor .
Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
Sequence Mass (Da): 24243
Sequence Length: 207
Subcellular Location: Virion
EC: 2.4.2.31
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P06597 | MKKLLKSVLVFAALSSASSLQALPVGNPAEPSLMIDGILWEGFGGDPCDPCTTWCDAISMRMGYYGDFVFDRVLQTDVNKEFQMGAKPTTATGNAAAPSTCTARENPAYGRHMQDAEMFTNAAYMALNIWDRFDVFCTLGATSGYLKGNSASFNLVGLFGDNENHATVSDSKLVPNMSLDQSVVELYTDTTFAWSAGARAALWECGCATLGASFQYAQSKPKVEELNVLCNAAEFTINKPKGYVGQEFPLDLKAGTDGVTGTKDASIDYHEWQASLALSYRLNMFTPYIGVKWSRASFDADTIRIAQPKSATTVFDVTTLNPTIAGAGDVKASAEGQLGDTMQIVSLQLNKMKSRKSCGIAVGTTIVDADKYAVTVETRLIDERAAHVNAQFRF | Function: In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the large cysteine-rich periplasmic protein. It has been described in publications as the Sarkosyl-insoluble COMC (Chlamydia outer membrane complex), and serves as the functional equivalent of peptidoglycan (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42550
Sequence Length: 394
Subcellular Location: Cell outer membrane
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F2YTN5 | MASNNNCAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYASKERTEKEWEKLFLEAGFSGYKIITSLGLRSLIEIYP | Function: Flavonoid 7/4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects . Catalyzes S-adenosylmethionine-dependent regioselective 7/4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including myricetin, quercetin and kaempferol . Mediates the formation of 4'-methyl derivatives from kaempferol, 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin) and 3'-methyl myricetin, producing 4'-methyl kaempferol (kaempferide), 3',4'-dimethyl quercetin (4'-O-methyl isorhamnetin), 7,4'-dimethyl quercetin (4'-O-methyl rhamnetin, rhamnacene) and 3',4'-dimethyl myricetin, respectively . Triggers the 7-O-methylation of quercetin, myricetin, 4'-methyl kaempferol (kaempferide), 3-methyl quercetin, 3',5'-dimethyl myricetin (syringetin) and 3',4',5'-trimethyl myricetin, thus leading to production of 7-methyl quercetin (rhamnetin), 7-methyl myricetin, 7,4'-dimethyl kaempferol (7-O-methyl kaempferide), 3,7-dimethyl quercetin, 7,3',5'-trimethyl myricetin (7-O-methyl syringetin) and 7,3',4',5'-tetramethyl myricetin, respectively .
Catalytic Activity: quercetin + S-adenosyl-L-methionine = H(+) + rhamnetin + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39377
Sequence Length: 355
Pathway: Flavonoid metabolism.
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P0DUJ5 | MKCIALFLVLSMVVLMAEPGEAFIHHIIGGLFHVGKSIHDLIRGKNRDMAEQQELERAFDRERAFA | Function: The amidated peptide is bactericidal on human pathogens like S.aureus or E.coli, as well as on the fish pathogen A.salmonicida . May also be active against a variety of fungi (By similarity). It can kill bacteria in less than 30 minutes (S.aureus) and 120 minutes (V.vulnificus) . It induces hemolysis of erythrocytes from human and fishes (sea bass and lesser-spotted dogfish) .
PTM: This peptide exists in N-terminally amidated and non-amidated forms. The amidated form is more active and has a greater alpha-helix content than the non-amidated form.
Sequence Mass (Da): 7508
Sequence Length: 66
Subcellular Location: Secreted
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P23848 | MTEDLFGDLQDDTILAHLDNPAEDTSRFPALLAELNDLLRGELSRLGVDPAHSLEIVVAICKHLGGGQVYIPRGQALDSLIRDLRIWNDFNGRNVSELTTRYGVTFNTVYKAIRRMRRLKYRQYQPSLL | Function: Activator of the Pm promoter, which controls middle genes expression. Activation of Pm allows expression of protein C necessary for late gene expression. In addition to Mor binding, activation of Pm might require the interaction of Mor with the C-terminus of host RNAP subunits RpoA and RpoH.
Sequence Mass (Da): 14714
Sequence Length: 129
Domain: The dimerization domain in the N-terminus and the DNA-binding domain in the C-terminus are connected by a linker containing a beta-strand.
