ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q820U0 | MEKVLVIVGPTAVGKTALSIALAKKFNGEIISGDSMQVYRSLDIGTAKVTETEKEGIPHYLIDCREVSETYSAADFQKEGRQKIKEITEKGKLPIIVGGTGLYIQSLLYDFQLGSREIDDSPEIRETYNLFAEEKGNQALWLLLQQKDPLAANSIHFNNRKKVIRALEVFDKTGYSILTPKEKPARLYDYYLLGLETDRALLYERINQRVDQMMTEGLLEEAKQMFQQPHAQAAQGIGYKEFFPYFSGEQSLEMAVETVKQQSRRYAKRQLTWFRNRMAAHWWNLVQQPTDLPKLEKEVAEWLQQKESE | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 35568
Sequence Length: 309
EC: 2.5.1.75
|
B0S1C3 | MRKKCIVIVGPTGVGKTRLSIFLAKRLSSEIISADSMQIYKYMDIGTAKVEPKYQRVIKHHLIDIVEPYENFNVEQFKNLCIEKIEEISSKNKIPIIVGGTGLYINSITHKLEFNAVKSDDKLREELENISLQYGNEKLHEILEDIDPKSADKIHMNNVRRVIRAIEVCKLTGHKFSEINDKFDHYNDDYDFYIIGLNDDRQVLYERINKRVDEMIDEGFMAECKYIYEMTDENSQSIQAIGYREAFMYLNNKISFKDMISLMKKNSRKYAKRQLTWFRQDKRIHWMNLKDFREFEDIEQICLKNVKEWLYDKR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 37372
Sequence Length: 314
EC: 2.5.1.75
|
A6H0V8 | MNYLITIIGPTAIGKTSLSIALAKQYNCDIISCDSRQFFKEMRIGTAVPSDEELSQATHHFIQNKSIFEEYTVGDFEKEAITKLDELFSKNNIQIMVGGSGLYADAVLKGFDSFPNIKPEIREKIQEQYDENGIQYLQQKLQELDTEYYSKILSQNPQTLQNPQRMMRFVEVCLGTGKPYSSFLNKDKITRNFTTIIIGLEADREIMYDRINQRVDIMINEGLLAEAEKLYPNKDLNALQTVGYRELFSFFDADFTLNFAIEEIKKNTRRFSKRQITWFKRTENTIWFDYKADTSKIIEVINTKMKH | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 35718
Sequence Length: 307
EC: 2.5.1.75
|
B0TZB0 | MNKLIYGLAGPTASGKTSLSISIANKINAEIISVDSSLVYKGMNIGTAKPTLDEQGDIKHHLIDIIEPTESFSVADFITNVNKLKKEIWSRGKEVLLVGGTMLYFKGLIEGLSSLPESQLEIRQTLELERKAKGLQYLHQQLNKMDQESAQKINPNDQQRIFRALEVIMITGKKYSELVKTSKVGGLEEQLKLCALVPNDRSILHNNIELRFKQMLDQGFLDEVQSLRKNPKLTKETTAIRSVGYRQAWEYLDGDISYEEFVKKGIVATRQLAKRQLTWIRNWQDEINLVEVENQNKEQQILEYFDYK | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 35218
Sequence Length: 308
EC: 2.5.1.75
|
A2BZ20 | MLPSKPLVIVLIGPTASGKTELAIDIAKYFNIHIHNVDSRQIYRFMDIGTAKPTKVQQRAIKHFLIDVEDPSVKVNAKQFQEIATKSINRELNQKKTPFLVGGSGLYMNSIIKGFFAPDVPPQSFLRSQFEKLGQEKCWELLKVCDPELTKTINYADQIRTIRGLEVFYVTGKRMSSQRFQNPPPWRILELGINRVDLKERIFKRTKNMFEFGIIEETKNIINQYGSTLPLLETIGYKEAKNVIKENLTIEEAIELTTTKTIQFAKRQKTWFRNKNNAIWLNNKNLLKDAIIKIEYALG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 34492
Sequence Length: 299
EC: 2.5.1.75
|
Q7TV89 | MQNPKPLVIVLLGPTASGKTDLAIQIAKKIKVSIHNIDSRQLYKGMNIGTAKPTIEQQEEIKHYLLDLKDPNNPITLHEFKKEAELSLKNIFSKEKCGFLVGGSGLYLKSLTSGLCPPSVPAQEKLRKEFRRLGQKECHQILKKCDPIAWEKISPRDSIRTIRALEVFYSTGQTISSLKTLKPPDWNLLELGLDPRNLQQRIAKRTKILFQKGLIDETKALIHQYGEDLPLLQTIGYKEACTVIKGEYSITEAIEITTQRTNQFAKKQRTWFRRQHNPKWLNEKNSLEEALSLIQNVIG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 34078
Sequence Length: 299
EC: 2.5.1.75
|
Q15NR1 | MNQHTDNQQLPPAILLMGPTASGKTALAIELCQALPCEIISVDSALIYKGMDIGTAKPTAEELAQAPHRLIDILDPVQSYSVAEFRRDALAAMQDITQRGRIPLLVGGTMMYYKALTDGLSTLPQADPLVRAEIEKQAEKNGWQALHQELQGIDPVSAQRIHPNDPQRLSRALEIYRISGKSMTELSLNKQPSAPYQFSQFAIAPSDRHILHDRIAQRFDIMLNSGFEDEVIELKSRADLHLDLPSMRCVGYRQMWQYLDGENIYQEMREKGLAATRQLAKRQLTWLRSWQNLHWLDTFSKDNLTNVMKLSRIRT | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 35733
Sequence Length: 315
EC: 2.5.1.75
|
Q0IDZ4 | MNQINSEFGPDAGAKAPLVVALVGPTASGKTALALELAEHFQLEILNIDSRQLYREMDIGTAKPTAEQQQRVTHHLLDLRSPDQPITLQEFQQEATAAVSQVLKERGVAFLAGGSGLYLKALTQGLQPPAVPPQAELRRQLSSLGQANCHQLLQQADPQAAAKIAPADAVRTQRALEVLYSSGKPMSAQQSTNPPPWRVLELGLNPMELRSRIAQRTLQIYQEGLLEETRQLSQRYGPDLPMLQTIGYGEALEVLQGGLSEAQAIATTTRRTQQFAKRQRTWFRRQHSPHWLTGQDALSEAIRLIEAGLG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 34056
Sequence Length: 310
EC: 2.5.1.75
|
Q0AYB0 | MYKLAAIVGPTAVGKTNISLEVARQINGEIISCDSMQLYRGMNIGTAKASKEEQNIVAHHLIDIADPHENFTVARYQSLVKDLISTINARGKIPILVGGTGLYYQSVVDDYTFFPMEVRQSIRDKWNAIIQEKGLPHVYRLLEQIDPAYAQIISPNDQKRVVRALEVYELTGKAFSTLQDRAENTYYLAVVGLYLERRELYARIERRVDEMIKKGLIEEVAALREKGIDLSYNSMQALGYKQVFYFLEGFINREELLNEIKRETRRYAKRQLTWFKKDQRIKWFNVGDFSDEELLVKNICTFMEGQFGIV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 35812
Sequence Length: 310
EC: 2.5.1.75
|
P74040 | MAKVPPLIVICGTTASGKSQLALDLAQRLNAVILGADSRQIYKELDIGTAKPTLGDRQTVPHYLIDICEPTENFTLAEYQRQAQELIASLNQPILLVGGTGLYIQAIVKGLKIPAVPPQTNLREQLANLGQPFCYQLLSQVDPVAQSKIEPADVVRTLRALEVFYATGRPISSLQGENPPSYPIVQIGLGLEPEQLQPRIVHRTHAMVEAGLVKEVEGLINQYGEDLPLLHTLGYAEIKQYLQGQISLTQATESIIVHTRQFAKRQRTWFRKDSAIHWFDANQPNLLDSVTKLVQVDVNEGMF | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 33562
Sequence Length: 303
EC: 2.5.1.75
|
A6LMU4 | MKYTIISGPTAVGKTDLIIEISTKIGAQIISLDSRQIYKLMDIGTAKPTKEEQQKVKHHLIDHIYPDEYYNAFYFRQDALKLRKQLTKKGIIPLFVGGTGLYIDALVKGFFEGAPKDENIRKHLNKLEKKEPGTLRTMLQKYDPEYALKIHPSDMKRTIRALEVFFKTGKKISELQSQTKISNKYKIIVLTRNRQELYERINTRVEKMIKAGLIDEVEKLLELYPKDINAFQTIGYKELIHYFENKYDLKTAIHLIKRNTRHFARRQLIWLRRYKNAIWINLSEISRRETIEKIEKIINEV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 35500
Sequence Length: 301
EC: 2.5.1.75
|
Q9WYZ5 | MKIAIVGGPTAVGKTDIMIEVCEEIGAEIISMDSRQIYRYMDIGTAKPTPEQRKRVLHHMIDIIDPDEYYNAFMYRKDSLRAMEDVLRRGKIPVYVGGTGLYADALVRGIFEGVPADENIRKELRELERREPGILRKMLEELDPEAATRIHPNDLKRTIRALEVYMKTGRRISELQKEAKGDDRFFIIVLTRERYELYERINKRVDKMIEMGLVDEVKRLLGMGYSKDLNSMKTIGYKEVIDYLEGKYDFDKMVHLIKRNTRHFARRQIIWFKRYKEAVWYNLTFEDVGEVKEKLKKLIVENFSV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 35926
Sequence Length: 305
EC: 2.5.1.75
|
B9L505 | MNKRKPVVALVGPTSVGKTATAIELALTFGGEVVSADSRYLYRGMDIGTDKPTLEERRGVPHHLIDILDPRDDYSLALFQRDAQRAIEEIHARGRLPIVAGGTPLYLRALLEGWRIPPAPPNPELRAQLELRARREGPEALHRELQTVDPVAAARIPPENVRRVIRALEIFLTTGRRMTELEGREAPPWRVLWLGLTMPRDELYRRIDERVDRQVARGLVEEVQRLLEQGVPPDAPAMTALGYRQIVAFLTGQLSLEEAIQRIKYDTHRYARHQLTWLRRMKQVEWYDVTQPGWYEQLRERVERSLREESDEGDVAVHQSGGGKEAPRA | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 37580
Sequence Length: 329
EC: 2.5.1.75
|
Q5SKS1 | MEAIPVLAGPTGSGKTFLALRLGEEVPVEVVSADATMVYRGLDIGTDKPTPEERARVPHHLVDVLEPHEAMSVARFLALAEEAIAHVLSRGKLPLVVGGTGYYIRALSEGLHDLPPPDPGVQEALWAELEARGLEALLAELARASPEDARRVGKNPRRLVRALEVLRRTGTPPARFPKRPPRFRYKKLVLWPDRAWLFPRLEERAKAQFARGLVEEVRGLLERYPRMPTALQAIGYKEVAGHLLGAYGLEEALERDIRAVKAYAKRQYTWFRHEPGDVVYLPRGGEEAYVGFRDWLCLHFGL | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 33811
Sequence Length: 302
EC: 2.5.1.75
|
B5YK93 | MKRKIVILLGPTGVGKTELSIKIAKLLNAEIISSDSMQIYKYMDIGTAKPTLEQRKEVIHHMIDIVNPWDYFSTGAYIEIVKEVIEKIFEREKIPLVVGGTGLYLRAMTEGIFEGPDADWNLRMELMNKERDNPGFLYNLLKEIDPIKADKIYPSDLRRILRALEVFFKEKKQISELQEKLTKPLSYNFIKIGVTRERKELYRIIEERVDKMICSGLIEEVRNVLTLIKRNATSLSPLPALQAIGYKEIAGCLADLYSIDEAVRLIKKRTKMYAKRQFTWFRKEKDIMWFDISGRHDFEIIAEQIYSALSEILHK | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, 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): 36666
Sequence Length: 315
EC: 2.5.1.75
|
Q3B6A6 | MPEGRRFYIQTFGCQMNEADSGIIARVLLDAGFRRADTEQDADVVLLNTCAVRENAVEKIAHLLEHLKGAKKRRKTLQVGVLGCVPQHQREEMFSRFPAIDFIAGPDSYRRLPSLIDDAASAVRSAMLDFDPSETYVGIRQVREGRISAFIPVMRGCNNMCAFCVVPFTRGRERSQPLAMVTGEARELAEAGYREITLLGQNVNSYSDPASGATFSALLDAVALAAPDVRIRFTTSHPKDISVGLIDTIARRPNICRHVHLPVQSGSDSVLRRMNRGHGISEYLEKIRIIRDALPGVTLSTDIIAGFCGEREEDHRATLDLLRTVRFDAAFMFHYSTREGTLAARTLPDDVAETDKKRRLQEIIDLQQEISAENNRRQVGTVAEVLAESESRRSPGRLLGRTDGNRAVVFDRGECMPGDLVRVRLTSSTSATLSGSREGLIRAFLS | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49431
Sequence Length: 446
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q8KB05 | MRQRMSRMPSSFYIHTFGCQMNQADSEIVTALLRAEGFVPSADETNADIVLLNSCAVRENAEERLGNILMHLKGRKRRCKELVIGVLGCVPQFERERVFSDYPFVDFIVGPDNYRELAGLVAGLREAVARPALLDYDQTETYAGIEPVRAGSISAFLPVMRGCNNHCAFCVVPVTRGRERSVGFERVVAEVVALEKAGFREVTLLGQNVNSWRDAEKGLDFAGLLEGVSLAVPSMRIRFTTSHPKDISEALVKVIAARPNLCNHIHLPVQSGSSRMLDLMKRGHTREEYLDRIAMIRSYIPEVAITTDLIAGFCTETEKDHRETLSLMEAVGYDTAFMFHYSVRPGTWAARNLPDDVPDTVKKARLQEIIELQNAISREIFQREIGKTVEVLAEAESKRSESMLMGRTPENRVVVFSRGRFNPSDTLLVKITGATSATLSGEAV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49472
Sequence Length: 444
