ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9UM21 | MRLRNGTVATALAFITSFLTLSWYTTWQNGKEKLIAYQREFLALKERLRIAEHRISQRSSELNTIVQQFKRVGAETNGSKDALNKFSDNTLKLLKELTSKKSLQVPSIYYHLPHLLKNEGSLQPAVQIGNGRTGVSIVMGIPTVKREVKSYLIETLHSLIDNLYPEEKLDCVIVVFIGETDIDYVHGVVANLEKEFSKEISSGLVEVISPPESYYPDLTNLKETFGDSKERVRWRTKQNLDYCFLMMYAQEKGIYYIQLEDDIIVKQNYFNTIKNFALQLSSEEWMILEFSQLGFIGKMFQAPDLTLIVEFIFMFYKEKP... | Function: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains . Involved in glucose transport by mediating SLC... |
Q73MR1 | MNLDFLSLSDKHNSVVVLGATATGKTSYAVGLAKELGGEIISADSRQVYKGLDLGTGKDLKEYGDVPHHLIDICTLEREYNVFDFQNDAYKAFEDIKRRKKLPIFAGGTGLYLDSLIREYELIPVPKNEELRASLAGKDLTELQKFFFEYNVPMHNKTDLENMDRLMRAIEIAEYKKTHPDAAEILNANRPDIRPLIIGLKYPREILRERIRLRLLERIKDGMIEETESLHKEGFSWERLESLGLEYKFTAQYLQGKIKSREEYVDSLYRAICQFAKRQETWFRRMEKNGVKINWVLK | 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(3... |
B0CG28 | MTPGLIVICGPTATGKSSLALALARRLGAPILSADSRQVYRGFDIGTAKPSVTDQEDVPHYLIDICDPTETLTVADYQEQAQALIAQFHTEGQTPILVGGTGLYIRAIVEGLKIPRVPPQLELRSQLQSQGQVQIYQWLQQVDPPAAQKIHAHDQVRTLRALEVFYTTGIPLSAQQGKNPPSYPILQIGLDISDLDQHTDIIQQRTAAMVEQGWLTEVQKLIDHYGVELPLLATLGYQEMKAYLHQQITLEEATAQTILHTRQFAKRQRTWFRANSGIHWFDATNSDLLSLVWKDIQGQPWL | 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(3... |
A9NGL4 | MKKVVCIVGPTGSGKTALSVKLAKSLGAEIINGDSVSIYKKLDIGSAKITTDEMDGVKHHLISHVALDEPYTVYNFQQDVRTLIDQIDKPFIVGGSGLYVKSALYNYEFEQQDNVEFPNINEMIEVIRKADPDIEIDLNNPRRIESAYRTIISGQKRSNKTKKNEPLYDIYLIYLDMDRKILKKRLETRLDLMIEKGFIEETKALINYDLNIIGYREIKDYLNGMNDLDTAKEKIITATMRFAKRQKTWFINQMKPKVYNALSPDLLDECLKDIKEFIGV | 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(3... |
Q6F9W1 | MSSTLPVINLMGPTASGKTALACELYERGHFELISVDSALIYKDMDIGTAKPTKEELALYPHHLIDIITPLEVYSAAQFVEDATQLIDQIHMKGKTPILVGGTMLYFKSLLEGLSTNLPSADAEVRAAIEKQAEQEGWQSVYDELARVDPVAGARFKVSDRQRIIRAIEVYRLTGQPITKLQAEQPKNVPYRYTFHNYALLPDRIELHKRIEQRLFKMWSIGFLNEVESLIKKYDLNDNLPSMRSVGYRQALDFLLKSDMSHNNRREMEDKALFATRQLAKRQYTWLRSLQETHYFKTYLTIKQAQEDLRNSYG | 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(3... |
A0LUZ6 | MSSSASLSSSASLQRVVVLVGPTATGKSVLAVRLAQRFNAEVVNADSMQVYRGMDIGTAKLPPAERDGVAHHVLDVWPVTKTASVAEYQHLARAAIEEIGRRGRLPILVGGSGLYVRAAVDRLEFPGTDPAIRARLEAELAAHGPEALHARLARLDPQAAERILPTNGRRIVRALEVLQLGRPRFAAELPEYASVYDALFLGLDLATPELDDRVERRVAAMWQAGFVDEVRHLAEDCGLREGRTASRALGYRQVLTMLDGGCDEAEARRRTVDATKRFVRRQRSWFRPDPRIHWLDAADAALETAAARTIEGWMTSRS | 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(3... |
A5G2E2 | MTQSPRACSAPPARPLLIVAGPTASGKSALALAAAQRFGGTIINADAMQCYADWRIITARPTPADEAAAPHRLYGVRRLEEAVDAAWWRGRALAELAAAELPILCGGTGMYLSSLVNGIAPIPDPGPNARAEARRMLAADGPAALHAWLAARDPATATKLRPSDPQRLARAAEVLLGTGRGLAAWHAAPRAGLAGYRVMLLLLDPPRPALREAIAARFEAMLAAGALAEVAAVAARAPDPALPGLRAHGVPELLAHLAGAISLDEAASRAIAATAAYTKRQATWFRHQKLADQRNTHTIRSRLTDSTQFSESTVRSIISF... | 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(3... |
B7JC25 | MQSWATDGSVFFLGRSRPPLSPRAMIPAIFLMGPTASGKTELAVRLADALPIDIISVDSLLVYRHFDIGSAKPSLALRQQYPHALVDIREPDEPYSAGLFREDALHCIALARERGRIPLLVGGTGLYFRALECGIDTLPPANPALRQSLMALAETAGWPALHQRLATLDPEAAAGIAPHDRQRIQRALEIILGSGQTISGARHWQGTFPGPLYKIILRPPRSWLHQRITQRFDVMLNEGFLDEIADLSARHYAPELPAMRAVGYRQYFTWHDGLCSAAEAYQAALAATRQLAKRQDTWFKRESAHYYLDPSRDDASSLLL... | 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(3... |
Q187T5 | MKKIPLIILTGPTAVGKTDLSIKLAKDMNAEIISADSMQIYEYMDIGSAKVTEKEMQGVKHYLIDEVKPDYPFSVSEFQQRAKKYIHEINKKEKCVLVTGGTGLYLNSLIYNMDFAQSDANNELREELQKQLAEKGIDYMHNKLKELDEESANRIHKNNTKRVIRALEVCLSGKKMNDFSSDLKFNEEYQPIIIVLNRDREHLYQRINMRVDIMIKNGLVEEVKKLLSMGFKKDMISMQGIGYKEILKYLDGEYTYEEAIEIIKRDSRRYAKRQITWFKRYKTAKWFDLDQYENIDELKNEIILYIKDSIK | 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(3... |
A0Q0M8 | MKQDLFILAGPTAVGKTDISIKLAQKLNGEIISADSMQIYKHMDIGSAKITEAEKEGIPHHLIDFVSPFDEFSVAEFKEKSKNAIKDIASRGKLPMIVGGTGFYIDSLIFNYDFANTYKDEEYREHLKNLASEHGKEYVHELLKDIDEVSYKKLYPNDLKRVIRALEVFKLTGKTISEFNKEQDIFDIPYNVYYFVLNMDRSKLYERINKRVDIMMEKGLIEEVKSLQNMGCTPDMQSMKGIGYKEILYYLDGKLSLDEAVELIKKGSRHYAKRQLTWFRKDNRVNWIDKDQYKDDTEVCNAIEEKFLNLKNNL | 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(3... |
Q895H4 | MKDLFILSGPTAVGKTEISLNLAKALRGEVISSDSMQIYKHMDIGSAKIFEEERQGIPHHLIDVVEPWENFSVAEYKNIAENKIEEIYNRDNIPMLVGGTGLYINSIIYNYSFTDANKDNDYRDYLEKLAKEKGKEYIHSLLKDIDEYSYNNLHYNNLKRVIRALEVYKVTGKPMSQYAKEEKENLFNIPYSIYYFVLYMDRDKLYDKINMRVDRMLQEGLLDEVKELKEMGCNETMQSMQGIGYKELLYYLNGEISFNEAVYLIKKGSRNYAKRQLTWFRRDPRAIWINKDEFENDDAIVKEILNKFNKLKGF | 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(3... |