Subcellular Location: Host cytoplasm
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Q7JQ07 | MSSFVPNKEQTRTVLIFCFHLKKTAAESHRMLVEAFGEQVPTVKKCERWFQRFKSGDFDVDDKEHGKPPKRYEDAELQALLDEDDAQTQKQLAEQLEVSQQAVSNRLREMGKIQKVGRWVPHELNERQMERRKNTCEILLSRYKRKSFLHRIVTGDEKWIFFVSPKRKKSYVDPGQPATSTARPNRFGKKTMLCVWWDQSGVIYYELLKRGETVNTARYQQQLINLNRALQRKRPEYQKRQHRVIFLHDNAPSHTARAVRDTLETLNWEVLPHAAYSPDLAPSDYHLFASMGHALAEQRFDSYESVKKWLDEWFAAKDDEFYWRGIHKLPERWEKCVASDGKYLE | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Function: Mediates transposition of transposon Mos1 by a 'cut and paste' mechanism. Transposases are sequence-specific nucleases and strand transferases that catalyze transposition through an ordered series of events: sequence-specific binding of transposase to the terminal inverted repeats (IR) present at each end of the transposon, pairing of the transposon IRs in a paired-end complex (PEC), cleavage of one or both DNA strands at each transposon end, capture of target DNA, and strand transfer to insert the transposon at a new site.
Sequence Mass (Da): 40851
Sequence Length: 345
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q07609 | MTRTSPRHHAPSETKRRVPMGGVHTNPGKKLTITAVAFQFFINGLVLAAWATSIPHVKNAYSFNDAELGVLLLIMAAGALLFMSLAGYFSHVFGSRRMSIQSALLFPSALVLIFAAPNCMTFLCSIVLFGAANGAMDVLMNHQAKALEENGFPRIMAFLHGCSSTGILAGIMTFGVIGDGHYVARSVTLLTGILIVARWLFPHLLDDVRSGEHRLAIGELRNCKLLMFGILSFLTMVTDGAIAEWSKLYLIRVEQVTDQVGSLGYVAFTLLMIAGRISGDRVKDAIGCRALIAISGSLASAGMTTALFMPSFAGKLAGFALLGLGMANLVPIIFSEAASMNTVSKTVGLTFVSVCGYSGFLVGPPIIGRIAEAVGLGRALLFIIAVGVIVACASVFFDRHRSGQPEP | Function: May be a membrane transport protein that could either transport a precursor for rhizopine biosynthesis into bacteroids or the finished product from the bacteroids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43216
Sequence Length: 407
Subcellular Location: Cell membrane
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P0AF07 | MKNQAHPIIVVKRRKAKSHGAAHGSWKIAYADFMTAMMAFFLVMWLISISSPKELIQIAEYFRTPLATAVTGGDRISNSESPIPGGGDDYTQSQGEVNKQPNIEELKKRMEQSRLRKLRGDLDQLIESDPKLRALRPHLKIDLVQEGLRIQIIDSQNRPMFRTGSADVEPYMRDILRAIAPVLNGIPNRISLSGHTDDFPYASGEKGYSNWELSADRANASRRELMVGGLDSGKVLRVVGMAATMRLSDRGPDDAVNRRISLLVLNKQAEQAILHENAESQNEPVSALEKPEVAPQVSVPTMPSAEPR | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34186
Sequence Length: 308
Subcellular Location: Cell inner membrane
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P56427 | MAKKNKPTECPAGEKWAVPYADFLSLLLALFIALYAISAVNKSKVEALKTEFIKIFNYAPKPEAMQPVVVIPPDSGKEEEQMASESSKPASQNTETKATIARKGEGSVLEQIDQGSILKLPSNLLFENATSDAINQDMMLYIERIAKIIQKLPKRVHINVRGFTDDTPLVKTRFKSHYELAANRAYRVMKVLIQYGVNPNQLSFSSYGSTNPIAPNDSLENRMKNNRVEIFFSTDANDLSKIHSILDNEFNPHKQQE | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 28849
Sequence Length: 257
Subcellular Location: Cell inner membrane
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O07887 | MARKRRAPRGAAQGWLTTYSDMVTLMLCFFVMLFNPTEVDITVLQSIAASIVGDPTGGGVSASSGRLADLGNTVNTLPSLEKGQKLATALKKAVSLFAPEIKSNKIAVTSDERGLVISLTSDSFFYPGSSDLNVEESREALLRVAQFLSDHALAGRRFRIEGHTDSVEVPEDGSTDNWELSTRRAVRVLHYLTDFGAQENRFSLAGYADTRAKFSNESPEGRAYNRRVDIVILDEGHF | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26050
Sequence Length: 238
Subcellular Location: Cell inner membrane
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Q98224 | MILLENGVRVFPKPGMGKDIYIGLANFGFENDVPELLGVAHLLEHILISFDYTRFVANASTARTYMSFWCRALRAEDYLAALETAVSWFFARGALRTDFSRVRIRNYVRELENEYYFRNEVFHCMDILTFLGGGDLYNGGRLSMLEQLDAVRELLGKRMRRLAGPNVVIFVRELSPAALALLERSFGTLPRFPSTIPATRLGSIHNKAVLVPAPFYALLIQVDNTVENVLAVICLAESYHFVDYETLGERLYVSFAFVHEQDCEAFLRNVGELRFEPAPRVELNYSDDYVMNLYVNFPWLQHDLADYLYTLNADCVPLLRGLEENLRRSVRERQLVVVYPSFSPSLFNSRDRQDHRLLVLDVDLARSAGPARVPRTFRRQPRAEVFVRYGDPALLDYVAFALARPRAAALRRLPRGVRLAHGFSHADMHEIMASETFIKYSRSRPAALFQYIFLAFFATGRSIAEILERREALVSFDARRCVNRLVFAKRARYDVVTKSSFVCGVLRGPRLSEAALTRAMWELKRKGLLYSLEHTRMHAKHTFYVFAFSIYPEQVYRYFARWQLVSKHCCVVSMRGEREDYSALRKEVVVNFV | Cofactor: Binds 1 zinc ion.