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
A8AJE9 | MTKKLHIKTWGCQMNEYDSSKMADLLDATHGYQLTEVAEEADVLLLNTCSIREKAQEKVFHQLGRWKLLKEKNPDLIIGVGGCVASQEGDHIRQRAHYVDIIFGPQTLHRLPEMINSVRGDRSPVVDISFPEIEKFDRLPEPRAEGPTAFVSIMEGCNKYCTYCVVPYTRGEEVSRPSDDILFEIAQLAAQGVREVNLLGQNVNAWRGENYDGTTGSFADLLRLVAAIDGIDRIRFTTSHPIEFTDDIIEVYRDTPELVSFLHLPVQSGADRVLNLMGRTHTALEYKAIIRKLRAARPDIQISSDFIVGFPGETTQDFEQTMKLIADVNFDMSYSFIFSARPGTPAADMVDDVPEEEKKQRLYILQERINQQAMAWSRRMLGTVQRILVEGTSRKSIMELSGRTENNRVVNFEGTPEMIGKFVDVEITDVYTNSLRGKVVRTEDEMGLRVAETPESVIARTRKENEIGVGFYQP | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53646
Sequence Length: 474
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
B2A3X6 | MTLYQLGNGKKFYTLTFGCQMNEHDSEVLAGMLDQMGFEKAASEEEADLLIINTCAVREKAEQKVLGKIGTLRYLKENKPDMKIAIGGCMVQQEHVANKIYRDFTHVDIIFGTHNINRFPQLLEHVMQKGKRVKEISQDDSQVFENLPHKREDSIKAWVVISYGCDNYCKYCIVPYVRGQQRSRDPEHIKYEVEKLAKEGLKEITLLGQNVNSYGKDLDQNISFTNLLEELSKIEGIERIRFMTSHPKDFDKELITTLKESNKICEHFHLPVQAGSNKILKKMGRGYTREHYVDIVNDIRAELPNASITTDIIVGYPGEEEEDFQETLDLVQNVKFDSAFTFVYSKRSGTPAAEMAEQVDEQTKKGRIQKLISVQQEISEQRNKDLENTVQRILVEGVSKNNEDMLSGRTRTDKLVHFPGDKELIGELVDVKITRGHSWNLYGEIFEDSLT | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51725
Sequence Length: 451
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
D5ZT17 | MSSIDRSQSVGGTRTYEVRTYGCQMNVHDSERLAGLLEDAGYVRAPEGSDGDADVVVFNTCAVRENADNKLYGNLGHLAPKKARRPGMQIAVGGCLAQKDRDTIVKRAPWVDVVFGTHNIGKLPVLLERARVQEEAQVEIAESLEAFPSTLPTRRESAYAAWVSISVGCNNTCTFCIVPALRGKEKDRRPGDILAEIEALVAEGVSEITLLGQNVNAYGSDIGDREAFSKLLRACGRIDGLERVRFTSPHPRDFTDDVIAAMAETPNVMPQLHMPLQSGSDAVLKAMRRSYRQERYLGIIEKVRAAIPHAAISTDIIVGFPGETEEDFEQTLHVVREARFAQAFTFQYSKRPGTPAAEMDGQIPKKVVQERYERLVALQEEISWEENKKQVGRTLELMVAEGEGRKDDTTHRLSGRAPDNRLVHFTKPEQEVRPGDVVTVEITYAAPHHLLAEGPVRDVRRTRAGDAWEKRNAAEAAKPAGVMLGLPKVGVPEPLPAVTGGCAVD | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 55465
Sequence Length: 505
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q67NJ9 | MAQMQIDPEAGRRIHGKPEPRVHIETFGCQMNEHDSEIMYGILAQMGYVKAQGPDDADLLLFNTCAVRESAVEHAFGRIGQLKPLKYTNPDLIIGVCGCVPQVEGQVERIKRMFPYLDLIFGTHNIHRLPELVERARSERETVVDVWESMGDDFPDILPAAREGDLKAWVTIMYGCDKHCTYCIVPTTRGKERSRPYEVILAEVQELARQGFKEITLLGQNVNAYGKDLYGRHGEGAFDFGDLIELIDRNSPGIERIRFTTNHPKDFTRKMVEQIARAEKVCEWFHLPVQSGSDSVLRRMKRSYNRKQYLRLVGWIRELIPDAVITTDIIVGFPGETEEEFQETLSLVEEVQYDAAFMFMYSERAGTPAAQMEDRLSVPEKKERLQRLMEVQNRIARAKNEARVGKVYDILVEGLDKGKPDVVFGWTRGNILVTFPGDESLRGRIVPVRITRAGTWTLEGELVESPVTLA | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 53517
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q2LT94 | MMKSSNKSSGSLIRLDKKHIYIQTLGCQMNVHDSEQIAALMEEKGYICTEDANEADLIILNTCSIREKAAQKAKSQLGRYRNLKRKKRNLLIGVGGCLAQQLGDELLTKVPDIDFIFGTHNIHQLPDFISRIEKSRKKIVETTLHPSTPSIGVLALPCNGQVSSFVTIMQGCNNFCSYCIVPYVRGREESRPPEDIIHEIRMLADHGVKEVTLLGQNVNSYARKTSGEMGFAELLREIEKIKGIERMRFTTSHPKDLSEFLITAFSDLSKLCHHIHLPFQSGSDRILALMNRGYTKSDYLAKVERLRTVCPDISITADVIVGFPGESDEDFKETIDMMNQIRFDNLFSFKYSEREGTAAVKMDGKVSEPLKLERLQILQALQEQHTLEKNKAMEGKQEDVLVEGFSKNCRKDLTGRTSTNKIVNFSGCVDLIGDMVSVLIKEAYLHSLRGEMLCEEVVHAN | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51938
Sequence Length: 461
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q3A594 | MKSFYLETFGCQMNVVDSEQIVGLVQSLGYSSVDSPEQANLIILNTCSIRARAERKVYGHLGRFKPLKQRRPELIIAVCGCVAQQEGQRMLEKVPYLDIVCGTHNIHRLADMVRDAELHRARHVEVDFLEADKRRRLFPERAPSAEVSRFVTVIQGCDNFCSYCIVPHVRGREVSRPSAEVLEEVRLLVEQGAREITLIGQNVNSYGCKEDDEISFASLLRKVAEVDGLERIRFMTSHPKDLSDELIDCFADLDKLCKHIHLPVQAGGDAVLKAMRRGYTRDQYLGRIERLRRVCPEIRMTSDVIVGFPGETESEFEQTMDLLERARFTEIYSFIFSARPGTSAADLPDDIPKEVKQQWFDRMLALQEEITRQYHQMDIGQVLPVLVEGSSRQGNGQLFGRTTWNRIVNFDGNPDLVGRIVPVRLTVAYRNSHLGERV | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49911
Sequence Length: 438
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
A0LFB7 | MITPLAKTAPAPRYLYVRTFGCQMNEYDSQRALRLLCAVGYRPTSDIADADVIFLNTCSVRDKAEQKVYSFLGRLRRLKAHRPWLKIVVAGCVAQQLGDGLLKRFEHVDLVVGTRGIGSIASLLEEVERSKRRVAHLPAEELQGFTTDKCRTVGTGDVVAQVTIMQGCNNFCTYCIVPHVRGRERSRAPDDILREIDFLASRGAREVLLLGQNVNSYGRGLPDPISFPDLLRRIGKETSIRRVRFTTSHPKDLTEDLIECFAGLPFLCKHLHLPFQSGSDGILKLMHRGYTARQYLEKIARLREVCPEIALSTDVIVGFPAESEEDYLQTLRLIEEVRFDSLFSFRYSDRPLTRAAGFPDKVPMDVKVRRLARLQSIQADITLQKNLAETGTVREVLVEGPSKASNGQMTGRTQQNRIINFQCPVDLTGKIVPVRIVAAYSHSLKGELLSQPGKES | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51141
Sequence Length: 456
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
A5GML6 | MLPSRERGSYWITTFGCQMNKADSERMAGILESMGYREASAELDADLVLYNTCTIRDNAEQKVYSYLGRQAQRKRTNPNLTLVVAGCVAQQEGESLLRRVPELDLVMGPQHANRLETLLQQVDSGQQVVATEEHHILEDITTARRDSSICGWVNVIYGCNERCTYCVVPSVRGKEQSRLPDAIKLEMEGLAAQGFKEITLLGQNIDAYGRDLPGITPEGRRQHTLTDLLHHVHDVEGLERIRFATSHPRYFTDRLIDACADLPKLCEHFHIPFQSGDNDVLRAMARGYTVERYRRIIDRIRERMPDASLSADVIVAFPGETDAQYRRTLALIEEIGFDQVNTAAYSPRPNTPAADWDNQLPEDIKVERLREINALVERCARERNGRYAGRVEEVLAEGINPKDPSQLMGRTRTNRLTFFSATGADDRRYQAGDLVNVHIDAVRSFSLSGTPLNC | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51251
Sequence Length: 454
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
Q0IC70 | MALSSPVSPSLAKTNPASSTLDEGQRGSYWITTFGCQMNKADSERMAGILETMGYQEANAELDADLVLYNTCTIRDNAEQKVYSYLGRQAIRKRTNPNLTLVVAGCVAQQEGESLLRRVPELDLVMGPQHANRLETLLTQVQAGQQVVATEDHHILEDLTTARRDSSTCAWVNVIYGCNERCTYCVVPSVRGKEQSRLPESILLEMEGLAARGFKEITLLGQNIDAYGRDLPGITAEGRRQHTLTDLLHQVHDVEGIERLRFATSHPRYFTERLIDACADLPKVCEHFHIPFQSGDNELLKAMARGYTVERYRRIIDRIRKRMPDAAISADVIVAFPGETDAQYRRTLALIEEIGFDQVNTAAYSPRPNTPAADWNNQLSEEVKVARLQEINALVESTAKERNARYAGRIEQVLAEGMNPKDPSQLMGRTRTNRLTFFSAESPQGITHRAGDLVDVRIDQVRSFSLTGTPVIN | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 52834
Sequence Length: 473
Subcellular Location: Cytoplasm
EC: 2.8.4.3
|
P91928 | MYRLAVRDQCKCALQRTLQQTTANNRQFGGSSSGSGGREQGRRQQEEQGQQGDQGYQGYQSLPPHMREAGFGKVVLFVSPLAAVGGVITYAKYDDDFRKLVEKNVPGAGSVIKVALQEEPPFKGITKNVNDQIDKVKSGIETVTSTVDSVTSKVTGLFGGGSGDDKSKKSKVEPVKATPAEEKRPSKPSEVSKTEAKPVSKPAAAAAPAPAAKPKDNPLPRDVVELEKAIELSAQLAVKEYNVAIGVLKGFNDDVRKVVDKAVENGENSLWTTLKNRASARDTAVATAERAAREAQEKIVACEIALSAAATAQNAKKVEAVRDKIKKLVDHIGNVKDELYRHKDTASVSDKYWRNVEKARNYFIDEIESIFPGLSLADKKLNLSKEDLDLFILHAYTHVLAYQKELQRLQTDGELRLKRAIDSVRGDNDSEALRAQLEYHLEAERRKLAVENQKKIFHIHAESDKLLRLQLKKQAEAHADHIKDIVAQRETDLTRSFKRELEDKLATEKANYKLQLAGMLGKLRGMDAALAERADAERTANQAQALWAACQALWASVRAATPGVHYKDRLRPLKNEINAIAKVAKGDDLVAAVLESVPKEAQERGVYPEDALRERFLNVERVARRLALVPEEGAGLPIYFLSYLQSLFILRPDNPISKDELENKPFDYSKLDTYDILNRARYHVDRSDFLQALKYMNLLQGASRKIAGEWMKEARLMLETQQAANTLMAHAAASGLLYL | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 82014
Sequence Length: 739
Subcellular Location: Mitochondrion inner membrane
|
Q5B6I7 | MLRSSVLQGRHILSSSARPRPAPQWLARAGASSRLAGQRFFADAKSPTPVTPSSATPVPAETAAKSTAGPSATETPTPAPTRKTGRFRKFLIYLILTSGLAYGGGVFLALKSDNFHDFFTEYVPYGEESVLYFEERDFYRRFPNTLRNKNRLSPASRDEGSRVTIPSKSGLSSKEVEETGTDVSQPGPHMSAVTPAKADEATIKPAAAKPEEKTAAVKEAKKQAQEPEKPREEPKQEPKLPGSAPITTLEFANVSEGDEPIVQELVKTFNDIITVISADEDSAKYSKPVAKAKEELQKIGEQILSVRDEARRAAQEEIEKAHATFDESARELIRRFEEVRANDAAQYREEFEAERERLALAYQQKIQTELQRAQEIAEQRLQNELVEQAIELNRKYIHEVKDLVEREREGRLSKLSELTSSVSELETLVTGWREVIDTNLKTQQLQVAVDAVRSALERSTVPRPFVRELVAVKELAGDDPVVEAAIASINPAAYQRGIPSTSQIIERFRRVADEVRKASLLPEDAGIASHAASLVLSKVMFKKDAEAGSDDVESVLLRTENLLEQGNLDDAAREMNSLKGWAKILSKDWLADVRRVLEVKQALEVIETEARLQCLRVE | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68634
Sequence Length: 618
Subcellular Location: Mitochondrion inner membrane
|