B5Y8R8 | MGKPLISILGPTGVGKTDLAFRLACSLDKANILSVDTGSFYKAATIGTAKPPKEFTSRVRHWFIDILECQEVYSVGAFVSDCSSILQDLWAEGVTPIVVAGTLFYYYALVGERSFSAVPSDSTVREKVEEKARVYGEEYLRQELRKVDPEREKNILPGDIRRLTRALEIAELGFKPTEAVVTNKLDFDINLKIGLKMPRDLYRTRLRDRVEYMISAGLIEEVQDILSKTGNSSLPCLNQIGYKEVCSYLKGEIKNKDELVERIFLSHWTYARKQIKWLKKDKTIVWFDVSEKSPDTLVEEVLTLVQSTLENC | 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(3... |
Q8FPE0 | MITPIAVVGPTASGKSALGIELALRLDGEVVNVDSMQLYRGMDIGTAKLTPEERQGIPHHQLDVLDVTETASVARYQQEAVADVEEIMSRGKTPILVGGSMLYVQSLVDDWQFPPTDPAVRARWEARLAEIGVTRLHEELRARDPEAAAIIENNDPRRTVRALEVIELTGQPFKASQPPKDAPPRWGTTILGLRTTADWLNPRIELRTHLMFERGFLEEVEGLVRDHGLIAESTAGRAIGYAQVLDALAGELTLDEAVERTITGTRRYVRRQRAWFNRDHRIRWIDADGDTTARALDILGR | 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(3... |
Q8NP72 | MVTPIAVVGPTASGKSALGIALAHKLDGEVVNVDSMQLYKGMDIGTAKLTVEEREGIAHHQLDVWDVTETASVARFQSDAVADVEDIMSRGKTPILVGGSMLYVQSLVDDWQFPPTDSAVRARFEARLADIGVEALHAELTQLDPEAAAVIESNDPRRTVRALEVIELTGQPFQASQPPKDAPPRWGTRIIGLKTTPEWLNPRIEQRTARMFEQGFVAEVEHLVQQGLIADSTAGRAIGYSQVLAAMAGEMTWEDAFERTVTGTRRYVRRQRSWFNRDHRVSWVDASGDPTAQALEILGLQ | 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(3... |
B1VDE1 | MDYSHSDSPSTAPAGKTPVDQLRPLLIVGPTGAGKSDLSLEVARRLDQPVEIINGDSMQMYRGMDIGTAKLSRAERAEFPHHLFDCLDVDDTASVAAYRDLAGETVEQIQARGARPIIVGGSMMYLQALVDDWQFPPTDAAVRAKWMAEQDRIGVEALHEVLRSKDPDAADIIEEKDPRRIVRALEVIELTGKPFAASQPPKNVPTRWGTRIFGLKAPGNWLNPRLEARVDRMFAAGLVAEVEGLATAGLSRESTAGKAIGYAQVLSALAGECSMEQAREDTVVGTRRYARRQRSWFRRDPRIHWLDATVADPGLLAGQV... | 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(3... |
A9KE31 | MNKNPFIVCLMGPTASGKTDLAIALARKLPFEIISVDSAMVYRGLDIGTAKPNEEELQLTSHRLINICDPSFPYSAGQFYKDALSEIKTIEIRNRTPLLVGGTMLYFHILEQGFSDLPTADETVRKKIQEEAAQHGWAKIHERLNAIDPKSAARINPNDAQRIQRAFEVYETTGQPLSSYQSLKRFKALPYQFINLILAPENRSWLHQRIEKRFDQMLKNNFLEEVRQLYNRGDLNSDLPAIRTVGYRQVWKYLSGEYDYETMRHKAIAATRQLAKRQLTWLRRWPDAKWFNSEDKDLISQVVDYLKGIGM | 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(3... |
B8EQB8 | MAAAKFTALLIAGPTASGKSALALRLAEKLGGILINADSMQVYRDLRILSARPSAEEELRAPHRLFGAIDGAVNFSVGLWLEAARNILEEARQAGALPIFVGGTGLYFKALTQGLSDIPAVPDDIRAKLRARTEGVAATELHAELSARDPLMAARLRPSDPQRLLRALEVLEATGRSLASFQSRRGPPVLDPAATRAIFLSPERAALNLRIDERFEAMLASGAWAEVEALRRRGLDPALPLMRAHGVPHLIAHLEGKIPQDEAIRLGKRDTRAYARRQFTFARHQLPGFVWAEPREAEALALA | 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(3... |
Q2RJG0 | MSTLSTKEPLAAIVGPTATGKSTIALKVAARLGAEIISVDSAQVYRGMDIGTAKLLPEERVGPDGRPIPHHLIDIVDPDEPFSVADYQKLARQTITAIIRRGHLPLLVGGTGLYYQAVVDPYRFTPEGGDPRVRQELEELAAKFGDAYLHEQLKRVDPEAAKRIHPHDRRRLVRALEVFKTTGQPISAALAWRRQQESPYHLAAVALSMPRPLLYRRIEARVDAMIAAGLIEEVSRLLARYDYRLPALQALGYKEIGAYLRKEIELEEAIAILKRNTRRLAKRQLTWFRRDRRLHWWEVDPDKIEEISAAIADFISRTID... | 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(3... |
Q7NBU2 | MIYSKRLILVVGPTGTKKSYLANMLAKKLNVPIISADAYQVYKELNAGVNKPSEKTLSEIKYHFISNISIFDEWSIAHFNKRAKEILEQAPDWTIVCGGSHLYVNSLINDYQLEKQELDTDLFDALDKLDNQEIFNQLCEYDFQEAIKIGKNNRKRLLRALYLFKKYGKKAKNDSKKFDYVVVKCMSDKEKLFPYLSKRLDEMIHDLNWTKEIEYLDKIITDKKLDKELIAMKALGYKEIYDAWKNNQPIDKEIINKKFKRLVKHQLTWTRNKFNDGMKQFTFNFFEDDANRTCDEIIEYIKSNHD | 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(3... |
A0QVX9 | MNRPLAVIGPTGTGKSALALEFAERVGGEIVNADAMQQYRGMDIGTAKLTVEERRGIPHHQLDVLDVVETATVARYQQAAAADIETIAARGATPVIVGGSMLYIQSLLDEWSFPATDPAVRAKYEARLAEIGVAALHAELARVDAAAAASILPTDGRRIVRALEVVELTGEPFAASAPTIGAPRWDTAIIGLDWDTAVLDERLAQRTDKMFADGLVREVVDLLERGLRDGVTAARALGYAQVLADLDAGGDGSGAREPTFIGTRRYVRRQRSWFRRDHRVVWLDGASEGLVDDALRVWRAVS | 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(3... |
O69967 | MSSAPPAPRVIAVVGPTAAGKSDLGVFLAQRLGGEVVNADSMQLYRGMDIGTAKLTPEERGGVPHHLLDIWDVTVTASVAEYQRLARERIDALLAEGRWPILVGGSGLYVRGAVDNLEFPGTDPGIRARLEEELELRGPGALHARLAVADPEAARAILPSNGRRIVRALEVIEITGRPFTANLPGHDSVYDTVQIGVDVARPELHERIALRVDRMWEAGLVDEVRALEAQGLREGRTASRALGYQQVLAALAGECTLDEARAETVRATKRFARRQDSWFRRDPRVHWLSGGVADRTELPRLALSLVERPVTA | 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(3... |
B1VXU2 | MTPPASAPRVITVVGPTAAGKSDLGVFLAQRLGGEVINADSMQLYRGMDIGTAKLTLPEREGVPHRLLDIWDVTETASVAEYQRLARREIDRLLAEGRTPILVGGSGLYVKGAIDALEFPGTDPEVRARLEAELAERGSGVLHERLAAADPDAARSILASNGRRIVRALEVIEITGKPFTANLPGDEPVYDAVQIGVDVERPELDERIARRVDRMWDAGLVDEVRALEAAGLREGLTASRALGYQQILAVLAGECTEDDARAETVRATKRFARRQDSWFRRDARVVWLGGGHRDRGELPHRALTLVERAVTA | 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(3... |