Function: Seems to be involved in viral proteins maturation by cleavage at Ala-Gly-|-Xaa motifs.
Sequence Mass (Da): 68420
Sequence Length: 593
EC: 3.4.24.-
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Q59XX2 | MLFKSFVTFTVLANALAAPLAHQHHQHKEEKRAVHVVTTTNVVVVTIGNGDQTTTFAAPSVAAESSVSVSVNTEPPQNHPTTTQDVASASTYPSSTDGSAASSSAAASSSSQAGSEPSGGVGSGGAKGITYSPYSDNGGCKSESQIASEIAQLSGFDVIRLYGVDCSQVEAVLKAKTSSQKIFAGIFDVSSITSGIESLAEAVKSCGSWDDIYTVSIGNELVNAGSATPSQIKAYVEEGRKALKAAGYTGPVVSVDTFIAVINNPDLCDYSDYMAVNAHAFFDGHVVAENSGAWVLQQIQRVWTACGGKKNVLITETGWPSRGDSNGVAVPSKSNQQAAISSIKSSCGASAILFTAFNDLWKADGPYNAEKYWGIYSN | Function: Surface mannoprotein required for hyphal morphogenesis, surface adherence, and pathogenicity. Contributes in a high proportion to the carbohydrate component of the matrix due to high levels of glycosylation and may play important roles during biofilm development and maintenance. Acts as a major antigen target of host cell-mediated immune response. Induces extensive T-cell proliferation of human peripheral blood mononuclear cells. Facilitates host dendritic cells maturation and promotes cytokine production through its glycosylated portion while its protein core is essentially involved in induction of T-cell response.
PTM: Glycosylated protein with a polysaccharide moiety composed exclusively of mannose and glucose at a ratio of 12.7 to 1. Contributes highly to the carbohydrate component of the matrix. Treatment with tunicamycin impairs glycosylation.
Sequence Mass (Da): 39264
Sequence Length: 378
Subcellular Location: Secreted
EC: 3.2.1.-
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P89035 | MATGKCYCPEDPRVGPLLVLCLLLLLILFSRSWNVAPVVVPSYHTVYHHEKYQNIEIQK | Function: Cell-to-cell movement.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6797
Sequence Length: 59
Subcellular Location: Membrane
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Q7KSC4 | MSIRRAMSTTASKEWRDYFMSTHFWGPVANWGIPVAALADTQKSPKFISGKMTLALTLYSCIFMRFAYKVQPRNWLLFACHATNATAQSIQGLRFLHYNYGSKEQQA | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12261
Sequence Length: 107
Subcellular Location: Mitochondrion inner membrane
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Q9Y5U8 | MAGALVRKAADYVRSKDFRDYLMSTHFWGPVANWGLPIAAINDMKKSPEIISGRMTFALCCYSLTFMRFAYKVQPRNWLLFACHATNEVAQLIQGGRLIKHEMTKTASA | Function: Mediates the uptake of pyruvate into mitochondria.
Catalytic Activity: H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12347
Sequence Length: 109
Subcellular Location: Mitochondrion inner membrane
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P63030 | MAGALVRKAADYVRSKDFRDYLMSTHFWGPVANWGLPIAAINDMKKSPEIISGRMTFALCCYSLTFMRFAYKVQPRNWLLFACHVTNEVAQLIQGGRLINYEMSKRPSA | Function: Mediates the uptake of pyruvate into mitochondria.