C7YIH6 | MLRTSLRSVRVLGGRPSVAAAARQWPVAASRRAALVGQRHYAVDKKPESASSPSLPNTQSVASDKIHETTIDDVGETKAATVDAPKTTPPPPPPPPAPKKKGFFRRLRNFVFTLFVLGAVGFAGGVWYSCFSDNFHDFFTGYVPFGEQAVLYLEEMEYKKRFPNSATNAKSRDADGAVRIPAQSGASWRVADGTRRSSAGPVPAKQEEPKAEAPKPKAAEPKPTAKVVEKPAPTPAPAPTPRSESGFKAPEVNEPSRYPPLKPIDLLSLDDAREPVIQDLVHMVNDLILVINADGAHGRYGSSVNKAKNEITKVGGKLKGMKEQFEKKAAGQVRDKIDEFDKAATDLIDRVESAMITQESQWRHEFEEEMKKVRENYEDRVKVLLERERKLNEEKLQNQLLEQALALKKEFVKDVENQVEQERESRLGKLTALSSAVADLEKLTTGWNEVLDTNLQTQQLHVAVEAVRASLEDDHHPRPFIRELVALREIASDDPVVNAAIASVNPTAYQRGISTSSQLIDRFRRVANEVRKASLLPDEAGVASHASSWVLSHVMFKKQGLAEGNDVESVLTRTQTYLEEGDLDSAAREMNGLEGWAKTLSKDWLGEVRKVLEVQQALDVIATEARLQSLRVD | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69945
Sequence Length: 633
Subcellular Location: Mitochondrion inner membrane
|
Q16891 | MLRACQLSGVTAAAQSCLCGKFVLRPLRPCRRYSTSGSSGLTTGKIAGAGLLFVGGGIGGTILYAKWDSHFRESVEKTIPYSDKLFEMVLGPAAYNVPLPKKSIQSGPLKISSVSEVMKESKQPASQLQKQKGDTPASATAPTEAAQIISAAGDTLSVPAPAVQPEESLKTDHPEIGEGKPTPALSEEASSSSIRERPPEEVAARLAQQEKQEQVKIESLAKSLEDALRQTASVTLQAIAAQNAAVQAVNAHSNILKAAMDNSEIAGEKKSAQWRTVEGALKERRKAVDEAADALLKAKEELEKMKSVIENAKKKEVAGAKPHITAAEGKLHNMIVDLDNVVKKVQAAQSEAKVVSQYHELVVQARDDFKRELDSITPEVLPGWKGMSVSDLADKLSTDDLNSLIAHAHRRIDQLNRELAEQKATEKQHITLALEKQKLEEKRAFDSAVAKALEHHRSEIQAEQDRKIEEVRDAMENEMRTQLRRQAAAHTDHLRDVLRVQEQELKSEFEQNLSEKLSEQELQFRRLSQEQVDNFTLDINTAYARLRGIEQAVQSHAVAEEEARKAHQLWLSVEALKYSMKTSSAETPTIPLGSAVEAIKANCSDNEFTQALTAAIPPESLTRGVYSEETLRARFYAVQKLARRVAMIDETRNSLYQYFLSYLQSLLLFPPQQLKPPPELCPEDINTFKLLSYASYCIEHGDLELAAKFVNQLKGESRRVAQDWLKEARMTLETKQIVEILTAYASAVGIGTTQVQPE | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 83678
Sequence Length: 758
Subcellular Location: Mitochondrion inner membrane
|
Q6CSB8 | MFRASKALGQRFASTNVPVKTARPFRNFLWKLGAATTVFYVGGVALSTYNYQFAELFTDNVPLAEELVQLVESYNDGTLNAPQLSLDEIRKKFGSITRKVQSVPHLGSTSSTVTESQSIASGSGSTAAAATTGTDSNSVVLSSVPPVGSVLLRLPHLKLDDDSNSFNNKSFVESFNKQVDSLNEKEFILPENAVESFLESYHGLSSQLNELNRDLADQLNSQLGQLSAELKQSVESDKVKEIESNKLQLMQQFEKDLSNLKVEFEQKFDSQLQSSLKANEQAMLAKHKNELAMLSIKQVQEFNKIISNKIENERNGRLKNLDELNGSVKTVSDSLAALEETLLRSECVNQLTNLVSSIKFKLNLDNTPSLDISKDLQKLTTLVNILPGKPNKCDAKEPQLIDVVVNELNSLTSAKENKQILSNEQLLNRWGLLQDKIREASLLPPNAGFLGHVSAKFFSLFLFNKSGISNENDIDSVISRVTENIKLNRLDKAVEDVVQLQGWSRLEADDWLQAARSKLELETLVDVVDHEIKTL | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59391
Sequence Length: 535
Subcellular Location: Mitochondrion inner membrane
|
C4QXN2 | MLRTIGTKASGITFRGVRFQSTNPTVKKSKPLRKFLFRLGLLTGVFYAGGVAVSLKNDIVQDAFIEHVPLGEALLDFTEYYVNHPEELSFSSTKQKLQNFDKTVLIPKRGVQSAKVEDVEHIKNVTRGSADESVSLSKTIYSNLNLPSIDLEFKDEVLQSSVEHLNHLIDTIRTQVNTVDLLPQVEQLKSSIKELGSKYNSFVTDRNTAVEEALAKLDDELKTKYQNKELALTDKYISDLQETKRQIELKHDQILAKELDTAQRRILLEAENIIVQARINTLSEFESIISDKIDNERNGKLKNLDALAKRVEELENVQIKLFDNISNAEKLTNLKKTVSKINRLLISSNDGVDAKTLINEVNKFKTYSKDLNNELISSVLLNLPNDKALSNGVLSQAQLLARWDLLTPELRSASLLPPNAGILGHLSSKLFSFFLLGKSGTPTSGNDIESVISRVHDNLLKNRLDDALEEVSSLKGWSRKLSEDWIVEARKKLELQVLVGVLENEVSLL | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57129
Sequence Length: 509
Subcellular Location: Mitochondrion inner membrane
|
C5E325 | MLRSRATINCVKSGRAGRALSRGMATFEGQPAARPNRLSKLLVRVGLATVGFYVGGVTLSLNNDQFGELFCDNVPLAESLVEMYEEFRDEKMQASRMSLDELKQKFGELGTKVDRIPNRGADPALTSQAVAALPASKEVRLEDESLVKLRLPEVEQLGSCKRATPLVESVNAAVAAVNEQSLLLPEDTYNAVHDAFTKLKSALQAINEDIRTNVAESVAVQYGQASKDLHESFEIRAKSREVELTQQFLNEFNAFKAQLEKHSSEELASALKANEQALLAKQSNEVALLSMKQVEEFTKILSEKLDQERQGRLSKLEALNGSVQELAEAVDQVDTLVMKSEVLSQLSLLTTLLKNKLHAGDESSVKIDSELARLKTLCDILPGRPSKCCSKNPQLLDVVVSQLDSLASQQLILSNEQLYNRWTLLQKDLSTSSLLPPNAGILGHISAKIFGFFLFNKNGAPVDNDIDSVIARVGQNLRLSKLDKAVEEVVALKGWPRVLCDEWVQEARKKLEIETLIDALDCEIRSS | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58100
Sequence Length: 527
Subcellular Location: Mitochondrion inner membrane
|
Q7SFD8 | MLRTSLRSVRALGSRPSAAVAGRQWQATVVRRAAVSGQRFFADDKKPVVPEPSQPAVLPASETLTSPSTPPPASPQVEPTSTVPPETTPLTPPTPEATVIPPVAEEPVVPPTLPTPRKKKGFFRRLRNFFLSLTILGAIAFGGGVYYSRINDAFHDFFTEYIPYGEQAVLYLEELDFKKRFPDVVSRVTGRPRDSGEQVKVPAQSGASWRVASGGEPAGRQSSSIKKAGAAAQDAVPKSEPAVVAAAKEDTAELPKTEATTTATPAEPAPAPAATDASGTPVKKPFKAPEVDEPSRWPPASPIDPLTVNGATDPIVQDLVKMLNDVITVINHDNANEKYAPTICKAKNELSKVADKINEMKAKVEADAAKQVKARVDGFDKAANELVSRVESAMAAQEAAWRREFEEEITRLKKSYDEKVHLIQDREHQIAEEKLNNRLLEQAIQLQRQFTENIKKHVEQERDGRLGKLNELHKAVAELERLTSGLNEVVDTNLRTQQLHVAVDAVRASLEDAHHPRPFIKELVALKEIAADDPVVDAAIASINPTAYQRGIPTTAELIDRFRRVATEVRKASLLPEDAGVASHASSYVLSKLMFKKEGLAAGDDVESILTRTQTYLEEGDLDNAAREMNGLKGWAKTLSRDWLGEVRKVLEVQQALDVIQAEARLQSLRVE | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73443
Sequence Length: 672
Subcellular Location: Mitochondrion inner membrane
|
Q0V4H8 | MLRASILRASPAVRPLARQTRPQWRVVQRCYADNKNLGETAVPNPAPTVTPSSTEKATIPSSDIPKPPPAPETAGASRSAPTIQPATTPPTGPGSASIAPDPKQPKPKKKGRIRRLLFWLTILSGLGYAGGVWYSLVSDNFHDFFTEYVPYGEDAVAYFEEREFRKRVPWPCWDSPRLQPQNLVRRTSSSILRPQWAEWRVLPTRATATSGTKGPHTIANVQEKKQEAAQTATVVKEEAAAPAPAKPVNHLDHLAVPDANDAVVQDVVKIVNDIITVINADSAHDGKYNSALDKAKSELGRVVSDINLMKANLRKESEEKVKSAHDEFEQAAKELVQRLDHQMQAQEAHWKEEFENERERLSQTYKDRLRSELEAAEKVYEQKTKNELLQQSIHLQKSFTASVRERVEAERDGRLGKLNELSSSVHELEKLTAEWNSVVDANLKTQHLVVAVEAVKSALETQATPKPFVTELAALKEIAADDPVVSAAIASINPAAYQRGIPSPALLIDRFRRVAAEVRKAALLPEDAGVASHIASLAMSKVLFKKSGLAVGQDVEAVLARTEVLLEEGDLDAAAREMNGLQGWAKVLSKDWLGECRRVLEVRQALDVIATEARLNSLLVD | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68438
Sequence Length: 621
Subcellular Location: Mitochondrion inner membrane
|
A5D9S8 | MLRARFSTSRSVLTKVVTPPPVVPPVLPPPVKPPKKSFSLPKFLFSATLIGSLAYGGTLYVATKNEKVMDYVIDYQPPFYEEILRMIETGSIDEIRDAWDSLRDRISNVDFSSSKSKIDKFANDLENRGEQLIQKTRQRWGQDTAPTPHEQLQKPVETTQKSPESLPLLSYKGINESVHATVASFNELIKSIDISGPGSNDLVKAIQDNVAKLSQKVDALTASFDDELKKNLKVSQNELLSSYTKKELELTENLLHQYNTERAQLEKKLNARLEQEIASAKEAISQAAVNAVTMVRIEQTKNFEKLVKDKVDGERSGRLANLDKLSSRLDELEQFAESLEQQIVANHNRSTINRSLAELRSLISSTEGTTPKSLAPYLGQLIEAVRPINDELIDATLKEIVPLLQHESSHSILSTSQLLARWELLSPELRSASLLPPNAGLLGHFTSFVFSKLLLPVKGAKPNGKDIESVIGRVEANLVRNELDLAVEEAASLKGWPRKLADDWVVEARKRLEAEFLLGLIEGEVRSL | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Plays a role in keeping cristae membranes connected to the inner boundary membrane. Also promotes protein import via the mitochondrial intermembrane space assembly (MIA) pathway (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58844
Sequence Length: 528
Subcellular Location: Mitochondrion inner membrane
|
P30290 | MDSSTTIPITPTRTPCFFNISSSFNEHSPLNFYDEPIYNFSSGHEENQSHKSSKLTFFKPSNTKRSPHTPMQNNAKAIRLSTTVRHGIFKNSDLDGCSKPFAFSSGLKLSKKIVDASTPIDLKRKRAVTSLSTGLLSKREKWSLWEGNLTNPRSEQPHTPCKKGTKIKLKPPQSPLSPTTSLLARKCKHIDLDTFSRLDHPNSDSSDETFEMEELPSLSYGSEDLLEFCETPCKSQPIFLSSSHVNNWDEKDVPSSLSWTPTSPIFLNINSADDYEEEEDWTSDLRIRFQQVKPIHESDFSFVYHVSSINPPTETVYVVKMLKKNAAKFTGKERHLQEVSILQRLQACPFVVNLVNVWSYNDNIFLQLDYCENGDLSLFLSELGLLQVMDPFRVWKMLFQLTQALNFIHLLEFVHLDVKPSNVLITRDGNLKLGDFGLATSLPVSSMVDLEGDRVYIAPEILASHNYGKPADVYSLGLSMIEAATNVVLPENGVEWQRLRSGDYSNLPNLKDLLLSKEKVQINKVRCAESLQCLLQRMTHPYVDCRPTTQDLLAMPEMIFISEHSQKAAIIYEDHNSWLET | Function: Protein kinase that acts both on serines and on tyrosines. It acts as a negative regulator of entry into mitosis (G2 to M transition). Phosphorylates and inhibits cdc2.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 65934
Sequence Length: 581
EC: 2.7.11.1
|
Q93Z01 | MTLNPPPSQQTSHSPRRIPNRRVLIVGNYCHDVLIQNGSVVAETLGGAASFISNVLDSSSVSCDLVSKVGHDFRYEVTHSPIVAPEKETTVFEAYFDLGIDGIGHADRVLKRVSACDPILPSDIPDSRFDFGMAVGVGGEILPETLEKMVEICDVVAVDIQALIRVFDPVDGAVKLVDLKESGFYHILHRIGFLKASSDEALFMDVEQMKHLCCVVVTNGEKGCRIYHKDDEMTVPPFLAKQVDPTGAGDSFLGGLIVGLVEGLTVPDAALLGNLFGSITVEHIGQPKFDLMMLQKVKDEVQRRKKQCNISSSHNNDHNEFHERLSPARFSCVDSQLQPKLLVNGHSCDDRSL | Function: Kinase that phosphorylates myo-inositol to produce multiple myo-inositol monophosphates. Participates in phytic acid biosynthesis in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Catalytic Activity: ATP + myo-inositol = 1D-myo-inositol 3-phosphate + ADP + H(+)
Sequence Mass (Da): 38646
Sequence Length: 353
EC: 2.7.1.64
|