B7J5B2 | MQNLYIKTYGCQMNEYDSERMADTLAVSHGLRLVDDPVLADVLLLNTCSIREKAEDKVFTQLGFWRPFKERRPEVVIGVGGCVASQEGERLRRRAPYVDLVFGPQTLHRLPDLLDACLAERRPQVDIAFPMLEKFDHLPQRPGRDGATAFVTIQEGCDKFCTFCVVPHTRGREYSRSMPDILREVRALVEQGVREITLLGQNVNAYRGATGLVGEGGLADLLERLARIPGLLRLRYTTSHPANLDDELIAAHGSIGILAPHLHLPVQSGSDRILRRMHRKHTVGQYLDKVDRLRAARPGIQISSDFIVGFPGETDADFAA... | 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 re... |
Q1IQH5 | MPVSSDPKTFYIETFGCQMNFHDSEKVVGTLISQGYRQVETELDAGLILYNTCSIRDKAEQKVFHRLSEFRQLQKEGKRFAVLGCVAQQEGEKIFERAPHVSLVAGSASYRNLAEMLVQIESGSQRITGLDDRETDQTFETEFTARGNAHRGYITIIEGCDKFCAYCVVPYTRGKERSRSAESVLREARQMADAGFTDVQLLGQNVNSYHDPSGTMTFAELLTAVGEITGIKRVRFTTSHPRDFTRDIVEAIDNHPTLCDHVHLPVQSGSSKVLREMFREYTREQYLERISWMKATKNRKLSITTDVIVGFPGETETEFE... | 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 re... |
A9KMU9 | MALCKAEVKKVADELGRPLTFNVQTFGCQMNAKDSEKLAGILETIGYVESDSEEADFVVYNTCTVRENANTRVYGRIGFLGNLKKKNPHMRIALCGCMMQESHVVEKIKKSYRFVDIVFGTHNIFKLAELIYARHTTKKMVIDIWKETDKIVEELPSEQKYKFKAGVNIMYGCNNFCSYCIVPYVRGRERSRNPEDIIKEIKQLVSKGVVEVMLLGQNVNSYGKTLDEPVSFAQLLQMVEQVEGLKRIRFMTPHPKDLSNDVIEVMKNSKKICNHIHLPVQSGSTELLMKMNRKYTKEDYLNLVDRIKMAMPNISLTTDI... | 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 re... |
Q1MQ52 | MLQRNFHIITFGCQMNTNDSFWLSCSLQKKGFQEVSLEDASIIIINTCSVREKPEQKVYSILGKIRHATKNNPDSFVVIAGCVAQQLGATFFEKFPQVRLVSGSDGIAMAPDAIERLYAEPDLKLNLTDFSEYYPEREYAFSKLTLSNNNTLALMAYVNIMQGCDNYCTYCIVPYTRGKQKSRSVQAIVEECQQLIDSGVKEIVLLGQNVNAYGLDKDKNSPANGVNFAMLVHTIASLPGLERLRFFSAHPKEFSSELIDLFGEFSTLCPRLHLPLQSGSDKILRRMGRKYSMDEYISIITKLKKVRPDIALSTDFIVGF... | 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 re... |
Q72PA4 | MSVLEQEKKSGKVYIETYGCQMNEYDSGIVSSLMRDAEYSTSSDPENSDIIFLNTCAIRENAHAKIYNRLQSLGYLKKRNPNLVIGVLGCMAQNLGDDLFHQELPLDLVVGPDNYRSLPELIQRIRKGENSISLTRLSKIETYDEIEPRVVNGIQAFVTIMRGCNNFCTFCVVPYTRGRERSRDPKSIVREVQDLVQKGIRQITLLGQNVNSYKEQDTDFAGLIQMLLDETSIERIRFTSPHPKDFPTHLLQLMSENPRFCPNIHLPLQAGNTRVLEEMKRSYSKEEFLDVVKEIRNIVPDVGITTDIIVGFPNETEEEF... | 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 re... |
B1HR59 | MNEEQRLANQQVNQPKKEDKPEKDYSKYFEKVFTAPSLKDAKKRGKEDVKYHKDFSIDEQFAGMGKDRTFYIRTYGCQMNEHDTEVMAGIFMQLGYTPTEIIEEADVVLLNTCAIRENAENKVFGELGFLLKYKRKNPEMLIGVCGCMSQEESVVNKILRSYPHVDMVFGTHNIHRLPNILKEAYMSKEMVVEVWSKEGDVIENLPKKRLGSIKAWVNIMYGCDKFCTYCIVPYTRGKERSRRPEEIIAEVRELAAAGYQEIMLLGQNVNAYGKDFEDIEYRLGDLMDALRKIDIPRIRFTTSHPRDFDDHLIEVLAKRG... | 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 re... |
A0L7K3 | MKHLYIKTFGCQMNSYDSTRMADLLGESHAFQSTDDPEKADLIILNTCHIREKAEDKLFSELGRLRPLAERGVILAVGGCVGQAEGRTIFSRAPYVRMVFGPQNYHKLPQMIQRALDGETRVIAEDIPSVDKFDNLPQVRAQGVVGQVTVQEGCDKFCAFCVVPYTRGREWSRPVAAILAETEALAQQGVREVLLLGQNVNAYAGVDEEGVSYDLALLIRRVALIEGIERIRFVTSHPVDMNEDLVEVFGEIEQLAPYLHLPIQSGSDAILAAMQRGHTVEEYCTWVEKVRAVCPDVALASDFIVGFPGETEQDFQATLD... | 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 re... |
Q8EUX4 | MKSHIMDSKSTKKRDLSKYFLPDIRQARKRIKKADIIKDGFEIPANIINYGEGKTYHIKTFGCQSNLRDTEVMMGMLELIGYEYNEDVNTSDLVLLNTCAVREHAESKVFADIGILDRIKKSNPNFIFGVCGCMAQEEAVVNRILKSNFNVDFIFGTHNVHRILNLLEQVIFEKNLVVEVWSHEGNVIENLPSKRTNNLKGFVNVMYGCDKFCTYCIVPMTRGKIRSRRKEDILDEVHQMISEGYKEVTLIGQNVNSYGIDFDNGENYLFNNLLEDVAKTGIERVRFTTSNPWNFTRSIVDTMKKYPNIMPHIHLPIQSG... | 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 re... |
Q7ULM9 | MISMTKTVYIKTVGCQMNVLDSEMVIADLKRHGYTVVDTPGEADLLLYNTCSIREQAEEKTYSALGKLKETKARHPEKTIGVMGCMAQKDQETIFRRAPFVDMVVGPGQLHAIPDMLTKVTSGEGRQMAVSLGRKDGKQTVVARSHETFDPLRDPTMRPTPFQAYLRIQIGCDKFCTYCVVPNTRGPEQGRSPEEIVSEARVLAEQGALEITLLGQTVNSYRHRGPDGETDMAGLLERLHDIDGLKRIKFVTNYPKDMTARLLETIRDLPKVSPYLHVPAQSGSDAVLKRMKRGYTIADYMEMFERIETVLPEASVSSDF... | 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 re... |
Q21C43 | MTQPRKLHIKSFGCQMNVYDAQRMVDALAPEGFVETANADEADLVILNTCHIREKASEKVYSELGRLRVAKDEAALQGRRMNIAVAGCVAQAEGAEIIRRQPAVDVVVGPQSYHHLPQLLAEAARGGRALETEFPVDDKFGFLPPPQPDAIRARGISAFVTVQEGCDKFCTFCVVPYTRGAEVSRPVDKIVEDVRRLADNGVREITLIGQNVNAYHGDGPDGRPWPLGALLHHLAKIPGIVRLRYSTSHPRDVDQSLIDAHRDLPALMPFVHLPVQSGSDAILAAMNRKHSADDYRRLVDRFRSANPAIAFSSDFIVGFP... | 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 re... |
Q88KV1 | MSLIPEIDAFLGCPTPDAWIEAALADQETLLIDHKNCEFKAASTALSLIAKYNTHLDLINMMSRLAREELVHHEQVLRLMKRRGVPLRPVSAGRYASGLRRLVRAHEPVKLVDTLVVGAFIEARSCERFAALVPHLDEELGRFYHGLLKSEARHYQGYLKLAHNYGDEADIARCVELVRAAEMELIQSPDQELRFHSGIPQALAA | Cofactor: Contains a nonheme dinuclear iron cluster.