Catalytic Activity: H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12455
Sequence Length: 109
Subcellular Location: Mitochondrion inner membrane
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O74847 | MNASEKLSQKAAQSVTRRFITWLKSPDFRKYLCSTHFWGPLSNFGIPIAAILDLKKDPRLISGRMTGALILYSSVFMRYAWMVSPRNYLLLGCHAFNTTVQTAQGIRFVNFWYGKEGASKQSVFENIMQAAKHPESGTRQK | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16056
Sequence Length: 141
Subcellular Location: Mitochondrion
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P53157 | MSQPVQRAAARSFLQKYINKETLKYIFTTHFWGPVSNFGIPIAAIYDLKKDPTLISGPMTFALVTYSGVFMKYALSVSPKNYLLFGCHLINETAQLAQGYRFLKYTYFTTDEEKKALDKEWKEKEKTGKQ | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14995
Sequence Length: 130
Subcellular Location: Mitochondrion
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Q8L7H8 | MATSKLQALWNHPAGPKTIHFWAPTFKWGISIANIADFQKPPENISYLQQIAVTCTGMIWCRCSTIITPKNWNLFSVNVAMAATGIYQLTRKIKYDYVSEAEAAVEIEG | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12222
Sequence Length: 109
Subcellular Location: Mitochondrion inner membrane
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O01578 | MGPHRLLYQALCKAGDKFVYPVLPAFAKPAWNHAAGPKTVFFWAPTIKWTLIGAGLADLARPADKLSLYQNSALFATGAIWTRYCLVITPINYYLSSVNFFVMCTGLAQLCRIAHYRYQNPDWETKEIMETHN | Function: May mediate the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15074
Sequence Length: 133
Subcellular Location: Mitochondrion inner membrane
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Q55GU3 | MNALRGLLNKYTGNQIVFSNKYATTFFEKFPKLAFLNNVTNLAPMMKWSLSIVPITQILSGTKLPENIDVYQASSLCATGSIWTYYATLISPQNTGTRMLAACNAAMAACHGYNIYRRTKWEKSQIIPIENKN | Function: May mediate the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14936
Sequence Length: 133
Subcellular Location: Mitochondrion inner membrane
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O95563 | MSAAGARGLRATYHRLLDKVELMLPEKLRPLYNHPAGPRTVFFWAPIMKWGLVCAGLADMARPAEKLSTAQSAVLMATGFIWSRYSLVIIPKNWSLFAVNFFVGAAGASQLFRIWRYNQELKAKAHK | Function: Mediates the uptake of pyruvate into mitochondria.
Catalytic Activity: H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14279
Sequence Length: 127
Subcellular Location: Mitochondrion inner membrane
|
Q09896 | MFRAGFKRFWNHPAGPKTVHFWAPAMKWTLVLSGIGDYARSPEYLSIRQYAALCATGAIWTRWSLIVRPKNYFNATVNFFLAIVGAVQVSRILVYQRQQKRITAQSEQRTELARSLAA | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13536
Sequence Length: 118
Subcellular Location: Mitochondrion inner membrane
|
P38857 | MSTSSVRFAFRRFWQSETGPKTVHFWAPTLKWGLVFAGFSDMKRPVEKISGAQNLSLLSTALIWTRWSFVIKPRNILLASVNSFLCLTAGYQLGRIANYRIRNGDSISQLCSYILSGADESKKEITTGR | Function: Mediates the uptake of pyruvate into mitochondria.