Q5GA22 | MPLAAEPDDAHEERENQQLLITTKGGPGLEGLVVGSYCHDVLIRGGRIVGETLGGAAAFVSNVLDAASPQGAALNETSPFVVVAKVGHDFIYARAPASARHPPLLCSSPTTSFHAQFSETAASAHAPDRELRRVRACDPIYPADLPDRRFAYGLAVGVAGEVLPETLEQMIRLCRTVLVDAQALIRAFDGDGAVGHVALGDTPYARLLPRVAFVKASSEEAPYVGVETTRRQCCVIVTEGRDGCRLYWDGGEAHVAPFPAVQVDPTGAGDSFLAGFAAGLLWGLSATDAALLGNFFGAAAVSQVGVPTFHPKMLQAVKEILEEKTRKRSSPCMNGASFTLEKSNMHNELHAALQEAAVLMSEQQQADPANGSGGDICSA | Function: Kinase that phosphorylates myo-inositol to produce multiple myo-inositol monophosphates, Ins(1)P, Ins(3)P, Ins(4)P, Ins(5)P and Ins(6)P. Participates in phytic acid biosynthesis in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Catalytic Activity: ATP + myo-inositol = 1D-myo-inositol 3-phosphate + ADP + H(+)
Sequence Mass (Da): 39898
Sequence Length: 379
EC: 2.7.1.64
|
Q84R36 | MAPSPAAAMPLAAEPDEVVVEVEEEEERGVKGGGGVAGLDEVEGLVVGSYCHDVLLRGGRVVGETLGGAAAFVSNVLDAASPAGASLAVVSKVGHDFAYATAAAPARHPPVLCASPTTSFHARFSDDAASAHAPDRQLRRVHACDPIYPADLPDRRFAYGLAVGVAGEVLPETLERMIRLCRAVLVDAQALIRAFDGEAKGGGAVRHVALEATPYARLLPRVAFLKASSEEAPYVGVETARRRCCVIVTEGRDGCRLYWDGGEARVAPFPAVQVDPTGAGDSFLAGFASGLLWGLSATDAALLGNFFGAAAVSQVGVPTFDPKMLQAVKQILEKAVKRPCTHINGNTFTFQRSSMHDELHKSLQEAAMLVCEQKQANSPATDNGDVCSINELTSLPS | Function: Kinase that phosphorylates myo-inositol to produce multiple myo-inositol monophosphates. Participates in phytic acid biosynthesis in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Catalytic Activity: ATP + myo-inositol = 1D-myo-inositol 3-phosphate + ADP + H(+)
Sequence Mass (Da): 41540
Sequence Length: 397
EC: 2.7.1.64
|
G3JUI7 | MTTVPTTQRAVVVGPEDGSVVVAESIPLPDIEPDAVLVQVSAVALNPVDTKMMPGFLNPGNVLGLDFAGTVVAVGPAQPAWRSLQVGDRVFGCTDGCDSRRPRVGAFTQFTACRGSILIKMPDHMSFATAASMGNAIFSSGFALFHSLQLPGSLTATAEKSHWVLIYGGATATGTMALQFLRRAGHKPIAVCSAKHFDMAREYGAVAAFDYHSESHVQEIRDLTKNALSFAFDCVTTQSSVLACEEAMGRLGGRYTALDPFDPTLVSRKAVKLDWILTLTLMGRGSVWPKPFGCEPDEALLTWGTKLAEVAEGVLAEGDHVLKAHPMRIMEGGLDAIPSGIDAIRQGQVRGFKLVYLL | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus . The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units . Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction . The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B .
Catalytic Activity: acetyl-CoA + 3 AH2 + 18 H(+) + 10 malonyl-CoA + 8 NADPH = 3 A + 10 CO2 + 11 CoA + cordypyrone A + 8 H2O + 8 NADP(+)
Sequence Mass (Da): 38191
Sequence Length: 358
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
|
G3JUI6 | MAIHAAYIFIAATLIALYVARRMREQHARQKLARDQGCEPLTTAINKLPYGLDRKWQIVTHRGNILDDLITTRFAELGCYIYTDNQWGSPPIICAEPATMKAVLSTKFRDWDMDSNRYPALGPWLGRGVLVSSHQGKGSLWATARALLRPMFANTATYNHALIEPSVQEFLSILGHLNQAGAPDKDLLPFIRRLNVDIITTVFCGGSINEQQSGLAIAVGADAKHRKPVLEEAFDTIEPIAGLRLQTGSMYWLFTSKPFRDGCETFTGLADGWINRALSKRDEKPDLSQDEGAAAREKNFTEELVSSTDDRELLRDILVQLLFAGIDTSTSMLSFALVELGRHPSAWARLRAELAAHNMLSGGPETITAAQLKECAFLQNIIKETLRLYPPVPINSREAIRDTVLPSGGGADGSKPVFVPKGTSLKYSPYVMHRREDLYGPDALLWNPDRWIGRAPGWDYLPFNGGPRVCIGQKFALSSSAYVLARLAQQFDTCTALPTTGPIDSKLGAVLVPKAGVPVSLTNSTT | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus . The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units . Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction . The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B .
Catalytic Activity: cordypyrone A + O2 + reduced [NADPH--hemoprotein reductase] = cordypyrone B + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57878
Sequence Length: 526
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
|
Q8N3F8 | MAGPRGALLAWCRRQCEGYRGVEIRDLSSSFRDGLAFCAILHRHRPDLLDFDSLSKDNVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFCSPGQAGVSPPRKGLAPCSPPSVAPTPVEPEDVAQGEELSSGSLSEQGTGQTPSSTCAACQQHVHLVQRYLADGRLYHRHCFRCRRCSSTLLPGAYENGPEEGTFVCAEHCARLGPGTRSGTRPGPFSQPKQQHQQQLAEDAKDVPGGGPSSSAPAGAEADGPKASPEARPQIPTKPRVPGKLQELASPPAGRPTPAPRKASESTTPAPPTPRPRSSLQQENLVEQAGSSSLVNGRLHELPVPKPRGTPKPSEGTPAPRKDPPWITLVQAEPKKKPAPLPPSSSPGPPSQDSRQVENGGTEEVAQPSPTASLESKPYNPFEEEEEDKEEEAPAAPSLATSPALGHPESTPKSLHPWYGITPTSSPKTKKRPAPRAPSASPLALHASRLSHSEPPSATPSPALSVESLSSESASQTAGAELLEPPAVPKSSSEPAVHAPGTPGNPVSLSTNSSLASSGELVEPRVEQMPQASPGLAPRTRGSSGPQPAKPCSGATPTPLLLVGDRSPVPSPGSSSPQLQVKSSCKENPFNRKPSPAASPATKKATKGSKPVRPPAPGHGFPLIKRKVQADQYIPEEDIHGEMDTIERRLDALEHRGVLLEEKLRGGLNEGREDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEYELRCLLNKPEKDWTEEDRAREKVLMQELVTLIEQRNAIINCLDEDRQREEEEDKMLEAMIKKKEFQREAEPEGKKKGKFKTMKMLKLLGNKRDAKSKSPRDKS | Function: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 93441
Sequence Length: 863
Domain: Probably exists in a closed and an opened conformation due to interaction of the C-terminal RAB-binding domain (RBD), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, with the N-terminal calponin-homology (CH) domain. The conformational change is regulated by RAB13 and may modulate MICALL1 interactions with functional partners.
Subcellular Location: Recycling endosome membrane
|
Q8BGT6 | MAGPRGALLAWCRRQCEGYRGVDIRDLSSSFRDGLAFCAILHRHRPDLLDFQSLSKENVFENNRLAFEVAEKELGIPALLDPNDMVSMSVPDCLSIMTYVSQYYNHFTSSGQAAASPPKPGKDPAPPSPTSTSPAVQPGEEAQGDDLSPDSLSEQGKQQPPSSACAACGQRVHLVQRYLAEGRLYHRHCFRCRQCSSTLVPGSYSSGPEEGTFVCAERCTRLGPGSRSGTRLLSQQRQQPAAAEAKDAEDNDPSLSVAAVAEADRLQASSEVQFHTPTKPPLPSKPQELASPPGGRPTPAPRKASESSALTPPTPRPRSSLQQDGTVEQSVSSGLVNGRLQEPPVPKPRGTPKLSERMAAPRKDPPWITLVQTEPKKKPAPQPPSSGPGPLSQAYRQVEDGGLEEQTQKSSGTEPEPKPYNPFEEEEEEEGEPAPPVPSPSLAPPVPSPSPAPPVPSPAPAPSEATPKSLHPWYGITPTSSPKTKKRPAPRAPSASPLAIHASRLSHSEPPSATPSPALSVESLSSESSSHTANAEPLEPPAVPKSSSDPAVHVPGTPGTSGNSVTPSANSSLSSSGELGQPSGEQMLQARTKGSAGTHSTKPFSGATPTPFLLAGDRNPAPPVGSASPQLQIKSSCKENPFNRKPSPSASPTVRKATKGAKPVRPPAPGHGFPLIKRKVQADQYIPEEDIYGEMDNIERQLDALEHSGVLLEEKLRGGANEGSEDDMLVDWFKLIHEKHLLVRRESELIYVFKQQNLEQRQADVEFELRCLLNKPEKDWTDEDRAREKVLMQELMTLIEQRDAIVNCLDEDRQREEEEDKMLETMIKKKDFQREAESDSKKKGKFKTIKVLKFLGNKREAKSKAPGDKS | Function: Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94079
Sequence Length: 870
Domain: Probably exists in a closed and an opened conformation due to interaction of the C-terminal RAB-binding domain (RBD), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, with the N-terminal calponin-homology (CH) domain. The conformational change is regulated by RAB13 and may modulate MICALL1 interactions with functional partners (By similarity).
Subcellular Location: Recycling endosome membrane
|
Q3TN34 | MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDAEDMVALKVPDRLSILTYVSQYYNYFHGRSPIGGMAGIKRPSSDSTEELSGKKGLSQPAKLPSPAQTQRSPLSPARTNPVVQRNEGGSQRPSPKAAPGTAGSSVSSICGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHHSSEVTSVSPKSSNLASRKPGGVTADTRPFGVSWTVQEANGEGTPLRVRTAAWEHAGGNTTAKGFVQTELKPPSTSQVHVGSSAGPKLPTITVTTTSVTSKALTHVTNSSPIGWSSPAQSSPANFNSRPVVSPSARNTHLPGSQGQTASKGVKTQLNLNSESSNTAVTPAWTSSASKTQQAREKFFQTPPSAPAPASAPAPAPTSKVPTVVTVPTSKVPNVVTAPTSKVPTVVTVPTSKVPTVVSAPTSKVPTVVSAPTSKVPTVVNSTNSRVTTVVNAPTSKVPTVVSATNGRVPTVVTAHTGRVPAVMNTSASKVSPVVDAPAQESSREQALSVLRKALPALTGSGTQAPNRSFPATSSVLVTLPKNEVPQKVPSDKLSALTTQTPNFTIKLEPSAPVNVGNTAVFLQAGKKSPSISPRVGKTSVGSRPQAEVAGVKGPGPISQEGQEEGPEGWRARLKPVDKKTPAGRSLEQKEPVLAEPRIGDTSRKASSSSDSSVHITLTSIQHKRKPCPAGSGPSPAALSPSPSHRKKLAVPPSLDVSADWLQPEPKKQEDGTRSCKEEKSPTRWSRERSAVLDSGLAPPGEAVTSPVRLHPDYIPQEELQRQLQDIESQLDALELRGVELEKRLRAAEGDASEDSLMVDWFRLIHEKQLLLRLESELMYKSKDQRLEEQQLDLQGELRRLMDKPEGLKSPQDRQREQELLSQYVNTVNDRSDIVDFLDEDRLREQEEDQMLENMIQNLGLQRKKSKSFLSKIWSSKSKSGQA | Function: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 108288
Sequence Length: 1009
Domain: Probably exists in a closed and an open conformation due to interaction of the C-terminal coiled-coil domain with an N-terminal region including the calponin-homology (CH) and the LIM zinc-binding domain. The conformational change is regulated by RAB13.