Function: Involved in specific tRNA modification. Catalyzes the oxygen-dependent hydroxylation of 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) to produce 2-methylthio-N-6-(cis-hydroxy)isopentenyl adenosine (ms2io6A) at position 37 in tRNAs.
Catalytic Activity: 2-m... |
Q8VZK0 | MEASPNDRLHFGKMGFGCKHYKRRCQIRAPCCNEVFDCRHCHNESTSTLRNIYDRHDLVRQDVKQVICSVCDTEQPAAQVCSNCGVNMGEYFCSICIFYDDDTEKQQFHCDDCGICRVGGRENFFHCKKCGSCYAVGLRNNHRCVENSMRHHCPICYEYLFDSLKDTNVMKCGHTMHVECYNEMIKRDKFCCPICSRSVIDMSKTWQRLDEEIEATAMPSDYRDKKVWILCNDCNDTTEVHFHIIGQKCGHCRSYNTRAIAPPVLPQ | Function: E3 ubiquitin-protein ligase that acts as a regulator of cell death and defense. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Attenuates the activation of defense and related cell death... |
Q9BRT3 | MSGEPGQTSVAPPPEEVEPGSGVRIVVEYCEPCGFEATYLELASAVKEQYPGIEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIRRASNGETLEKITNSRPPCVIL | Function: Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process.
PTM: Isoprenylation facilitates association with the plasma membrane and enhances the migrato... |
Q5ZXE0 | MKMKLVTAAVMGLAMSTAMAATDATSLATDKDKLSYSIGADLGKNFKNQGIDVNPEAMAKGMQDAMSGAQLALTEQQMKDVLNKFQKDLMAKRTAEFNKKADENKVKGEAFLTENKNKPGVVVLPSGLQYKVINSGNGVKPGKSDTVTVEYTGRLIDGTVFDSTEKTGKPATFQVSQVIPGWTEALQLMPAGSTWEIYVPSGLAYGPRSVGGPIGPNETLIFKIHLISVKKSS | Function: Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 24881
Sequence Length: 233
Subcellular Location: Cell outer membrane
EC: 5.2.1.8
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Q09734 | MHRENYFSKIAFCLLGVLFLSCITSVQTVSGDAASHEERMNNYRKRVGRLFMEQKAAQPDAVKLPSGLVFQRIARGSGKRAPAIDDKCEVHYTGRLRDGTVFDSSRERGKPTTFRPNEVIKGWTEALQLMREGDRWRLFIPYDLAYGVTGGGGMIPPYSPLEFDVELISIKDGGKGRTAEEVDEILRKAEEDREDM | Function: Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 22136
Sequence Length: 196
Subcellular Location: Secreted
EC: 5.2.1.8
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P90495 | MEDEDVPVCWICNEELGNERFRACGCTGELENVHRSCLSTWLTISRNTACQICGVVYNTRVVWRPLREMTLLPRLTYQEGLELIVFIFIMTLGAAGLAAATWVWLYIVGGHDPEIDHVAAAAYYVFFVFYQLFVVFGLGAFFHMMRHVGRAYAAVNTRVEVFPYRPRPTSPECAVEEIELQEILPRGDNQDEEGPAGAAPGDQNGPAGAAPGDQDGPADGAPVHRDSEESVDEAAGYKEAGEPTHNDGRDDNVEPTAVGCDCNNLGAERYRATYCGGYVGAQSGDGAYSVSCHNKAGPSSLVDILPQGLPGGGYGSMGVI... | Function: Membrane-bound E3 ubiquitin ligase expressed during late stages of lytic replication to mediate polyubiquitination of various host membrane proteins related to the immune response . Promotes ubiquitination and subsequent degradation of host MHC-I and CD1D molecules, DC-SIGN and DC-SIGNR, presumably to prevent... |
O41933 | MDSTGEFCWICHQPEGPLKRFCGCKGSCAVSHQDCLRGWLETSRRQTCALCGTPYSMKWKTKPLREWTWGEEEVLAAMEACLPLVLIPLAVLMIVMGTWLLVNHNGFLSPRMQVVLVVIVLLAMIVFSASASYVMVEGPGCLDTCTAKNSTVTVNSIDEAIATQQPTKTDLGLARETLSTRFRRGKCRSCCRLGCVRLCCV | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of host surface class I (MHC-I) H-2D(b)/H2-D1 and H-2K(b)/H2-K1 molecules before they exit the endoplasmic reticulum, leading to their degradation by the endoplasmic reticulum-associated degradation (ERAD) system, thus blocking the immune detection of v... |
P90489 | MASKDVEEGVEGPICWICREEVGNEGIHPCACTGELDVVHPQCLSTWLTVSRNTACQMCRVIYRTRTQWRSRLNLWPEMERQEIFELFLLMSVVVAGLVGVALCTWTLLVILTAPAGTFSPGAVLGFLCFFGFYQIFIVFAFGGICRVSGTVRALYAANNTRVTVLPYRRPRRPTANEDNIELTVLVGPAGGTDEEPTDESSEGDVASGDKERDGSSGDEPDGGPNDRAGLRGTARTDLCAPTKKPVRKNHPKNNG | Function: Membrane-bound E3 ubiquitin ligase expressed at the immediate early stage of viral reactivation to mediate polyubiquitination of various host membrane proteins related to the immune response . Promotes ubiquitination and subsequent degradation of host MHC-I, CD86, DC-SIGN and DC-SIGNR, ICAM1 and CD1D molecule... |
Q8X1Z7 | MALDDISAVPKGALDTDPAVERPPPLLDADRSDSERLQPGVKRAEMLRKGWTRQGLIIAFTGLFLATLSINFGDYSTQVYVPYATSAFKQHSAMSAARVVGNITRIAAYPIIAKLGDVFGRAEMFILSIVFQAVGYAIYAGCKNVGQYIAGGIFEAIGSTGFGLTQQVFVADVTNLINRAVWSTLPDSLTVIPALYLGTEIAEAVLEKNEWRWGFGMWAIIEPVCSVLLVGTMLYYQKRARKDPSPAEFASEPTERNVDDGWWKRIYNLVWVQLDAFGAILLLLGLSLFLVPLSLTGSGNSDDWHRGSFIAMLVLGVVIF... | Function: Involved in the transport of siderophore enterobactin and so has a role in iron homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66311
Sequence Length: 609
Subcellular Location: Membrane
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Q4WF31 | MLHVLSVGPSHAAFTVEAAMATMKKFHSIVGEKPAQDAEAPSVDDPNVGQIRADDKEAAHAPANAETNNEEANPSDGAQAGVKKIEAVTLSWTRGTAIWFLTLVNDFRLSMYTSLNAYATSSFLGHSLLTVINIVSYVMGGSVYIPMAKALDLWGRAEGFLLMTFFCILGLILLASSQNLPTYCAGQVFYKVGFGGLSYTWNVLAADVTNLRNRGLAFAFTSSPALISAFAGSKAASDLLAHSTWRWGFGMWAIILPVVALPIYGLLAYHLRQAEKKGVLVKETRDWSITPKTVWWAIMEFDLPGVLLFAGGFVIFLLPF... | Function: Major facilitator transporter involved in triacetylfusarinine C (TAFC) uptake . Can also transport ferricrocin and coprogen, but not ferrichrysin . MirB plays a crucial role for virulence in a murine model of pulmonary aspergillosis, indicating that TAFC-mediated iron uptake plays a dominant role during infec... |
Q4WHE1 | MPFLDHRTGPSYGTIDQMEQHSDDEGERFLQEQCDTGRFSSDITSISEDSVQEGVRKIEAINLTWTARSLVIAYVSIFLMSFCTSLEGQTVMSLGAYATSAFSKHSLISTVLVVQNVVNAVIKPPMAKVADVFGRFEAFCVSILIYVLGYIQMAASTNVQTYASAQIFYSAGSTGLQILQQVFIADSSNLLNRAFLALLPEFPFLVTVWIGPTIADAVLKHASWRWGYGMWSIILPASFLPLALSLLLNQRKARRLNLIKPKSRPRGGVFAVLRRTWYDLDMGGLILLSAAVTLILVPLTLAANSKNGWKSDSIVAMIVV... | Function: Major facilitator transporter that contributes to the maintenance of intracellular siderophore ferricrocin (FC) levels . Plays a role in conidiation and confers protection against oxidative stress . Contributes also to fungal virulence in the Galleria mellonella animal model system . Does not appear to play a... |
Q90327 | MNKNKREKEFYSVDVGDSTFTVLKRYQNLRPIGSGAQGIVCSAYDHNLERNVAIKKLSRPFQNQTHAKRAYRELVLMKYVNHKNIICLLNVFTSQKTLDEFQDVYLVMELMDANLCQVIQMELDHERLSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAATGLLMTPYVVTRYYRAPEVILGMGYQANVDIWSVGCILAEMVRHKILFPGRDYIDQWNKVIEQLGTPTQEFMMKLNQSVRTYVENRPRYTGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVEEALQHPY... | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. May play a role in the regulation of the circadian clock.