Catalytic Activity: H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14555
Sequence Length: 129
Subcellular Location: Mitochondrion
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Q8LD38 | MATSKLQALWNHPAGPKTIHFWAPTFKWGISIANIADFQKPPETLSYPQQIVITGTGLVWSRYSTVITPKNWNLFSVSLGMAVTGIYQLTRKIKHDYVYEANSIVAKE | Function: Mediates the uptake of pyruvate into mitochondria. Negatively regulates ABA-induced guard cell signaling and mediates drought stress responses.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12181
Sequence Length: 108
Subcellular Location: Mitochondrion
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P53311 | MSASAFNFAFRRFWNSETGPKTVHFWAPTLKWGLVFAGLNDIKRPVEKVSGAQNLSLLATALIWTRWSFVIKPKNYLLASVNFFLGCTAGYHLTRIANFRIRNGDSFKQVIHYIIKGETPAAVAAKQTASTSMNKGVIGTNPPITH | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16230
Sequence Length: 146
Subcellular Location: Mitochondrion
|
O49636 | MATSKLQAIWNHPAGPKTIHFWAPTFKWGISIANIADFAKPPEKLSYPQQIAVTCTGVIWSRYSMVINPKNWNLFSVNVAMAGTGIYQLARKIKHDYATEAEPAVASE | Function: Mediates the uptake of pyruvate into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12005
Sequence Length: 108
Subcellular Location: Mitochondrion inner membrane
|
Q4WUN7 | MAEFVRAEVLGTKFEYTTRYVNPQPIGMGSFGLVCSAFDQITQQPVALKKIMKPFDSSSLAKRTYREIRLLKYLRHENLICMRDIFISPLEDIYIATELLGTDLGRLLSIKPLDSKFSQYFIYQILRGLKYIHSANVIHRDLKPTNILINENCDLKICDFGLARLQEPQMTGYVATRYYRAQEIMLTWQRYGVQVDVWSAGCILAEMLRRKPLFPGKDHVHQFHLITNILGNPPDAVIEKITSKNTVNFVKSLPSREPRDLSTVVPKDTDFDAIDLLKKMLVIDPDTRISAQDALRYPYLAPYHDPTDEPVASGPFDWSFDSADFPKETWKIMIYSEVLDYLNVDNPADPAPFDPSTPFDPSALEREFSEFLSDSGQI | Function: Mitogen-activated protein kinase required for growth on media where sorbitol or mannitol is the sole carbon source.
PTM: Dually phosphorylated on Thr-171 and Tyr-173, which activates the enzyme.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 43308
Sequence Length: 378
Domain: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
EC: 2.7.11.24
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Q55CS7 | MIFKKLFSKGSTSPTTRPRGATFSGTFPTDVLSDDGSGTNTNGLSNSTTNPSSIHSTPTTPTTTASTNLTNSNKLSTLAPITNGNRSLRGSKDGSGTTKESKKKVLTLNEKQKLLLKSMEYIKGSGTYYGNYMEFYEIPIQIYVGTEPSETYPSLSYNTELRSLILDFNKITEIPEQIGLLPNLKHLSLAANQLSQVPEFLSQLKSLESLELGINQFTSFPLNICKIKSLTLLRLETNNIKSLPDDFINLENLKDLSLLDNQLKEIPDSLPNNIEKLNLGCNDIINSYSKSLIRISHSLTTLNLSENKIEVLDESLSCLVNVKTLILDCNMIKVIPGSVLGSWKSLVTLNLPHNFISDLPAEIVTLDNLRIIDLRGNNFEFCKNYPSSESSSILFKIEEFIKDKEKLKSLILKENLEILSKLKDDNSTTTTTNINSNLDVPIIITTNIETIPTTSTTATTTETTNDITFKISDITEIIEKTDTTTTTTTTNQTDNVKLEEKVYEKQENDENNSVTLETTTTISIASDNTDEASIQIPQKEDGDKENLENDDKLLQESFSENNNNNNNEKQQEQQENPLKESQGKIQQLEEELEKLEQKQLELKDKIRLEKIKYQEIQQQSPRLSQQENNQEAIVVNTQPSSPPPTIIVNEQKSEKLENEKPTKREQPMVVVTKNNNKAEVEMTAPNQLIFWQSIVPDLIIDKLYLGCRECAMNKSWLKDNNVTHILTVANFKPLYPDLFKYLIINIDDVDEANIYQYFKEMNTFIDEGREKGGVLIHCRAGVSRSATATIAYIMMKNSVKFQEAFDITIKGRSRIYPNRGFLNQLKKFEKDLSK | Function: Probable phosphatase with dual specificity toward Ser/Thr and Tyr-containing proteins (By similarity). Dephosphorylates pNPP, in vitro. Essential for proper regulation of erkB (erk2) and optimal motility during development.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 94023
Sequence Length: 834