Subcellular Location: Cell membrane
|
Q8HWE5 | MKASSGKPREFRPAVLLLILGLLLRDSRGSSIQGFLADVEVHGSSRLTRTHTLRYNVRAHSLEGSEKTQLLVLIYVDEELFLKYNGDSRETEPLGCWIKGHGGNETCARETNNLLKVEEKLRGMMAEVINQKSQEEGLHTLQATLGCELLSNGSTRGFWHLGYDGQNFLTFDQKTLTWTVDGPSTQQNKMFWKTHAPRADLVKTFLDDICPAHLQRYLASLRNGLQDTGPPMVTVTCRNYPVGRVTLTCRAFNLYTREATLVWLQDGKPVQQKTFRSETILPSGDGTYQARVSIRVLPGQEPQFSCNLRHGNHSIMQTAVSGHAAEDSQDVASSATASAGSALPVVLAVALARAN | Function: Binds to heparan sulfate proteoglycans on the surface of fibroblast (NIH-3T3) cells.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 39224
Sequence Length: 355
Subcellular Location: Cell membrane
|
F4KDA5 | MWKLTRRLQPHINSTRWLVRNFRNGGAGDATGLYGFDHLKTAKGFQRFVADAIERSGELVSYISGMPSSPEIIKAMDEISDTVCCVVDSAELCRQTHPDREFVEEANKAAIEMNDYLHHLNTNHTLYAAVKKAEQDSNLLTKEASRTAHHLRMDFERGGIHLDPEKLDKVNNLTTNIFQLCREFSENIADDPGHVDIFPGSRIPRHLHHLLNPTYRSTSGGSRGSTRSAHKSKQKGFRINTDPRTVSSILQWTSDEEVRKMVYIQGNSVPHANHGVLEKLIAARHELSQMMGCNSYADIMVEPNLAKSPKVVTSFLQELSKTVKPKADEEFIAIRDFKREKCGNPSAELEPWDETYYTSMMKSSINDVDTAVVASYFPLPQCIEGLKVLVESLFGATFHTIPLAPGESWHPNVVKLSLHHPDEGDLGYLYLDLYSRKGKYPGCASFAIRGGRKISETEYQLPVIALVCNFSRACDSSIVKLNHSEVEVLFHEFGHALHSLLSRTDYQHFSGTRVALDLAEMPSNLFEYYAWDYRLLKRFARHYSTGETIPEKLVNSLQGARNMFAATEMQRQVFYALIDQMLFGEQPETARDVSHLVAELKRQHTSWNHVEGTHWYIRFSHLLNYGAGYYSYLYAKCFASTIWQSICEEDPLSLNTGTLLREKFFKHGGAKDPAELLTDLAGKEIISVHGEGIVPATTYLLNELRL | Cofactor: Binds 1 zinc ion.
Function: Aminopeptidase which cleaves preproteins, imported into the mitochondrion, to their mature size. Could cleave both preproteins and preprotein intermediates already cleaved by the mitochondrial processing peptidase (MPP).
Sequence Mass (Da): 79925
Sequence Length: 706
Subcellular Location: Mitochondrion
EC: 3.4.24.-
|
P28238 | MRELRSSSFWRAILAEFLGSLLYTLLGLGASLRWAPGPHGVLGSALAFGLAQATLVQALGHVSGGHINPAITLAFLLASQLSLPRALGYLLAQLLGALAGAGVLYGVTPAAVRGTLGLSALHPSVGPGQGTVVELLLTAQFILCVFASFDDRHDGRPGSAALPVGFSLALGHLFGIPFTGAGMNPARSFAPAVITRNFTNHWVFWAGPLLGAALAALLYELALCPRARSMAERLAVLRGEPPAAAPPPEPPAEPLELKTQGL | Function: Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27072
Sequence Length: 262
Domain: Aquaporins contain two tandem repeats each containing two membrane-spanning helices and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Each tandem repeat contains a loop and a short helix that enter and leave the lipid bilayer on the same side (By similarity).
Subcellular Location: Cell membrane
|
P26623 | MKNILSWMLMFAVALPIVGCDNGGGSQTSATEKSMVEDSALTDNQKLSRTFGHLLSRQLSRTEDFSLDLVEVIKGMQSEIDGQSAPLTDTEYEKQMAEVQKASFEAKCSENLASAEKFLKENKEKAGVIELEPNKLQYRVVKEGTGRVLSGKPTALLHYTGSFIDGKVFDSSEKNKEPILLPLTKVIPGFSQGMQGMKEGEVRVLYIHPDLAYGTAGQLPPNSLLIFEVKLIEANDDNVSVTE | Function: PPIases accelerate the folding of proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 26663
Sequence Length: 243
Subcellular Location: Cell outer membrane
EC: 5.2.1.8
|
P51752 | MKRLILPFLSVGLLLGTTAHAATPLKTEQDKLSYSMGVMTGKAFRKHDIKIDPQTFSMGLSDAYLGKETQMTEAEMRQTLQQFEKQSLQKMQHKMKQTAQQNAEKSRAFLTANKNKPGVKTLANGLQYKVLQAGQGQSPTLNDEVTVNYEGRLINGTVFDSSYKRGQPATFPLKSVIKGWQEALTRMKPGAIWEIYVPPQLAYGEQGAPGVIGPNEALIFKVNLISVKKK | Function: May be an essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 25518
Sequence Length: 230
Subcellular Location: Secreted
EC: 5.2.1.8
|
P30301 | MWELRSASFWRAIFAEFFATLFYVFFGLGSSLRWAPGPLHVLQVAMAFGLALATLVQSVGHISGAHVNPAVTFAFLVGSQMSLLRAFCYMAAQLLGAVAGAAVLYSVTPPAVRGNLALNTLHPAVSVGQATTVEIFLTLQFVLCIFATYDERRNGQLGSVALAVGFSLALGHLFGMYYTGAGMNPARSFAPAILTGNFTNHWVYWVGPIIGGGLGSLLYDFLLFPRLKSISERLSVLKGAKPDVSNGQPEVTGEPVELNTQAL | Function: Water channel . Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core (By similarity). Plays a role in cell-to-cell adhesion and facilitates gap junction coupling .
PTM: Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28122
Sequence Length: 263
Domain: Aquaporins contain two tandem repeats each containing two membrane-spanning helices and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Each tandem repeat contains a loop and a short helix that enter and leave the lipid bilayer on the same side (By similarity).
Subcellular Location: Cell membrane
|
Q0U3N7 | MSSITETFGVRIDATNSLVQAAIYGFLLAGVAAFAAPIVSTIRVLLSLFVLPGKSLSSFGPRGTWALITGASDGIGKEFALALAAKGYNLILVSRTQSKLDSLAADISSKYGPKISTKTLAMDFAQNKDSDYNNLKKLVDGLDVSILINNVGLSHSIPVPFAETPKQEMTDIIMINCMATLRVTQLLTPGMISRKRGLILTMASFGGFFPTPLLATYSGSKAFLQQWSSALGSELEPHGVHVQCVQSHLITTAMSKIRKPSALVPNPKQFVKATLSKLGRSGGAQNVAFTSTPYWSHGIMQWFLSRFLGERSPIVVKINRGMHEDIRRRALRKAERDAKKQ | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36959
Sequence Length: 341
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.330
|
Q10245 | MDGEVLANKSCCGAVVTAFSVIGIVFTILKFTSFASFVYKTFFAKGVKLSVYGAKKGYWAVVTGATDGIGKEYATQLAMSGFNVVLISRTQEKLDALAKELETVAKVKTRTIAIDYTKTTAETFEKLHQDLVGTPITVLINNVGQSHYMPTSFAETTVKEMDDIMHINCFGTLHTTKAVLSIMLRERQKNEKGPRCLILTMGSFAGLLPSPYLSTYAGSKAFLSNWSASLGEEVKKQGIDVWCFNSYLVVSAMSKVRRPTLTIPTPKKFVRAALSSIGLQRGGTNPYISQPYPSHAVMSWSLEQLLGSAKGFVVSQVAAMHLSIRKRALRKEARLQAQNQA | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37307
Sequence Length: 341
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.330
|
Q4P622 | MAIEQHIDGLLRHVGLRVDHGLTPVSASLVLLAGIGALSVGTFALRLVRLFADVYILPGNSVSKYGANKKDLTRASWAVVTGATDGIGREFALQLARKGFNIVLVSRSPEKLGSVAAEIEAATPGVRTKTQAIDFALGDERQYEGLEHTVKGLNVGVLVNNVGKSHNMPVTFTETSEEEMEDIIEINVVSVLRVSKMIIPGMVDRKRGLVLNLGSFAGQVTTPMLATYAGSKAFLSGWSQALGEEVKRSNVDVSLLNTYFVVSNLSKIRKSSAMIPTPKQYVTQVLKTLGRNGGAVGRPYTATPWPGHALVDWATTFVLPRGWLLSYTYGQQVATRKRALNKAHKAVKSA | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37725
Sequence Length: 350
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.330
|
P38286 | MTFMQQLQEAGERFRCINGLLWVVFGLGVLKCTTLSLRFLALIFDLFLLPAVNFDKYGAKTGKYCAITGASDGIGKEFARQMAKRGFNLVLISRTQSKLEALQKELEDQHHVVVKILAIDIAEDKESNYESIKELCAQLPITVLVNNVGQSHSIPVPFLETEEKELRNIITINNTATLLITQIIAPKIVETVKAENKKSGTRGLILTMGSFGGLIPTPLLATYSGSKSFLQGWSNSLAGELSKDAIDVELIISYLVTSSMSKIRRSSLMIPNPQQFVKSTLRSVGRRCGSQERYATMTPYWAHAVYQFVITETFGVYSKIVNSINYSFHKSIRIRALKKAARQVKKE | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 38708
Sequence Length: 347
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.330
|
Q5AAG6 | MDQQEAPIYYGRSVNKVYNQEFIIDSRFKIVKELGHGAYGIVCSAKYDNGSKKVPDSNNGNASSSANASFVAIKKITNIFSKNILCKRALRELKLLQFFRGHKNITCLYDLDIIPNPMTGEFNEIYLYEELMECDMHQIIRSGQPLSDQHYQSFIYQVLCGLNFIHSADVLHRDLKPGNLLVNADCELKICDFGLARGFSENPDENAGFMTEYVATRWYRAPEIMLSFTNYTKAIDIWSVGCILAELLGGKPLFRGKDYVDQLNQILMILGTPPESTLQRIGSHRAQNYVRSLPITRKASYEELFPDANPLALDLLERMLTLDPRERITVRDALNHKYLELWHDPKEEIECQVKFDFKSFETVDGLDEMKQLIMDEVQKFREFVRKPIEEQQRIQMQLHMQKREEQRQEEEEKELLEQQRQFPAQESMDISQTPYNNLETNIGTPQVEDDYPRPQELDEFTFSNLESSSSMNLFQDMAKPSGEEYIKLEEELGFGLDGAMFNNYCNDHQ | Function: Serine/threonine protein kinase component of the cell integrity pathway, a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. Participates in cell wall construction, azole resistance, and host interaction. Required for the signaling for invasive filamentous growth and biofilm formation, and plays a crucial role in virulence.
PTM: Activated through phosphorylation of Thr-211 and Tyr-213 from the TXY motif (By similarity). Phosphorylated in a PKC1-dependent manner in response to cell wall perturbations, oxidative stress, osmotic stress, and low temperatures. Also activated in response to physical contact leading to contact-dependent cellular behaviors such as invasive hyphal growth and biofilm development. Phosphorylation is also PBS2- and HOG1-dependent.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 59036
Sequence Length: 509
Domain: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
EC: 2.7.11.24
|
P53379 | MKLSVLTFVVDALLVCSSIVDAGVTDFPSLPSNEVYVKMNFQKKYGSSFENALDDTKGRTRLMTRDDDYELVELTNQNSFYSVELDIGTPPQKVTVLVDTGSSDLWVTGSDNPYCSTKKKDTTGSSFKQVNKDALASVVESVFTEISYDTTIVTSEATATFDSTASTSQLIDCATYGTFNTSKSSTFNSNNTEFSIAYGDTTFASGTWGHDQLSLNDLNITGLSFAVANETNSTVGVLGIGLPGLESTYSGVSLSSVQKSYTYNNFPMVLKNSGVIKSTAYSLFANDSDSKHGTILFGAVDHGKYAGDLYTIPIINTLQHRGYKDPIQFQVTLQGLGTSKGDKEDNLTTLTTTKIPVLLDSGTTISYMPTELVKMLADQVGATYSSAYGYYIMDCIKEMEEESSIIFDFGGFYLSNWLSDFQLVTDSRSNICILGIAPQSDPTIILGDNFLANTYVVYDLDNMEISMAQANFSDDGEYIEIIESAVPSALKAPGYSSTWSTYESIVSGGNMFSTAANSSISYFASTSHSATSSSSSKGQKTQTSTTALSISKSTSSTSSTGMLSPTSSSSTRKENGGHNLNPPFFARFITAIFHHI | Function: Cleaves proteins C-terminally to the most C-terminal basic residue. Can process the alpha-mating factor precursor. Required for cell wall integrity.
Catalytic Activity: Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non-prime and prime positions.