PTM: Dually phosph... |
Q91Y86 | MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPY... | Function: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death . Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SA... |
P45984 | MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPY... | Function: Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP... |
P53779 | MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPA... | Function: Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signal... |
Q15759 | MSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKCQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEA... | Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway . MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to d... |
Q9WUI1 | MSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKCQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGNDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSVFHGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPDDEPEA... | Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to di... |
P53778 | MSSPPPARSGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEALAHPYFESLHDTEDE... | Cofactor: Binds 2 magnesium ions.
Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokine... |
Q63538 | MSSPPPARKGFYRQEVTKTAWEVRAVYQDLQPVGSGAYGAVCSAVDSRTGNKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHETLSEDRIQFLVYQMLKGLKYIHAAGVIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKILFKGNDHLDQLKEIMKVTGTPPPEFVQKLQSAEAKNYMEGLPELEKKDFASVLTNASPQAVNLLEKMLVLDAEQRVTAAEALAHPYFESLRDTEDE... | Cofactor: Binds 2 magnesium ions.
Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokine... |
O22752 | MITRSRCRRSLLWFLVFHGGATATGAPSGGKELSQTPTWAVAVVCTFLILISHLLEKGLQRLANWLWKKHKNSLLEALEKIKAELMILGFISLLLTFGEPYILKICVPRKAALSMLPCLSEDTVLFQKLAPSSLSRHLLAAGDTSINCKQGSEPLITLKGLHQLHILLFFLAIFHIVYSLITMMLSRLKIRGWKKWEQETLSNDYEFSIDHSRLRLTHETSFVREHTSFWTTTPFFFYVGCFFRQFFVSVERTDYLTLRHGFISAHLAPGRKFNFQRYIKRSLEDDFKLVVGISPVLWASFVIFLLFNVNGWRTLFWASI... | Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity). Controls pollen tube reception in the female gametophyte synergids.
Location Topology: Multi-pass mem... |
O22757 | MGIIDGSLLRRLICLCLWCLLGGGVTVVTAEDEKKVVHKQLNQTPTWAVAAVCTFFIVVSVLLEKLLHKVGKVLWDRHKTALLDALEKIKAELMVLGFISLLLTFGQTYILDICIPSHVARTMLPCPAPNLKKEDDDNGESHRRLLSFEHRFLSGGEASPTKCTKEGYVELISAEALHQLHILIFFLAIFHVLYSFLTMMLGRLKIRGWKHWENETSSHNYEFSTDTSRFRLTHETSFVRAHTSFWTRIPFFFYVGCFFRQFFRSVGRTDYLTLRNGFIAVHLAPGSQFNFQKYIKRSLEDDFKVVVGVSPVLWGSFVLF... | Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67212
Sequence Length: 593
Domain:... |
O49873 | MAGPAGGRELSDTPTWAVAVVCAVMILVSVAMEHALHKLGHWFHKWRKKALGEALEKMKAELMLVGFISLLLIVTQDPVSRICISKEAGEKMLPCKPYDGAGGGKGKDNHRRLLWLQGESETHRRFLAAPAGVDVCAKQGKVALMSAGSMHQLHIFIFVLAVFHVLYSVVTMTLSRLKMKQWKKWESETASLEYQFANDPSRCRFTHQTTLVRRHLGLSSTPGVRWVVAFFRQFFTSVTKVDYLTLRQGFINAHLSQGNRFDFHKYIKRSLEDDFKVVVRISLKLWFVAVLILFLDFDGIGTLLWMSVVPLVILLWVGTK... | Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60875
Sequence Length: 544
Domain:... |
Q0DC45 | MAGGRSGSRELPETPTWAVAVVCAVLVLVSVAMEHGLHNLSHWFRRRQKKAMGDALDKIKAELMLLGFISLLLTVAQAPISKICIPKSAANILLPCKAGQDAIEEEAASDRRSLAGAGGGDYCSKFDGKVALMSAKSMHQLHIFIFVLAVFHVTYCVITMGLGRLKMKKWKKWESQTNSLEYQFAIDPSRFRFTHQTSFVKRHLGSFSSTPGLRWIVAFFRQFFGSVTKVDYLTMRQGFINAHLSQNSKFDFHKYIKRSLEDDFKVVVGISLPLWFVGILVLFLDIHGLGTLIWISFVPLIIVLLVGTKLEMVIMQMAQE... | Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60728
Sequence Length: 540
Domain:... |
P81785 | RIRARYPIIAAHLAPGSESRFDFQKYVNRSLEDDFKVVVGISPILWFFAVLFLLSNTHGWVAYLWLPFIPLIIILVVGTKLQVIITQLGLSIQDRGDVVKGAPVVQPGDDLFWFGRPRLVLFLIHFCLFQNAFQLAFFIWSVYEFGIKTCFHEKTEDIVRASGLVPNRDTSATQTTELSKGKLMMADTCLPTEDLVGMVVTAAHSGKRFFVDSIRYD | Function: May be involved in modulation of pathogen defense and leaf cell death.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24604
Sequence Length: 217
Subcellular Location: Membrane
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P93766 | MSDKKGVPARELPETPSWAVAVVFAAMVLVSVLMEHGLHKLGHWFQHRHKKALWEALEKMKAELMLVGFISLLLIVTQDPIIAKICISEDAADVMWPCKRGTEGRKPSKYVDYCPEGKVALMSTGSLHQLHVFIFVLAVFHVTYSVITIALSRLKMRTWKKWETETTSLEYQFANDPARFRFTHQTSFVKRHLGLSSTPGIRWVVAFFRQFFRSVTKVDYLTLRAGFINAHLSQNSKFDFHKYIKRSMEDDFKVVVGISLPLWGVAILTLFLDINGVGTLIWISFIPLVILLCVGTKLEMIIMEMALEIQDRASVIKGAP... | Function: Seems to be involved in modulation of pathogen defense and leaf cell death. Down-regulates broad spectrum resistance to powdery mildew fungus and its defense suppression activity is enhanced by Ca(2+)-dependent calmodulin binding. Signaling seems not to require heterotrimeric G proteins.