EC: 3.1.3.16
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Q54Y32 | MGNSHSSENGGNSGSGGGSGGGGSGYSGVSENMIIDLEGRYHIDYKNRNYKKLKPQMFSTFFEHYEIVQADSLINSDFIKNKTVKKNRDNSSNNNSNNNSNNNNNNNTLNNSTIITTTTTTTTTSTPTTTIMITPPQQQQQQRTSLDLTNRDISESSTPNEQQIRLAQEETENQEIVESSFLKSSPVPSPSSSVLKSFESDFQLNTDLTTETFDDNSAEKKRQQQQQQQQNEDSKQSSQQQTQKSKDKDESAKIVNNKSSSTTNIKPILAAAQTSRSTSIPAFNRNKTKEPTKQKIKKEHSTLRKNSLSSSNIITPNNTTNTNAKDGASYFNENSLMSVKSDIKIFSLDLSINRLENITNDILSIMARFEIQELTLSTNFFQIIPDLQLVKSLTTVNLTRNKLSKLQTSVFIELPSLTSLILDRNFISSIPDDIDQIKNLKYLSIKHNALEYLPNSLSNLSQLISLDLSQNKLKTLPPNFDDLINLRMVWLSYNQITSLPSMRKLVNLVTFDISSNKLLSLPKDFAYLVPSRIKQSYSDIDIDEYDENINTCNNINSNNNDSNNSNNNNNNNNDNNNNCNKNNILEMINSTELEGGGLGCLKELNIRDNRELISLPVEYKQVESLMTLVTSIPSEIIPGIFLGGLDSANNAPILQTLGITHILLAIGDCEPFFPKTFKYYSIDDARDAPQYDISQHFEQTNCFIESGRKSGGVLVHCRAGISRSSTLVISYLMKYQRMTFKQAMDLVQSKRPQIQPNPGFKDQLLKYEAKLFCTNILNISSHNSNNKNNNSSNNRKSINNRKSNNIIITINNSSNSNNNNSTDNSNNSSTSTTPNLSSLSSDSSSSASLSKLSISK | Function: Probable phosphatase with dual specificity toward Ser/Thr and Tyr-containing proteins.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 95418
Sequence Length: 856
EC: 3.1.3.16
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Q8TAP9 | MQRQNFRPPTPPYPGPGGGGWGSGSSFRGTPGGGGPRPPSPRDGYGSPHHTPPYGPRSRPYGSSHSPRHGGSFPGGRFGSPSPGGYPGSYSRSPAGSQQQFGYSPGQQQTHPQGSPRTSTPFGSGRVREKRMSNELENYFKPSMLEDPWAGLEPVSVVDISQQYSNTQTFTGKKGRYFC | Function: May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis.
PTM: Phosphorylated during mitosis in the cell cycle probably by CDK1.
Sequence Mass (Da): 19147
Sequence Length: 179
Subcellular Location: Nucleus
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P37773 | MRIHILGICGTFMGGLAMLARQLGHEVTGSDANVYPPMSTLLEKQGIELIQGYDASQLEPQPDLVIIGNAMTRGNPCVEAVLEKNIPYMSGPQWLHDFVLRDRWVLAVAGTHGKTTTAGMATWILEQCGYKPGFVIGGVPGNFEVSAHLGESDFFVIEADEYDCAFFDKRSKFVHYCPRTLILNNLEFDHADIFDDLKAIQKQFHHLVRIVPGQGRIIWPENDINLKQTMAMGCWSEQELVGEQGHWQAKKLTTDASEWEVLLDGEKVGEVKWSLVGEHNMHNGLMAIAAARHVGVAPADAANALGSFINARRRLELRGEANGVTVYDDFAHHPTAILATLAALRGKVGGTARIIAVLEPRSNTMKMGICKDDLAPSLGRADEVFLLQPAHIPWQVAEVAEACVQPAHWSGDVDTLADMVVKTAQPGDHILVMSNGGFGGIHQKLLDGLAKKAEAAQ | Function: Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate by linking it to UDP-N-acetylmuramate. The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in vitro.
Catalytic Activity: ATP + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Sequence Mass (Da): 49874
Sequence Length: 457
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Secreted
EC: 6.3.2.45
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Q08CH3 | MGSEPPSSPQVVEEGADEEDEELSGAEDADLRSSSGRGSLLTRRGITLRVLLKDGLVEPGDGVLSIHYLGKKFVGDLLNDGKIRWVETGQIFNSPSAWATHCKRLVNPAKKSGCGWASVRYRGQKLVQYKTTWLHKYQPSADMSLISEGEDDEMGDDDEEEGKTTIPVEDKNKKSKPELHEIGLTQRRDRERIPVRYCTLGTRDAARDPHTLVELSAFSAINRFQPFNVAVSSNVLLLMDFHCHLTSSEVVGYLGGRWDTNTQLLTVLRAFPCRTRLADKDAAPAVEEEICQNLFMRGLSLVGWYHSHPRGPALPSLQDIDSQMDHQLRLQGSSNGFQPCLGIICGPYYHGNQGVASTITPFWVVPPPEQRPNDHGIPVAVEVTYVQDNFLTTDVLNEMMLLVEFYRSAPDLVQFSQMWSPNTSILDKIKASLSGHAPKDQAYAQILEHVYNQLRNTQ | Function: Probable protease (By similarity). Acts as a sensor of N(6)-methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA, leading to its degradation (By similarity).