Location Topology: Lipid-anchor
Sequence Mass (Da): 64269
Sequence Length: 596
Subcellular Location: Cell membrane
EC: 3.4.23.41
|
Q54MY9 | MDNNSTLNNITITVASSHNNTTTNSNNNNNNNNGSNSNNNNEQLNTLSNSITSLKSLNISGSGVITNNSEVNTPSEGNITPLPLLSLSDALSPLRELYSCLYVGDIRALMSNQYLKFEENEKIRILGFPEPHLEIDEKTQKYFSYQIIEFESDEDILSIAKSFEQYSQLILGRTPTQPVVIQECCFGLVLASIYFIKYELFSLPQAHDLIGYNDFFGTSKKHSHFEKVDSCTLINDITSYYYNNMSSKRKTTIFSNNISFTNLQTTTPPTTTTTTTTTTTTSSSNNSEQIESTSKNNSSGITSPTSIKPKNKVGLLKKLFNKMDKESSNNNNNKEKVEKIKEKKESKKEREAREAKEEKEREEREKEHQLALKNIPPAELYKHHMEQIQKIQKQQIAELNATSPDGGNDLSNGSNGSKNGNNNNNNNNSNNNNNNNNSNEPNSQHQNHNPITNLMDQELIENYDDGSDRMKNSKTIISPNFESLPDEYKTMVKTWDIKQESVDEHFEIILSLLHFHTKQRFYSSDPTNLPDKPKYYNVGNVCGNCTPPMILDPAGSGQMVVAKSFYKRPFDQICKKPTNEMKKLYTFREKVGKGGFGTVYLVRNNMDKSKSRIAIKKLPHVRKKEKKFNVKEIRVLEFTNHPNIITYYNSHMLHDEVWIAMEFMEGGTLAEASNQYPFQESNIAYVAREVLQGLAYLHGIQLVHRDLKSQNIMMTTSGEIKLIDFGLCANLSKGERIRMCGSPIWMPPEMIQQKQHGYTCDIWSTAICLLELANRNNKLRKNPIKTMFMVGSEGIKDPFEDPHKWSDEFHDIINKCLQMDPHKRPSAQELLKHPFIQLADNKKKMGKILSSIFLKSIVGI | Function: Coordinates organism morphology with cellular differentiation during development. Negative regulator of sporulation, synchronizing encapsulation with culmination. May have an additional function in prestalk cells.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 97846
Sequence Length: 860
EC: 2.7.11.1
|
P64605 | MQTKKNEIWVGIFLLAALLAALFVCLKAANVTSIRTEPTYTLYATFDNIGGLKARSPVSIGGVVVGRVADITLDPKTYLPRVTLEIEQRYNHIPDTSSLSIRTSGLLGEQYLALNVGFEDPELGTAILKDGDTIQDTKSAMVLEDLIGQFLYGSKGDDNKNSGDAPAAAPGNNETTEPVGTTK | Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 19576
Sequence Length: 183
Subcellular Location: Cell inner membrane
|
P45029 | MRQTIKYEFWVGLFLLLGIGALVFLGLRVANVQGFAETKSYTVTATFDNIGGLKVRAPLKIGGVVIGRVSAITLDEKSYLPKVSIAINQEYNEIPENSSLSIKTSGLLGEQYIALTMGFDDGDTAMLKNGSQIQDTTSAMVLEDLIGQFLYGSKKSDGNEKSESTEQ | Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 18111
Sequence Length: 167
Subcellular Location: Cell inner membrane
|
P45030 | MIVNFISALGKQVIDFFRALGRAGFMLFGALIGKPQIRKHFPLLVKQMHVLGVQSLLIILLSGLFIGMVLGLQGYVVLIDFSAETSLGQLVALSLLRELGPVVTALLFAGRAGSALTAEIGLMKATEQLSSLEMMAVDPLRRVIAPRFWAGVISMPVLSILFIAIGIWGGSLVGVDWKGVDSGSFWSVMQNSVSWSYDILNGFIKAVFFAVAVTWIALFNGYDCMPTSEGISQATTRTVVHASLVVLGLDFILTAIMFGAG | Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28015
Sequence Length: 261
Subcellular Location: Cell inner membrane
|
P45031 | MNQNLIEVKNLTFKRGDRVIYDNLNLQVKKGKITAIMGPSGIGKTTLLKLIGGQLMPEQGEILFDGQDICRLSNRELYEVRKRMGMLFQSGALFTDISTFDNVAFPIREHTHLPENLIRQIVLMKLEAVGLRGAAALMPSELSGGMARRAALARAIALDPDLIMFDEPFTGQDPISMGVILSLIKRLNEALNLTSIVVSHDVEEVLSIADYAYIIADQKVIAEGTSEQLLQSQDLRVVQFLKGESDGPVRFKYPAQDYVKELFE | Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29395
Sequence Length: 264
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
|
Q15049 | MTQEPFREELAYDRMPTLERGRQDPASYAPDAKPSDLQLSKRLPPCFSHKTWVFSVLMGSCLLVTSGFSLYLGNVFPAEMDYLRCAAGSCIPSAIVSFTVSRRNANVIPNFQILFVSTFAVTTTCLIWFGCKLVLNPSAININFNLILLLLLELLMAATVIIAARSSEEDCKKKKGSMSDSANILDEVPFPARVLKSYSVVEVIAGISAVLGGIIALNVDDSVSGPHLSVTFFWILVACFPSAIASHVAAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSIMRIVEMFKDYPPAIKPSYDVLLLLLLLVLLLQAGLNTGTAIQCVRFKVSARLQGASWDTQNGPQERLAGEVARSPLKEFDKEKAWRAVVVQMAQ | Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41141
Sequence Length: 377
Subcellular Location: Membrane
|
Q60HE7 | MTQEPFREELAYDRMPTLERGRQDPASYAPDTKPSDLQLSKRLPPCFSPKTWVFSVLMGSCLLVTSGFSLYLGNVFPAEMDYLRCAAGSCIPSAIVSFTVSRRNANVIPNFQILFVSTFAVTTTCLIWFGCKLILNPSAININFNLILLLLLELLMAATVIMSARSSEEYCKKKKGSMSDGTNILGEVPFPARVLKSYSVVEVIAGISAVLGGIIALNVDDSVSGPHLSVTFFWILVACFPSAIASHVTAECPSKCLVEVLIAISSLTSPLLFTASGYLSFSVMRIVEMFKDYPPAIKPSYDVLLLLLLLVLLLQAGLNTGTAIQCVRFKVSARLQGASWDTQSGPQERLAGEVARSPLKEFDKEKAWRAVVVQMAQ | Function: Regulates the response of astrocytes to hypo-osmosis by promoting calcium influx.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41158
Sequence Length: 377
Subcellular Location: Membrane
|
P10916 | MAPKKAKKRAGGANSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD | Function: Contractile protein that plays a role in heart development and function . Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (By similarity). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity).
PTM: N-terminus is methylated by METTL11A/NTM1.
Sequence Mass (Da): 18789
Sequence Length: 166
Subcellular Location: Cytoplasm
|
P51667 | MAPKKAKKRIEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD | Function: Contractile protein that plays a role in heart development and function . Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (By similarity) . During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly .
PTM: N-terminus is methylated by METTL11A/NTM1.
Sequence Mass (Da): 18864
Sequence Length: 166
Subcellular Location: Cytoplasm
|
P08733 | MSPKKAKKRLEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD | Function: Contractile protein that plays a role in heart development and function (By similarity). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force . During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity).
PTM: N-terminus is methylated by METTL11A/NTM1.
Sequence Mass (Da): 18880
Sequence Length: 166
Subcellular Location: Cytoplasm
|
A5U029 | MVNDLTPHFEDVQAHYDLSDDFFRLFLDPTQTYSCAHFEREDMTLEEAQIAKIDLALGKLGLQPGMTLLDIGCGWGATMRRAIAQYDVNVVGLTLSKNQAAHVQKSFDEMDTPRDRRVLLAGWEQFNEPVDRIVSIGAFEHFGHDRHADFFARAHKILPPDGVLLLHTITGLTRQQMVDHGLPLTLWLARFLKFIATEIFPGGQPPTIEMVEEQSAKTGFTLTRRQSLQPHYARTLDLWAEALQEHKSEAIAIQSEEVYERYMKYLTGCAKLFRVGYIDVNQFTLAK | Function: Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.
Catalytic Activity: 1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32724
Sequence Length: 287
Pathway: Lipid metabolism; mycolic acid biosynthesis.
EC: 2.1.1.79
|
Q7U1K1 | MTRMAEKPISPTKTRTRFEDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERLDVNVIGLTLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGRMTVQSSVSYHPYEMAARGKKLSFETARFIKFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPHYIKTLRIWGDTLQSNKDKAIEVTSEEVYNRYMKYLRGCEHYFTDEMLDCSLVTYLKPGAAA | Function: Involved in the biosynthesis of hydroxymycolate, a common precursor of oxygenated mycolic acids (methoxymycolate and ketomycolate). Probably transfers a methyl group from the S-adenosylmethionine (SAM) cofactor and, subsequently or simultaneously, a water molecule onto the double bound of ethylene substrates, leading to the formation of the hydroxylated product at the distal position.
Sequence Mass (Da): 34636
Sequence Length: 301
Pathway: Lipid metabolism; mycolic acid biosynthesis.
EC: 2.1.1.-
|
Q8IVH4 | MPMLLPHPHQHFLKGLLRAPFRCYHFIFHSSTHLGSGIPCAQPFNSLGLHCTKWMLLSDGLKRKLCVQTTLKDHTEGLSDKEQRFVDKLYTGLIQGQRACLAEAITLVESTHSRKKELAQVLLQKVLLYHREQEQSNKGKPLAFRVGLSGPPGAGKSTFIEYFGKMLTERGHKLSVLAVDPSSCTSGGSLLGDKTRMTELSRDMNAYIRPSPTRGTLGGVTRTTNEAILLCEGAGYDIILIETVGVGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVAVTKSDGDLIVPARRIQAEYVSALKLLRKRSQVWKPKVIRISARSGEGISEMWDKMKDFQDLMLASGELTAKRRKQQKVWMWNLIQESVLEHFRTHPTVREQIPLLEQKVLIGALSPGLAADFLLKAFKSRD | Function: GTPase, binds and hydrolyzes GTP . Involved in intracellular vitamin B12 metabolism, mediates the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis . Functions as a G-protein chaperone that assists AdoCbl cofactor delivery from MMAB to the methylmalonyl-CoA mutase (MMUT) . Plays a dual role as both a protectase and a reactivase for MMUT . Protects MMUT from progressive inactivation by oxidation by decreasing the rate of the formation of the oxidized inactive cofactor hydroxocobalamin (OH2Cbl) . Additionally acts a reactivase by promoting the replacement of OH2Cbl by the active cofactor AdoCbl, restoring the activity of MMUT in the presence and hydrolysis of GTP .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 46538
Sequence Length: 418
Subcellular Location: Mitochondrion
EC: 3.6.-.-
|
Q8C7H1 | MTISTLLLSPNRRLLTCLSRVPSPWLLHSSHPAPGPPGALPNCFGHHCTKRVLLSDGFRRTLCVQATLKDHTEGLSDKEQRFVDRLYTGLVKGQRACLAEAITLVESTHTRKRELAQVLLQRVLALQREQELRNQGKPLTFRVGLSGPPGAGKSTFIECFGKMLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVGVGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVIRISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIPLMERKVLSGALSPGRAADLLLKAFKSRH | Function: GTPase, binds and hydrolyzes GTP (By similarity). Involved in intracellular vitamin B12 metabolism, mediates the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis (By similarity). Functions as a G-protein chaperone that assists AdoCbl cofactor delivery from MMAB to the methylmalonyl-CoA mutase (MMUT) (By similarity). Plays a dual role as both a protectase and a reactivase for MMUT (By similarity). Protects MMUT from progressive inactivation by oxidation by decreasing the rate of the formation of the oxidized inactive cofactor hydroxocobalamin (OH2Cbl) (By similarity). Additionally acts a reactivase by promoting the replacement of OH2Cbl by the active cofactor AdoCbl, restoring the activity of MMUT in the presence and hydrolysis of GTP (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 45932
Sequence Length: 415
Subcellular Location: Mitochondrion
EC: 3.6.-.-
|
Q5MFW3 | MAMLLPHPHPDFLKGLLKAPFRCYRFIFHSSTHLGSGIPCAQPFNLLGLHYAKWMLLSDGLKRNLCVQTTLKDHKEGLSDKGQRFVDKLFTGLIQGQRACLAEAKTLVESTHSRKKELAQVLLQKVLLFQREQEQPNKGNPLAFRLGLSGPPGAGKSTFIEYSGKLLTERGHKLSVLAVGPSSCNSGGSLLGDKTRMTEFSRDMNAYIRPSPTRGNLGGVPRTTNEVILLCEGAGYDIILIETVGVGQSEFAVADTVDILFYYCHQLEEMNCRVSKEVYLRWQHGSNNYVCWRLDCASSKDTGRVCDALKLLRRRLAVWRPKVVRISARSWRGGHWNVGYDARILGPNTCQRGAACQTTKATESLDVEPHSGKRVRAFQESPHSPGADSCSGTKGPPWGPGPRASSRFVVEGF | Function: GTPase, binds and hydrolyzes GTP (By similarity). Involved in intracellular vitamin B12 metabolism, mediates the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis (By similarity). Functions as a G-protein chaperone that assists AdoCbl cofactor delivery from MMAB to the methylmalonyl-CoA mutase (MMUT) (By similarity). Plays a dual role as both a protectase and a reactivase for MMUT (By similarity). Protects MMUT from progressive inactivation by oxidation by decreasing the rate of the formation of the oxidized inactive cofactor hydroxocobalamin (OH2Cbl) (By similarity). Additionally acts a reactivase by promoting the replacement of OH2Cbl by the active cofactor AdoCbl, restoring the activity of MMUT in the presence and hydrolysis of GTP (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 45682
Sequence Length: 413
Subcellular Location: Mitochondrion
EC: 3.6.-.-
|
Q58D49 | MAVWGPGGRLGLRGCLGARKLLCPRFQSRGPQGVEDGDRPQPSSKTPKVPKIYTKTGDKGFSSTFTGERRSKDDQVFEAVGTTDELSSAIGFAMELIAEKGHPFVEELQKIQCSLQDVGSALATPRSSAREAHLKHATFEAGPILELEQWIDKYSRQLPPLTAFILPSGGKSSSALHFCRAVCRRAERRVVPLVQTGETDANVVKFLNRLSDYLFTLARYTAMKEGNPEKIYKKNDLSDRT | Function: Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), a coenzyme for methylmalonyl-CoA mutase, therefore participates in the final step of the vitamin B12 conversion . Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor to MUT in a transfer that is stimulated by ATP-binding to MMAB and gated by MMAA (By similarity).