Location Topology: Mu... |
A1JPV7 | MKKILALLVIAPLLVSCSGNKNQADNEAFIKDTNGFEILMGQFAHNIENIWGLKEVLIAGPKDYVKYTDQYQTRSHINFDAGTITVETIATTDPAAHLRQAIITTLLMGDDPGSIDLYSDANDIQISKEPFLYGQVLDNNGEPIRWEWRAAHFADYLLQNKMQKRTSGLHVIWSVTLQLVPNHLDKRAHKYLPLVRQSAEKYGVEESLILAIMQTESSFNPYAVSGSDALGLMQVVQHTAGRDVFKMKGKSGQPSRSYLFDPANNIDAGTAYLSILQNTYLGGIQNATSRRYAVITSYNGGAGSVLRVFSSDKNQAVNII... | Function: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reduc... |
Q9HXN1 | MFALTAYRLRCAAWLLATGIFLLLAGCSEAKAPTALERVQKEGVLRVITRNSPATYFQDRNGETGFEYELAKRFAERLGVELKIETADNLDDLYAQLSREGGPALAAAGLTPGREDDASVRYSHTYLDVTPQIIYRNGQQRPTRPEDLVGKRIMVLKGSSHAEQLAELKKQYPELKYEESDAVEVVDLLRMVDVGDIDLTLVDSNELAMNQVYFPNVRVAFDFGEARGLAWALPGGDDDSLMNEVNAFLDQAKKEGLLQRLKDRYYGHVDVLGYVGAYTFAQHLQQRLPRYESHFKQSGKQLDTDWRLLAAIGYQESLWQ... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
Q3IHZ1 | MLKEKLIIIITLVMLLCACDIQEQSTQLAQIKAQNKIRVGTLASASNYYQAVQGEQGFEYELSQAFADYLGVELEIVPFFNLSDMFARLQSGDLDLIASGLTYNKTRAQQYRFGPTYRTISQKLVYKQGIERPRDYDDLTGNLMVIAKSSHSLTLQKVKKSNPELNWSETEEFDEEELLQAVIDGEIDYTLADTHTLSLFRRYHPNLSIGFSITHNDPIAWMLRKSNDDSLYALLVPFFGEAKQNNQLYVLEEKYFGHVRQFNYVNTLAYIEAIKETLPKYQPWFEQYAGTLDWRLLAALSYQESMWNPRAKSPTGVRGI... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
Q21KP0 | MTKILLNTASTVLTRLWKLSLLGLVFAVAAATLVSSRIPTTLEEVKSSGKLIVISRNGPTTYYEGPAGHTGFEYVMAKAFAKHLGVDLEVREIEDLGEMLDKVGTKAGHLAASGLTVTEKRARKVLFAEPYLQVTQQLIYRSGESKPETIEDLYGKRVMVISNSSHSERLKELQREYRDLAWEEQHDVDMLDLLEMVHNGKIDYTIVDSNAYQINRPVYPKATVAFDISEPQDLAWAFPQQKDASLYNEAQKFFKDIKQTGAIDDAMETFYGHLGEIDYSGAILFAHRLQSRLPKWETHLKAAAEKNDLDWQLLAALSYQ... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
A8GI11 | MKRLKINYILIGVVTLLLALALWPNITWRGGQGGQLEEIKSRGELRISTLNSPLTYFTTKQGPSGLDYELAKRFANYLGVKLVVIPHKNINDLFDDLDDDDADLLAAGLIYNQDRLSRARTGPAYYSVSQQLVYRLGTARPKTFADIKGKLAVASGSAHVSTLKQLKQSKFPDLSWEASSDLTSKELLEQVADGKLDYTLGDSVTIALLQRIHPQLAVAFDVTDEEPVTWYLKRGTDDSLYAAMLDFYSQMVDDGTLARLEEKYLGHVGSFDYVDTKTFLSAIDSVLPTFRSLFEKYASEIDWKLLAAIAYQESHWNPQA... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
Q9P353 | MADICPSRSEPTLSFTQGLILGQLSVVLLLAAFIKFFIFGDPPSPEVVASIRATDRRSRTLAHKKSILSLRETNALQLVQNPALNKKHVLRPGPPILTIGSILSKTYYKVDSHQPESLDWFNVLIAQTIAQFRSDAQHDDAILSSLSKALNGTARPDFLDEIKVTELSLGEDFPIFSNCRIIPVDEDGLSFGTGKAFDANMATREGARLQARMDVDLSDMITLAVETKLLLNYPKRLSAVLPVALAVSVVRFSGTLSISFIPSNPSNNEPAKMIFTFLDDYRLDFSIRSLLGSRSRLQDVPKIAQLVESRLHRWFDERCV... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria (By similarity). Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER... |
B6HDM7 | MALQQHEPAPFAPQSSLSFTQGFLLGQLSVVLLIGAFIKFFIFGEAPPPPSRGMSNRTTHRRYSSVYSPPQDSQKSLREKPSTSNVLRPVPSTSTNTRSILRKTYYSAIPTNPTSKHGRHRMHHSSHQPESLDWFNVLIAQTIAQYRETAYSLKDSPTSSILSSLTAAMNNPEKKPSFIDKIKVTDISLGEEFPIFSNCRIIAVDDPVSDGGRLQALLDVDLSDDNLSIAVETSMLLNYPKPRSAIIPIALSVSVVRFSGTLCISLIPASTEPPEPLQTPAGSPAPPTSDPRDNAGNRPPGPGEHTASQDELPPKSSPKS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q0TYM0 | MATQVATPLSPSYTSELIIVCHHVLQHSPTPLTPHSLSFTQGFLLGQLSIALLIFFFIKFFIFGEPPSADDRSLHLNSLRRARTLAHQQSIKQLRTRSNSISLSLRHKDSRSIIRKGEETRGGPSIATILAKTYYNVKGHQPESLDWFNVLIAQTIAQLRADARQDDAILGSLTEVLNSGSKPDWIGEIKVNEIALGDEFPIFSNCRVMPAEDGFWYGPGTTGTEEGRLQARMDVDLSDVITIGIETTLNLNWPKPLSAVLPVALAVSIVRFSGTLALSFIPSSSPPSTSTTTPNPEHHRSNSTTSSSTSPPHRPTTLAF... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A5DGW8 | MQVLNFYVNPYLNLSFDLLPVANHFCRYSRHWKMSRDITRPDELASLIQLQDRLQTQQDELFRKQQELQFRETYAGTGSTKSFTQGLIIGQLSVIILLGIFIKFFVFADSSTTSSTSGNGISSKTDVSNILVKRKKNGDGDAGSEGRSDEVDTILEKTYYDVDNHAPESLDWFNVLIAQTISSFRYEALQSDNIYHSLKEFLSKSELPDYLGDIQLTEIDIGDDFPIFSNCRIRPSKDSHGRLEAKIDVDLSDTLTMGIQTKLILNQPRPLTAVLPISLSVSIVRFSGCLTVSLINTNEEEFSEPRVAMDSPQSTRDDNS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
B2VVB9 | MADEVPTAVPLATPAGSSSLSFTQGFLLGQLSIAILIFCFIKFFIFGEPPSADDRALHLNSLRRARTLAHQQSYKQLRTRANSTSLSLRHKPSTSIIRKGEETRGGPSIATILAKTYYNVKGHQPESLDWFNVLIAQTIAQLRADARQDDAILTSLTEVLNTGSKPDWIGEIKVTEIALGDEFPIFSNCRVMPAEDGFWYGPGSTGNDKERLQARMDVDLSDVITIGVETTLNLNWPKPMSAVLPVALAVSIVRFSGTLAMSFIPSSSPPSTTAPMPSPTSNTHRSSSPSRPASSSGAPPHRPTTLAFTFLDDYRLDLSV... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
B6K6N3 | MVQLFHLTFTQGFFIGQLSVIVIVYIFLRFFLFCTKEELKNVQEESYPLSPSNEKSTTEFNDATHKVTPSLSEIYDVKTHEEESLDWFNVLVAQALSQIRQDAVSDDAALKKLQTLFNGKRKPSFLGPIHIKSISLGQRYPVFSNCRIQAQPDDTNGLRATMDLSLEDDIHFVVNTSAVLNVPRPAFAMLPVSLSVRIVHIRGKLSIYFSQSSKSAKRAYLNFTFDPDFDMGIEIQSLVGSRSKLQDIPKIAHIIETRIRKWFITRCVSPQFQQISIPNIWPSSAREGHRQKSTE | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