PTM: Degraded following binding to N(6)-methyladenosine methylated DNA (m6A).
Sequence Mass (Da): 51102
Sequence Length: 458
Domain: The RAMA domain recognizes and binds N(6)-methyladenosine methylation on DNA (m6A).
EC: 3.4.-.-
|
C0H3X7 | MLIKKNALSILKIVFPIAVLLFVIYQSKKELTNLSFKRTLMVINGLERTDLFMLVLIGLLAVAAMSLYDYVLKYSLRLSITNGKVFRVSWIANSFNNVLGFGGLAGVGLRMMFYKEHTKDHKALVKGIAWLTSSMLLGLSVFSIFVAARVLPVDEVIHEKPWLWAVVIGFALILPLSLAVSKIKDRKAGDEENADKVKNPIFAYIGASVVEWLMAGTVIYFALFAMGIHADIRYVFGVFVIAAIGGMISLVPGGFGSFDLLFLLGMEQLGYHQEAIVTSIVLYRLAYSFIPFILGLFFAAGDLTENTMKRLETNPRIAPAIETTNVLLVVQRAVLVRILQGSLSLIVFVAGLIVLASVSLPIDRLTVIPHIPRPALLLFNGLSLSSALILLILPIELYKRTKRSYTMAITALVGGFVFSFLKGLNISAIFVLPMIIVLLVLLKKQFVREQASYTLGQLIFAVALFTVALFNYNLIAGFIWDRMKKVLRHEYFVHSTSHITHATIMAIIIVPLFFLIFTVVYHKRTKPIGEKADPERLAAFLNEKGGNALSHLGFLGDKRFYFSSDGNALLLFGKIARRLVVLGDPSGQRESFPLVLEEFLNEAHQKGFSVLFYQIEREDMALYHDFGYNFFKLGEEAYVDLNTFTLTGKKKAGLRAINNRFEREEYTFHVDHPPFSDAFLEELKQISDEWLGSKKEKGFSLGFFDPSYLQKAPIAYMKNAEGEIVAFANVMPMYQEGEISVDLMRYRGDAPNGIMDALFIRMFLWAKEEGCTSFNMGMAPLANVGTAFTSFWSERFAAVIFNNVRYMYSFSGLRAFKEKYKPEWRGKYLAYRKNRSLSVTMFLVTRLIGKSKKDSV | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96322
Sequence Length: 856
Subcellular Location: Cell membrane
EC: 2.3.2.3
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Q2G2M2 | MNQEVKNKIFSILKITFATALFIFVAITLYRELSGINFKDTLVEFSKINRMSLVLLFIGGGASLVILSMYDVILSRALKMDISLGKVLRVSYIINALNAIVGFGGFIGAGVRAMVYKNYTHDKKKLVHFISLILISMLTGLSLLSLLIVFHVFDASLILDKITWVRWVLYVVSFFLPLFIIYSMVRPPDKNNRFVGLYCTLVSCVEWLAAAVVLYFCGVIVDAHVSFMSFIAIFIIAALSGLVSFIPGGFGAFDLVVLLGFKTLGVPEEKVLLMLLLYRFAYYFVPVIIALILSSFEFGTSAKKYIEGSKYFIPAKDVTSFLMSYQKDIIAKIPSLSLAILVFFTSMIFFVNNLTIVYDALYDGNHLTYYILLAIHTSACLLLLLNVVGIYKQSRRAIIFAMISILLITVATFFTYASYILITWLAIIFVLLIVAFRRARRLKRPVRMRNIVAMLLFSLFILYVNHIFIAGTLYALDIYTIEMHTSVLRYYFWLTILIIAIIIGMIAWLFDYQFSKVRISSKIEDCEEIINQYGGNYLSHLIYSGDKQFFTNENKTAFLMYRYKASSLVVLGDPLGDENAFDELLEAFYNYAEYLGYDVIFYQVTDQHMPLYHNFGNQFFKLGEEAIIDLTQFSTSGKKRRGFRATLNKFDELNISFEIIEPPFSTEFINELQHVSDLWLDNRQEMHFSVGEFNEEYLSKAPIGVMRNEENEVIAFCSLMPTYFNDAISVDLIRWLPELDLPLMDGLYLHMLLWSKEQGYTKFNMGMATLSNVGQLHYSYLRERLAGRVFEHFNGLYRFQGLRRYKSKYNPNWEPRFLVYRKDNSLWESLSKVMRVIRHK | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides. Consequently, MprF is shown to affect resistance and susceptibility to moenomycin and vancomycin, resistance to human defensins (HNP1-3) and evasion of oxygen-independent neutrophil killing and susceptibility to methicillin, oxacillin, bacitracin, gentamicin, beta-lactams and synthetic peptides (hBD3, CAP18) and other cationic antimicrobial peptides.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96866