Catalytic Activity: ATP + cob(I)alamin-[corrinoid adenosyltransferase] = adenosylcob(III)alamin + apo-[corrinoid adenosyltransferase] + triphosphate
Sequence Mass (Da): 26587
Sequence Length: 241
Subcellular Location: Mitochondrion
EC: 2.5.1.-
|
Q96EY8 | MAVCGLGSRLGLGSRLGLRGCFGAARLLYPRFQSRGPQGVEDGDRPQPSSKTPRIPKIYTKTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAIGFALELVTEKGHTFAEELQKIQCTLQDVGSALATPCSSAREAHLKYTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGGKISSALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIYMKNDPSAESEGL | Function: Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), a coenzyme for methylmalonyl-CoA mutase, therefore participates in the final step of the vitamin B12 conversion . Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor to MUT in a transfer that is stimulated by ATP-binding to MMAB and gated by MMAA (Probable).
Catalytic Activity: ATP + cob(I)alamin-[corrinoid adenosyltransferase] = adenosylcob(III)alamin + apo-[corrinoid adenosyltransferase] + triphosphate
Sequence Mass (Da): 27388
Sequence Length: 250
Subcellular Location: Mitochondrion
EC: 2.5.1.-
|
Q8N119 | MLAASIFRPTLLLCWLAAPWPTQPESLFHSRDRSDLEPSPLRQAKPIADLHAAQRFLSRYGWSGVWAAWGPSPEGPPETPKGAALAEAVRRFQRANALPASGELDAATLAAMNRPRCGVPDMRPPPPSAPPSPPGPPPRARSRRSPRAPLSLSRRGWQPRGYPDGGAAQAFSKRTLSWRLLGEALSSQLSVADQRRIVALAFRMWSEVTPLDFREDLAAPGAAVDIKLGFGRGRHLGCPRAFDGSGQEFAHAWRLGDIHFDDDEHFTPPTSDTGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLYGSCEGSFDTAFDWIRKERNQYGEVMVRFSTYFFRNSWYWLYENRNNRTRYGDPIQILTGWPGIPTHNIDAFVHIWTWKRDERYFFQGNQYWRYDSDKDQALTEDEQGKSYPKLISEGFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKRITEVFPAVIPQNHPFRNIDSAYYSYAYNSIFFFKGNAYWKVVNDKDKQQNSWLPANGLFPKKFISEKWFDVCDVHISTLNM | Cofactor: Binds 1 zinc ion per subunit.
Function: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway . Cleaves alpha-1-antitrypsin .
PTM: The precursor is cleaved by a furin endopeptidase.
Sequence Mass (Da): 65043
Sequence Length: 569
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
|
O93470 | MPSIKLLVWCCLCVISPRLCHSEKLFHSRDRSDLQPSAIEQAELVKDMLSAQQFLAKYGWTQPVIWDPSSTNENEPLKDFSLMQEGVCNPRQEVAEPTKSPQFIDALKKFQKLNNLPVTGTLDDATINAMNKPRCGVPDNQMAKKETEKPTAAQSLENKTKDSENVTQQNPDPPKIRRKRFLDMLMYSNKYREEQEALQKSTGKVFTKKLLKWRMIGEGYSNQLSINEQRYVFRLAFRMWSEVMPLDFEEDNTSPLSQIDIKLGFGRGRHLGCSRAFDGSGQEFAHAWFLGDIHFDDDEHFTAPSSEHGISLLKVAAHEIGHVLGLSHIHRVGSIMQPNYIPQDSGFELDLSDRRAIQNLYGSCEGPFDTAFDWIYKEKNQYGELVVRYNTYFFRNSWYWMYENRSNRTRYGDPLAIANGWHGIPVQNIDAFVHVWTWTRDASYFFKGTQYWRYDSENDKAYAEDAQGKSYPRLISEGFPGIPSPINAAYFDRRRQYIYFFRDSQVFAFDINRNRVAPDFPKRILDFFPAVAANNHPKGNIDVAYYSYTYSSLFLFKGKEFWKVVSDKDRRQNPSLPYNGLFPRRAISQQWFDICNVHPSLLKI | Cofactor: Binds 1 zinc ion per subunit.
Function: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway.
PTM: The precursor is cleaved by a furin endopeptidase.
Sequence Mass (Da): 70146
Sequence Length: 604
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
|
O75900 | MGRGARVPSEAPGAGVERRWLGAALVALCLLPALVLLARLGAPAVPAWSAAQGDVAALGLSAVPPTRVPGPLAPRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLHRLYGCLDRLFVCASWARRGFCDARRRLMKRLCPSSCDFCYEFPFPTVATTPPPPRTKTRLVPEGRNVTFRCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAHLSIIANAVNEGTYTCVVRRQQRVLTTYSWRVRVRG | Cofactor: Binds 1 zinc ion per subunit.
Function: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43935
Sequence Length: 390
Domain: The ShKT domain associates with, and blocks several potassium channels in the nanomolar to low micromolar range. The relative affinity is Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4 (By similarity).
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.24.-
|
Q9Y5R2 | MPRSRGGRAAPGPPPPPPPPGQAPRWSRWRVPGRLLLLLLPALCCLPGAARAAAAAAGAGNRAAVAVAVARADEAEAPFAGQNWLKSYGYLLPYDSRASALHSAKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERQPRPPRPPLGDRPSTPGTKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCNQKEVERRKERRLPQDDVDIMVTINDVPGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity).
PTM: Cleaved by a furin endopeptidase in the trans-Golgi network.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 73231
Sequence Length: 645
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q9R0S2 | MPRSRGGRAAPGQASRWSGWRAPGRLLPLLPALCCLAAAAGAGKPAGADAPFAGQNWLKSYGYLLPYESRASALHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERHPRPPRPPLGDRPSTPGAKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCKQKEVERRKERRLPQDDVDIMVTIDDVPGSVNAVAVVVPCTLSLCLLVLLYTIFQFKNKAGPQPVTYYKRPVQEWV | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence . Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia . Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence . May play a role in axonal growth . Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin .
PTM: Cleaved by a furin endopeptidase in the trans-Golgi network.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70460
Sequence Length: 618
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q9NPA2 | MRLRLRLLALLLLLLAPPARAPKPSAQDVSLGVDWLTRYGYLPPPHPAQAQLQSPEKLRDAIKVMQRFAGLPETGRMDPGTVATMRKPRCSLPDVLGVAGLVRRRRRYALSGSVWKKRTLTWRVRSFPQSSQLSQETVRVLMSYALMAWGMESGLTFHEVDSPQGQEPDILIDFARAFHQDSYPFDGLGGTLAHAFFPGEHPISGDTHFDDEETWTFGSKDGEGTDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDPDKYRLSQDDRDGLQQLYGKAPQTPYDKPTRKPLAPPPQPPASPTHSPSFPIPDRCEGNFDAIANIRGETFFFKGPWFWRLQPSGQLVSPRPARLHRFWEGLPAQVRVVQAAYARHRDGRILLFSGPQFWVFQDRQLEGGARPLTELGLPPGEEVDAVFSWPQNGKTYLVRGRQYWRYDEAAARPDPGYPRDLSLWEGAPPSPDDVTVSNAGDTYFFKGAHYWRFPKNSIKTEPDAPQPMGPNWLDCPAPSSGPRAPRPPKATPVSETCDCQCELNQAAGRWPAPIPLLLLPLLVGGVASR | Cofactor: Binds 1 zinc ion per subunit.
Function: May activate progelatinase A.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Lipid-anchor
Sequence Mass (Da): 62554
Sequence Length: 562
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q3U435 | MCFPGSQISPARLYYLVSAPWICTGSLTSSRLPRRRESGPLRVPPRSVQAERILRLPAFGLPLLALLLVPLLPVRAQNPDAKVVSMGVEWLTRYGYLPPADPVHAQMQSLEKLQDAIKVMQRFAGLPETGQMDPMTIKTMRKPRCSLPDVLGAAGLVRRRRRYSLSGSVWKKRTLTWSIRSFSQKSQLSPQIVRTLLSYALAVWATESGLTFQEVNSQYQEPDIIIHFARAYHQDSYPFDGSGGTLAHAFFPGEHPISGDTHFDDEETWTFGSTDDNGIDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDPATYRLPQDDRDGLQQLYGRVSQNPNARPTRKPLVPPPQPPAMPPDSPATPVPDRCEGNFDAVANIRGEIFLFKGPWFWRLQPSGQLVSPRPAGLHRFWEGLPTHVKVIQAAYARPLDGRIILFSGPQFWVFQERQLEGAARPLVEFGLPPGEDVDAVFSWPHNGKTYLIRGQKYWRYDEVAARPDPGYPRALSLWDGAPFAPDDVTISNTGDTYFFKGTHFWRFAEGSVKAESDSPQPIGPKWLDCPAPNSDPRVTSPPKTTSKTRSCDCHCELNQASEQLSPLLLPLLPLVAGEVFSY | Cofactor: Binds 1 zinc ion per subunit.
Function: May activate progelatinase A.
PTM: The precursor is cleaved by a furin endopeptidase.
Location Topology: Lipid-anchor
Sequence Mass (Da): 68496
Sequence Length: 615
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q9NRE1 | MQLVILRVTIFLPWCFAVPVPPAADHKGWDFVEGYFHQFFLTKKESPLLTQETQTQLLQQFHRNGTDLLDMQMHALLHQPHCGVPDGSDTSISPGRCKWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLPNSGNPGVVHFDKNEHWSASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYGEKCSSDIP | Cofactor: Binds 1 zinc ion per subunit.
Function: May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.
Sequence Mass (Da): 29708
Sequence Length: 261
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q9H306 | MKRLLLLFLFFITFSSAFPLVRMTENEENMQLAQAYLNQFYSLEIEGNHLVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIMKTPRCGVPDVGQYGYTLPGWRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFRTRVHGRCPRYFDGPLGVLGHAFPPGPGLGGDTHFDEDENWTKDGAGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYGGLPKEPAKPKEPTIPHACDPDLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQYKGFFFFSRGSKQFEYDIKTKNITRIMRTNTWFQCKEPKNSSFGFDINKEKAHSGGIKILYHKSLSLFIFGIVHLLKNTSIYQ | Cofactor: Binds 4 Ca(2+) ions per subunit.
Function: Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens.
PTM: N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59026
Sequence Length: 513
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.4.24.-
|
Q9H239 | MVARVGLLLRALQLLLWGHLDAQPAERGGQELRKEAEAFLEKYGYLNEQVPKAPTSTRFSDAIRAFQWVSQLPVSGVLDRATLRQMTRPRCGVTDTNSYAAWAERISDLFARHRTKMRRKKRFAKQGNKWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFDGPGGALAHAFLPRRGEAHFDQDERWSLSRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYGKPLGGSVAVQLPGKLFTDFETWDSYSPQGRRPETQGPKYCHSSFDAITVDRQQQLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQLCRAGGLPRHPDAALFFPPLRRLILFKGARYYVLARGGLQVEPYYPRSLQDWGGIPEEVSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGCWHANSGSALF | Cofactor: Binds 1 zinc ion per subunit.
Function: Can degrade casein. Could play a role in tissues homeostasis and repair.
PTM: The precursor is cleaved by a furin endopeptidase.
Sequence Mass (Da): 58939
Sequence Length: 520
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
|
Q90611 | MKTHSVFGFFFKVLLIQVYLFNKTLAAPSPIIKFPGDSTPKTDKELAVQYLNKYYGCPKDNCNLFVLKDTLKKMQKFFGLPETGDLDQNTIETMKKPRCGNPDVANYNFFPRKPKWEKNHITYRIIGYTPDLDPETVDDAFARAFKVWSDVTPLRFNRINDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGIGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFWFNGKEYNSCTDAGRNDGFLWCSTTKDFDADGKYGFCPHESLFTMGGNGDGQPCKFPFKFQGQSYDQCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFIFLGNKYDSCTSAGRNDGKLWCASTSSYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSEDPGALMAPIYTYTKNFRLSQDDIKGIQELYEVSPDVEPGPGPGPGPGPRPTLGPVTPELCKHDIVFDGVAQIRGEIFFFKDRFMWRTVNPRGKPTGPLLVATFWPDLPEKIDAVYESPQDEKAVFFAGNEYWVYTASNLDRGYPKKLTSLGLPPDVQRIDAAFNWGRNKKTYIFSGDRYWKYNEEKKKMELATPKFIADSWNGVPDNLDAVLGLTDSGYTYFFKDQYYLQMEDKSLKIVKIGKISSDWLGC | Cofactor: Binds 4 Ca(2+) ions per subunit.
PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3).
Catalytic Activity: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Sequence Mass (Da): 74941
Sequence Length: 663
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.24
|
P08253 | MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | Cofactor: Binds 4 Ca(2+) ions per subunit.
Function: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.
PTM: Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.