O74368 | MIHLPQGSFTQGLIVGQLLTLAIIYVFLRFFLFCSPIPKSVANSPKQTGNETPDETPSTPLSNNKKRYKKPLTILEPHILNLLYDVNEHEPESLDWFNVLIAQALIQFRYDACSNDVALRKLETVLNKGAQDKSMVDHIYVRDLSLGDGFPVFSHCRVLPHQHNSSQLRAEMLVSLTDNINCTVDTKLLLNFPKPAFATLPLSITVRICKFVGKIMIYFSPSNGAGQPAYMNLSFDPNFVISLQVSSLVGARSKLQDIPKITQLIESRIRQWFTNRCVSPQFQQIAIPNLWPTSAKEGHARSHAPQEESSNED | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A7E559 | MWLDDVASELSFTQGLLLGQLSIVILIGAFIKFFIFGDPPSPDVSAALRATERRSRTLAHKRSLLTLRSSTPRHASQSLNRKRSSVLRNPAPLTTNAILSKTYYNVDSHQPESLDWFNVLIAQTIAQFRADAQHDDAILTSLTKALNGGNRPDFLDEIKVTELSLGEDFPIFSNCRVIPVDEDGITLGREGGAAGREHGRLQARMDVDLSDFITLAVETKLLLNYPKPLVAVLPVALAVSVMRFSGTLSISFVPGSPLNGSPTTLAFCFLDDYRLDLSIRSLVGSRSRLQDVPKIAQLIEARLHTWFDERCVEPRFQQIE... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
Q4P8B7 | MQQPQQQDLQIGLPYAPVQPPIPSPAAYFAYLPSPSRWTFTQGLIVGQVSMVIVALLLIRYVIFEDSATALEKERLMRLKVSQRRSKLHAKALLQDARKANSAAASAAAAAAPSPASHPLRKSHRLASDTRASMFANILDKTAYDLSSHLPESADWLNVMFAQAIAGYREDVLTGGVSSHHHTASDAIPSPNPLEPQKERTARDLMEEILNRATSSFLDPIRVTEADFGDAYPIFTNARVRPADDTGRTRIEIDVDYSDQITLAIDTKLLINFPKPRFAVLPVSLGLTIVRFSGTLAIELFSSDPNATVLPTANPNPSSS... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
P9WJU6 | MPSPAGRLHRIRYIRLKKSSPDCRATITSGSADGQRRSPRLTNLLVVAAWVAAAVIANLLLTFTQAEPHDTSPALLPQDAKTAAATSRIAQAFPGTGSNAIAYLVVEGGSTLEPQDQPYYDAAVGALRADTRHVGSVLDWWSDPVTAPLGTSPDGRSATAMVWLRGEAGTTQAAESLDAVRSVLRQLPPSEGLRASIVVPAITNDMPMQITAWQSATIVTVAAVIAVLLLLRARLSVRAAAIVLLTADLSLAVAWPLAAVVRGHDWGTDSVFSWTLAAVLTIGTITAATMLAARLGSDAGHSAAPTYRDSLPAFALPGAC... | Function: Required for export of phthiocerol dimycocerosate (PDIM) to the cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95122
Sequence Length: 920
Subcellular Location: Cell inner membrane
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P9WJU0 | MVGCWVALALVLPMAVPSLAEMAQRHPVAVLPADAPSSVAVRQMAEAFHESGSENILVVLLTDEKGLGAADENVYHTLVDRLRNDAKDVVMLQDFLTTPPLREVLGSKDGKAWILPIGLAGDLGTPKSYHAYTDVERIVKRTVAGTTLTANVTGPAATVADLTDAGARDRASIELAIAVMLLVILMVIYRNPVTMLLPLVTIGASLMTAQALVAGVSLVGGLAVSNQAIVLLSAMIAGAGTDYAVFLISRYHEYVRLGEHPERAVQRAMMSVGKVIAASAATVGITFLGMRFAKLGVFSTVGPALAIGIAVSFLAAVTLL... | Function: Required for the biosynthesis of polyacyltrehalose (PAT) and the transport of diacyltrehalose (DAT) and possibly PAT to the cell surface.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 106415
Sequence Length: 1002
Subcellular Location: Cell inner membrane
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A0QP18 | MMRLSSTLRRFRWAVFATWLLLLVPSIYLALNQSSNLTGGGFEVEGSQSLHVQRQLEEHFPDQGASPLALVAAPRADASYEDMNAAVVHLEKLAAEVPSVKIVPNPQQPAPQPDRPYVITLQLDFNNTGAVDVAKQLRQKVGIHGEEPGESQNGKVKFYVIGQGALGAAATQATKHDIAAAEKWNMPIVLIVLLAVFGSLAAAALPLVLGVCTVVVTMGLVYLLSMFTTMSVFVTSTVSMFGIAVAIDYSLFILMRFREELRAGRDQQDAIDAAMATSGLAVALSGLTVIASVTGIYLINTPVLVSMATGAILAVAVAVL... | Function: Contributes to cell wall biosynthesis and biofilm formation. Transports the mycolic acid-containing lipids monomeromycolyl diacylglycerol (MMDAG) and mycolate ester wax (WE) to the bacterial surface.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102692
Sequence Length: 954
Subcellular Loc... |
Q6NE78 | MDINEKAPGPSGRRPARRRDGGGQVLVLYLAIAVVVAVLAWPWLAPRLGSFPGSLLSWIGDGGSVGAPRPATLDERMDMVEAALAPLAMRIAEADRRLAMLEANPRTAGEDPRKEAAGVSADPEQMSWMAAEIATLKGDLEIVRKLAADEGGATKLSGAVEKAEAAFRRIAERRDRAPLFLAALGQLREAVDRGSPYPAQMKAAMILAEKGTADKLAPLVMGSATGIVTRVGLAESFRVTAAAARKLDVPADSGWVPPNIRRWLGGAVLIRRTEGGEEGLDGILNSTSRLLAGGDLAGAAALLRRAEGPSLAAIQPWLEA... | Function: The 4 genes of this operon collectively influence magnetosome size and number.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36376
Sequence Length: 347
Subcellular Location: Magnetosome membrane
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Q3BKD5 | MLLRLIVLLIFMSPVVFATLWFSDNVGSVQVEWLGWHVDSNMPVLLAVILVVFLIFSALSRLSALVADLPSKLGKSRQARGLEKGMSALLAALDAAESGDVGEGRRFAAEAARLLNNPGLAARLDRLLPRPPAQPVAPTRLEAAKGRLFARKPGPPPPPTPVVDKIQPVVVEKLAAAPAGPSREDLEAFSAKIRAGEWGAAQAWIGEAVLAGRLTPLVAARWRSVALEGQALEASPGDPARPLRLAREAMAADQTFLPPALHVIRAEVSEGRKAEAETLLASVWPHVPARVLLDACAPLWRDEDQDACLKRLEALAAIAP... | Function: Overexpression in wild-type cells increases the number of cells with double magnetosome chains significantly. The 4 genes of this operon collectively influence magnetosome size and number.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 48032
Sequence Length: 449
Subcellular Location: Magn... |
P38257 | MSQIVDFVEDKDSRNDASIQIIDGPSNVEIIALSESMDQDECKRAHVSSAEMIPSSPQRKSVSNDVENVDLNKSIELSAPFFQDISISKLDDFSTTVNSIIDSSLRNENNAKGNAKKLLDDLISDEWSADLESSGKKHNKSQYNLRDIAEKWGVQSLKNPEPIAVDCEYKTQGIGKTNSDISDSPKSQIGAADILFDFPLSPVKHENPTEEKHNSIANENSSPDNSLKPAGKQNHGEDGTSMAKRVYNKGEDEQEHLPKGKKRTIALSRTLINSTKLPDTVELNLSKFLDSSDSITTDVLSTPAKGSNIVRTGSQPIFSN... | Function: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably o... |
Q2W8J4 | MLSAKGVSLGLGLGLGAWGPVLLGVVGVAGAIALYGYYKNRNAEPAAAEAV | Function: Might be involved in magnetite crystal growth.