Sequence Length: 840
Subcellular Location: Cell membrane
EC: 2.3.2.3
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Q7ZVH1 | MLNLIKLPQVFTINQVPKVFHEDGIISGYRHPCSSAKDCVLSLFQLTNETLNIWTHFLPTWFFLWKLLTVVLVLEDWRDPFIWPFLVFLLSCCVYPLASSCAHTFSTMSERARHICFFFDYGALSFYSLGSAIIYSSYSFPDKWVNGTFHLNYVSIAVVNSIISTALACYSRLGLPFLEYNCHSIKRPSGKLDQKLCKCLRIIAFVYPYLFDNIPLFYRIFVCAGEGCTVNEANTVHYQHTSLAFFTGFLFATHLPERLAPGSFDYIGHSHQLFHVFAIIGTYFQMTAIELDMAARKQWLHAHLPPVTFLNTVGAAFFSVVSGLCIVYVFSLSLFSTRGVKNKSF | Function: Steroid membrane receptor. Binds progesterone. May be involved in oocyte maturation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39356
Sequence Length: 345
Subcellular Location: Membrane
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Q6DC77 | MLSLIKLQRVFNVHQVPKAFHEDGIISGYRHPRSSATECVWSLFQLTNETLNVWTHFLPTWYFLWKLMTVLLMEDVWNEAYTWPLLVFLFSCCVYPLASSCAHTFSSMSTRARHICYFFDYGALSFYSLGSAISYSAYVFPDAWLSSSFHAYYISVAVFNTVLSTSLACYSRLGLPLLHYSHDIVERFSERQCPRMSKVLRILAFAYPYLFDNIPLFYRLFVCVGEGCTDNEANSVHVQHTLLAFLTSFLFATHLPERLAPGRFDYIGHSHQLFHVCAIIGTHFQMKAIEMDMGLRRSQLLASAPAISFNNTIGAALLCVSVSLGIICVYSLPLLYSSNPKNTANKE | Function: Steroid membrane receptor. Binds progesterone. May be involved in oocyte maturation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39519
Sequence Length: 347
Subcellular Location: Membrane
|
Q81C25 | MQQKTDVILIGAGIMSATLGSLLKELAPEWEIKVFEKLASAGEESSNEWNNAGTGHSALCELNYTSEKADGSIDISKAVKVNEQFQLSRQFWAYLVKSKLIRNPQDFIMPLPHMSLVQGKKNVEFLKNRFEALSKNPLFQGMEFSDAPETLKKWLPLIMEGRTSNEPMAATKIDSGTDVNFGALTRMLFDYLKTKNVELNYKHSVENIKRTKNGLWEVKVHDMNSGKIEHHTAKFVFIGGGGGSLPLLQKTGIPESKHIGGFPVSGLFMVCKNQKVVEQHHAKVYGKAKVGAPPMSVPHLDTRYIDNKKALLFGPFAGFSPKFLKTGSNLDLIGSVKPNNVLTMLAAGVKEMGLTKYLIQQVMLSHEKRMLDFPAFIPNAKSEDWDIVVAGQRVQVIKDTDAGGKGTLQFGTEVVSAADGSIAALLGASPGASTAVHVMLEVLEKCFPSRMIEWEEKIKEMIPSYGISLTENPRLFQDLHTSTGRTLGLNEKETVHN | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 54803
Sequence Length: 497
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
|
Q6NGC5 | MTQIIIAGAVGLLVSIFVTPVLIRRFSAEGLGQEIREDGPKSHLRKRGTPTMGGIAILIGITVAYAVTGIVGQVTGTGGLTASGLLVLGLTLALGGLGFADDFIKLYMGRNLGLNKKAKLIGQLAISLIFGALILLFPNADGLTPGSSHLSFLRDLPTVDLAIGPKAVGIAIFLLFIYILISAWSNAVNLTDGLDGLAAGSTAIVMGTYTVITFWQFRNSCSAGAQPGCYDVRDPLDLAILAAAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLSVASRTELLMIIVGALFVLEAASVVIQVAGYRTKKIRIFRMAPFHHHFENGGWAETTVVIRFWLIAAVAALIGASIFYGEWLSLTGV | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38273
Sequence Length: 366
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.13
|
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