Catalytic Activity: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Sequence Mass (Da): 73882
Sequence Length: 660
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.24
|
Q49W90 | MNRQKNNLIFQYSAVVIFFLIVMFGLSLFLAGHYTPGGGFVGGLLLSSALVIITVAFDIKTMRKIFPWDFKILIGIGLLFCLATPMASWFYNKNFFTHTPFEIPLGILPPMEMHTATFFDLGVMCAVVGTVMTIILSIGENE | Function: Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15794
Sequence Length: 142
Subcellular Location: Cell membrane
|
Q9PJ66 | MKILVAMSGGVDSTVTAYKLKNLGHEVIGCYMKLHGKPNYHEENIKKVEKVANFLQIPYHILDLQEDFKNKVYMPFVDTYKEGKTPNPCALCNRFIKLGKLLEFAKSLGCEKLATGHYARLENNLIKTAVDESKDQSYFLASADKEALKYLIFPLGEMKKEDVKKFASTIEVLKSFATQKESSEICFVEDTYVQVLDQFMDTKIPGEVLDSSGKVVGKHEGYMHYTIGKRRGFEVRGAHEPHFVLKINPKQNQIIVGTKEELKISEFNLKNINLFIDAKELDCEVKIRYRSKSTPCKVEIYEDKSAKIILKDPVYGLASGQMAVFYDHDKVIASGFIE | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 38420
Sequence Length: 338
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q7MBC9 | MTSSPKIVAALSGGVDSSVAAALVRKQGYRVCGVTLWLMRGKGSCCSDGMKDAARVCEQLDIPHHIVDIRQQFEETIVDFLVEGYREGITPLPCSRCNKELKFGLLLEYARRKLGIGTVATGHYARTGFDGQTGRHWLARAVDRTKDQSYFLYDLSQEQLASAVFPLGEMTKDQTRTLAAELGLSVAHKPESMDLCLVEAAGSMRNFLNAHIDTRRGEIVDTSGKILGEHDGAHHYTVGQRRGLGVAAPYPLYVVAVDAANNRVVVGAREEATACECTVGQVNWVSMAEPEAPIQAEVQVRYRSQPVQATIIPLPARGARIAFDDAPQFAISPGQAAVWYAGERVLGGGIILASGRS | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 38614
Sequence Length: 357
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q5FR73 | MRILVAMSGGVDSSVVAALLKRQGHEVIGATLQLYDHGQAAKPGACCAGRDIMDARAVADRLGFPHYVIDAESRFRDSVVESFADAYARGETPVPCVACNQGVKFTDLLGMARDLGCEAMATGHYVRRVEGPEGAEMHRPVDAERDQTWFLFATTKDQLDYLRFPLGEMPDKAHVRALAQELGLEIAAKPDSQDICFVPSGSYAELVEKLRPEVRGEGEIVDEDGRVLGRHEGVARYTVGQSKRLGDIHTATGERQMVTRIDVPKRRIVVGPRVQVSEADSRRSVRLRDMNWLIDAPAEGVRCGVQIRAREKLREALVKPLENGGALVELTEAAMPAPGQACVLYDGSRVLGGGFITAGDA | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 39220
Sequence Length: 361
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q2SJL8 | MSTHRNQRVIVGISGGVDSSVSAYLLKALGYEVEGLFMKNWDEDDGTEYCTALSDLEDAQKVCDKLGIKLHTASFSAEYWDRVFEHFLDEYRAGRTPNPDILCNKEIKFKAFLDYAQALGGDLIATGHYAQFSRFGEHTYLMKGADPSKEQSYFLHAVPGQALARTLFPVGGLLKKEVRRIARELDLITHDKKDSTGICFIGERKFSDFLKTYLPAQPGKIVTDKGEEIGRHQGLMYHTIGQRQGLGIGGLKGYDDAPWYVVEKDLDNNELVVAQGGDHPRLFSAGLTASKLDWINGVPAKSSFSCYAKTRYRQPDQLCRVDVQDGGVRVTFDKRQRAVTPGQSVVFYDGARCLGGGVIESVFK | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 40487
Sequence Length: 364
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q9KDF2 | MEAKRPEQTRVVVGMSGGVDSSVTALLLKEQGYDVIGIFMKNWDDTDENGVCTATEDYQDVVQVCNQLGIAYYAVNFEKEYWDKVFTYFLEEYKAGRTPNPDVMCNKEIKFKAFLNHALTLGADYVATGHYAQVKNVDGQYQLIRGKDPNKDQTYFLNALSQQQLSRVMFPLGHLEKKEVRAIAERAGLATAKKKDSTGICFIGKRDFKEFLSSYLPAQPGEMQTLDGEVKGTHDGLMYYTLGQRQGLGIGGSGEPWFVIGKNLEKNILYVGQGFHHPGLYSEGLRAIKVNWILRRESDEPFECTAKFRYRQPDQKVTVYPQSDGAVEVLFAEPQRAITPGQAVVFYDGDVCLGGGTIDHVLKKKEDRESA | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41625
Sequence Length: 371
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
A1WWV9 | MTESPKRIVVGLSGGVDSAVAALRLVRAGHEVIGLFMKNWEDDDTLTQCSAEDDIAAAVAVAEHLGIPIRRVNFAAHYRREVFEHALQELRAGRTPNPDILCNRHVKFDRFLRHAREQFEADAVATGHYARTGRAGDGEPALLRGIDPSKDQSYFLAGVPRQALDAVRFPLGDSTKETVRAEARSAALPNFDRPDSTGICFIGERDFTQFMQRYIDPHPGPILTEDGREIGRHCGLAFYTLGQRRGLGIGGDRNRDSSAPWYVAGKDARRNALFVVQGHDHPWLQSAAVSTEPFHWLAPVPAEGARLHAQVRYRQEPQAGQLSHAEGGRVVFRFDEPQRAATPGQHLVLYDREQCLGGGVIDTAHPADRSAPPALQTQSTEVV | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 42167
Sequence Length: 383
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q98HL0 | MNSLDLPGRPENTRIVVAMSGGVDSSVVAGLLKREGYDVVGVTLQLYDHGAATHRAGSCCAGQDIDDARRVSETLGIPHYVLDYEERFRKAVIDPFAESYVAGETPIPCVSCNQTVKFADLLATAKELGADALATGHYIRSGANGAHRALYRPVDADRDQSYFLFATTQAQIDYLRFPLGGLSKPQVRAIAEEMGLTVAAKQDSQDICFVPQGKYSDIIAKLKPAAANPGDIVHIDGRVLGRHEGILRYTIGQRRGIGIASGEPLYVVHLDAERARVVVGPREALETHKIYLRNMNWLGDGPLGDIPEGGLELFAKVRSTRPPRPAVLRYVAGVTSVELADGESGIAPGQACVLYSDDGNEARVFGGGFIERSERGAEAEAMLTKLAARPAQIPAE | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 42537
Sequence Length: 396
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q7TTZ4 | MSRVVLAMSGGVDSSVAAHLLLRDGHEVIGVFMRHGEASAAACRIDSDEPQNTNPLNLPVLGDSAGGKRADHKQGCCSATDAADARRVAMSMGIPFYSLDLQEDFRKIVDYFVDDYLAARTPNPCVKCNHWIKFGRLFDYADGVDAEFVATGHYARMVHSNGRSELHRGLDGHKDQSYALFGIDPARLSRMMLPVGDFTKPEIREMATSLGLGVSDKKDSQEICFVTQGHHSDFVKSRRPEMVGATAGEIVTTGGKVVGEHKGFEAFTIGQRKRLGVAMGEPHFVIRIEPDTRRVVIGRAEELLRPGLVADQCNWFVTREELADAQSVGIQIRYNGQPHPGHVVMDGSDPTRMKVMFDDPQAAVAPGQAAVVYDGERVLGGGWITHAIDHIADGSPPPA | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 43371
Sequence Length: 399
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q07SU0 | MLNSLDLEGRPQDTRVVVAMSGGVDSSTTAALLKAEGYDVVGITLQLYDHGEAIHRKGACCAGQDIHDARTVAERIGIPHYVLDYESRFRESVIDSFATSYATGETPVPCIECNRSIKFRDLLSTARELGAAVLATGHYVSSRRLPDGSRALVCAADADRDQSYFLFATTREQLDFLRFPLGDMTKPQTRELARSFGLSVADKHDSQDICFVPSGRYSDVVGRLKPNAMEPGDIVDLDGRVLGKHHGIVHFTVGQRRGLGIASHAPLYVLRLEPSTRRVVVGPRAALRMDRILLRDVNWIGDNSLDLAVGDGLEMFVRVRSTRRPQPAWLRAIDGEYQVELIAGEDGVSPGQACVFYDAPEGQARVLGGGFIKSAAPRAANKDARGAAAANRPLAAGVRG | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 43369
Sequence Length: 400
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
A1TRM7 | MSEPIDWLPDGTPFNPRFGDRYHSHTGLAQAREVFLRGCGLPGAWAGQAMWRVLETGFGCGLNFLATWAAWRADPARPRLLHFVSCEAFPVSADDLLRSMQGHGELEPLARALHAQYWGLLPGVHRLAFEGGQVLLTLYIGDAQAMLRQQQPVADAVYLDGFSPQVNPELWDVHTLKAVARCCRRGTRLATWSVAGAVREGLAQCGFRVQKVPGLPPKRSNLQAEFDPAWEPRPVQPELPDVRVAGGPSSVLVIGGGLSGAAVAASLARRGWQVRVLDQGAEPAAGASGLPAGVFAPHVSPDDSLLSRLSRCGVRATLQALEASGLSEGEDWSACGVLEHEVDGKHRLPPAWAGDAAVGAEWSRPADAAALEAAGLPGATVAYWHARGGWLRPARLVRALLAHPGIHWQGRSAVARLEPVAAPGGATHWQAYGSDGTVLAEAPHVVVAAGYGSRPWLPARYPIHPLRGQVSWGTRADSPAAAWPPFPVNGHGNLVPHAGTAGGGIWVMGSTFERGQTELPPAPQEQAQAHAANAAKLEQLLPALAQGLAPAIAGPGAAPGHWAAVRCTAPDRLPFVGPVDAARQAGLWVCAAMGARGLTLSQLCGELLAARMMGEPLPVEVRLARALSTERLPAD | 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): 66954
Sequence Length: 635
Subcellular Location: Cytoplasm
|
B0V636 | MNKSNRIQTAELDWESIDGIEVPISKQFGDVYFSKDNGLLETRHVFLNGNDLSERLANLQDFEYFSVGETGFGTGLNILALWQLWQQVRPNNHSHLHAISVEKFPLSKADLIRALNVWDELKPLSKQLIEQYPLPLAGCHRLSFPEERFSIDLWLGDAQDIFPSMVKTKAVNAWFLDGFAPSCNPDMWEQNVLNNIVRLSNYGTTFASFSVAGVLKRGLKAHGIDISRPRGFGHKREMLKAIWKAPVSEEILFEPVSDTFHFTQQRIAIIGAGIAGLSTAWAFAQRGHQVTLFERTAPLSGASGNPLALLNPKLCPIEQSHEHLMTLSWQHALNFYKNFQAFRPIQIQQMALKNAQDLLDLTNQYPADIVTQQTSSLESDYPHIILTEAGAVSPHQLRDEILQHPGIELKIANITTLVSFENKVQLKSGNETTLEADHVVVCCARESAALFENYPLLKPIRGQVSWVDNSFATLPLHEAYSYGGYCMQLNTSELILGASFYPNRDDQEVLLDDHVHNFELIHSVFPHYAKQLPPVEQWQGRASVRAQSPDYFPVVGKMQNESRISTFAGLGSKGFLFAPLCSEVLVAQILGEAYPVPKSLLQKLDAQRFQKKVKPKKPYFKSQ | 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): 70136
Sequence Length: 623
Subcellular Location: Cytoplasm
|
A1W6V9 | MSEPIEWLEDGTPYSPRFSDRYHSEHGGLEQARGTFLAGCGLPQAWQNQPQWRVLETGFGLGLNFLVTWAAWRADPHRPQRLHFVSCEAWPVSAADLLRAAPIDSTLQSLAQQLAAQYWGLLPGVHRLSFDGGQVLLTLYIGDAQALLRQQQPTADSVYLDGFDPQHNPQMWDIHTLKAVARCCRRGTRLATWTVARGVRDGLVQCGFEVQKVPGVRPKRDNLQATYAPRWEPRAGQPVLPDATVAAPARCLVVGAGLAGAAVAASLAHRGWQVQVLDRADHPAAGASGLPAGVFAPNVSQDDNLISRLSRAGVRITLNTLAQLPAETRGTDWSACGTLEHRVDGTTGLAWSDGPGLDWSRPATPAQLQANGLSADTVACWHEHAGWVRPPQLIAHLLNDPAIRWRGSAAVAELRRTTVDGQPLWQALDAEGHVLAEAELAVVCAGHHTGPLTHAHWPMNPLRGQLAWGLHAQAPAGAPWPPQPLNGNGNLVPRVPLQDGAGWVLGSTFERLKTALPPSPDDHAKGLATNQAKLHALLPPLGAAMDAAFSQAATAPDGPVRTWAAVRCGALDRRPIVGPVDSVRQPGLWLCTAMGARGLTLSLLCGELIAARLHSEPLPLDAPLARALSSERWLGYEPQ | 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): 68618
Sequence Length: 639
Subcellular Location: Cytoplasm
|
Q21WM8 | MVELAAATCLHECGLPQAWCKQEAWRILETRFGQGLHFLTTWQAWRNDPQRPRMLHYVAVTAAPPDIDELLAGMASSPELLLLAKELAPQCLGLSTGFQRLTFDGGHVLLTLCVGDLTAMLRAQQFAADSIYLTPDPTDCPDRCAASNWRVWTAKALARCCRRGTTLVAPVDADHLYADLTQCGFELSTIQAGQPTGPEAAPTNISLRAQFNPRWTIKNTRNTLPARAMAVSSCAVIGAGLAGASVAASLARRGWQVQVLDQAHTPAAGASGLPVGLVVPHVSADDCVLSRLSRSGVRLMLQQARSLLRQGQDWDATGVLERRLDGPPGVPDIWHPQAAWLKPTQLVRAWLAQLGITFQGDAKVAALRQRGDEWELLDTDGGMLHRASRVVFANAGGAMALLDTLQARLPALNIRVNQFPVMQGVRGQVSWAMHTGLPDETFPPFPINGAGSIVPWVPVDEDCGQNLAWFVGASYQPDSQPPAPDEKNHATNLARLHKLSPKLGQALAGKFAAGAVNAWKNTRCVTADRLPAVGPLDQVDHPGLWMCAGMGSRGLSFSMLCAELLAARWSGEPLPIDAGLARTLEARRGADCHRNRLDRSPELPVSCAP | 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 (By similarity).
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): 65624
Sequence Length: 609
Subcellular Location: Cytoplasm
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.