PTM: Seen in gels as a band of about 5 kDa, with an N-terminus that corresponds to residue 8, suggesting it may undergo N-terminal cleavage.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4987
Sequence Length: 51
Subcellular Location: Magneto... |
Q2W8R5 | MGEMEREGAAAKAGAAKTGAAKTGTVAKTGIAAKTGVATAVAAPAAPANVAAAQGAGTKVALGAGKAAAGAKVVGGTIWTGKGLGLGLGLGLGAWGPIILGVVGAGAVYAYMKSRDIESAQSDEEVELRDALA | Function: Promotes the formation of magnetite in Fe(2+)-rich conditions, when magnetite is not readily formed . Binds Fe(3+) and Fe(2+) (Probable). May play a role in nucleation of magnetite crystal formation (Probable) . May help control production of crystals with a specific morphology (Probable) . Greatly improves ... |
Q7QC84 | MALLRLVATECRNVLQRGYSTASVPTTKMFIDGKFVESKTNDWIDLHDPATNEVVTRVPKCTQDEMQTAVESSKKAYKTWRQSSILSRQQVMLKLQHIIRNNMSELAKNITKEQGKTLIDAEGDVLRGLQVVEHCCSITSLQMGETVPNIAKDMDTYSYHLPLGVTAGIAPFNFPAMIPLWMFPVAITCGNTSIIKPSERVPGATMLLMEMLNEAGCPPGVVNVIHGAHDAVNFVCDNPDIRAVSFVGSDQAGKYIYERAGRNGKRVQCNMGAKNHGVIMADANKENTLNQLAGAAFGAAGQRCMALSTAVFVGEARNWI... | Function: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity).
Catalytic Activity: 2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + hydrogencarbonate + NADH + propanoyl-CoA
Sequence Mass (Da): 56714
Sequence Length: 521
Subcellular Location: Mitochondrion
EC: 1.2.1.18
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Q0WM29 | MVRVKQKNLESYRSNGTYPPTWRNPTTSFAPDQHRVSIHSSLKSKTKRRRLYKEADDNTKLRSSSSTTTTTTTMLLRISGNNLRPLRPQFLALRSSWLSTSPEQSTQPQMPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN... | Catalytic Activity: 2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + hydrogencarbonate + NADH + propanoyl-CoA
Sequence Mass (Da): 65927
Sequence Length: 607
Subcellular Location: Mitochondrion
EC: 1.2.1.27
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P52713 | MLSRLARVQPKCQQLAHFSTSKSAAAAPTVKLWIDGQAVESKTTDFVELTNPATNEVIAMVPNATQAEMQAAVDSAKNAFNTWKNTSPLTRQQCMFKLQALIKRDMKKLAESITIEQGKTLPDAEGDVSRGLQVVEHACSVPSLMMGETLPNVSRDMDTHSYRIPLGVTAGICPFNFPAMIPLWMFPVALATGNTMVIKPSEQDPGAAQLLVELAKEAGVPDGCVNIIHGQHSAVNFICDNPDIKAISFVGGDAAGKHIYERGAKNGKRVQSNMGAKNHGVIMADANKEQTLNQLTAAAFGAAGQRCMALTTAVLVGEAR... | Function: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity).
Catalytic Activity: 2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + hydrogencarbonate + NADH + propanoyl-CoA
Sequence Mass (Da): 56462
Sequence Length: 523
Subcellular Location: Mitochondrion
EC: 1.2.1.18
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Q54I10 | MLSFKFAKSASKVIGNRNFHSSSASLANTTKLFINGKFVESKTKEWLEVRNPATQELVTKVPVSTKEEMEAAVKAASDAFPAWRDTSVSNRSRIISNYKNLINKNMDKIAAIITEEQGKTLPDAKGDVFRGLEVVEHSVNVASLMMGETVENVSKNVDIYSYVQPLGVCAGITPFNFPAMIPLWMFPLAIACGNTFVLKPSERVPSASMFLVQLAQEAGVPDGVVNVIHGGKEAVNFICDAPEVRAISFVGADQAGRHIHARGTANGKRVQSNMAAKNHATIVPDAHKERTLDALTGAAFGASGQRCMALSAAVFVGESK... | Function: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA (By similarity).
Catalytic Activity: 2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + hydrogencarbonate + NADH + propanoyl-CoA
Sequence Mass (Da): 56696
Sequence Length: 528
Subcellular Location: Mitochondrion
EC: 1.2.1.18
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Q02252 | MAALLAAAAVRARILQVSSKVKSSPTWYSASSFSSSVPTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMAL... | Function: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Catalytic Activity: 2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + hydrogencarbonate + NADH + propanoyl-CoA
Sequence Mass (Da): 57840
Sequence Length: 535
Subcellular Location: Mitochondrion
EC: 1.2.1.18
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P28810 | MSVPVRHLIAGAFVEGLGAQRIPVSNPLDNSTLAEIACASAEQVEQAVASARETFASWKETPVSERARVMLRYQALLKEHHDELAKIVSSELGKTFEDAKGDVWRGIEVVEHACNVPSLLMGETVENVARNIDTYSITQPLGVCVGITPFNFPAMIPLWMFPLAIACGNAFILKPSEQVPLTSVRLAELFLEAGAPKGVLQVVHGGKEQVDQLLKHPQVKAVSFVGSVAVGQYVYHTGTAHNKRVQSFAGAKNHMVIMPDADKAQVISNLVGASVGAAGQRCMAISVAVLVGAAREWIPEIRDALAKVRPGPWDDSGASY... | Catalytic Activity: 2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) + hydrogencarbonate + NADH + propanoyl-CoA
Sequence Mass (Da): 53663
Sequence Length: 497
Pathway: Amino-acid degradation; L-valine degradation.
EC: 1.2.1.27
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P63936 | MTTIAFLGLGNMGAPMSANLVGAGHVVRGFDPAPTAASGAAAHGVAVFRSAPEAVAEADVVITMLPTGEVVRRCYTDVLAAARPATLFIDSSTISVTDAREVHALAESHGMLQLDAPVSGGVKGAAAATLAFMVGGDESTLRRARPVLEPMAGKIIHCGAAGAGQAAKVCNNMVLAVQQIAIAEAFVLAEKLGLSAQSLFDVITGATGNCWAVHTNCPVPGPVPTSPANNDFKPGFSTALMNKDLGLAMDAVAATGATAPLGSHAADIYAKFAADHADLDFSAVIHTLRARADA | Catalytic Activity: 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + H(+) + NADH
Sequence Mass (Da): 29679
Sequence Length: 294
Pathway: Amino-acid degradation; L-valine degradation.
EC: 1.1.1.31
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Q4L4W5 | MEIIMIFVCGILASISVYLVLSKSLIRIVMGTTLITHASNLFLITMGGLKHGEMPIYEKNISQYVDPIPHALILTAIVIAFATTAFFLVLAFRTYKELGTDNVERMKGVLDDD | Function: Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12522
Sequence Length: 113
Subcellular Location: Cell membrane
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Q8ABF5 | MNIAALLSGGVDSSVVVHLLCEQGYKPTLFYIKIGMDGAEYMDCSAEEDIEMSTAIARKYGLSLEVVDLHKEYWENVAAYAIDKIKKGLTPNPDVMCNKLIKFGCFEQQVGKNFDFTATGHYATTIRQDGKTWLGTAKDPVKDQTDFLAQIDYLQVSKLMFPIGGLMKQEVREIASRAGLPSARRKDSQGICFLGKINYNDFVRRFLGEREGAIIELETGKKVGTHRGYWFHTIGQRKGLGLSGGPWFVIKKDVEENIIYVSHGYGVETQFGSEFRINDFHFITENPWKDAGKEIDITFKIRHTPEFTKGKLVQEEGGQF... | 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): 39741
S... |
Q8RAH7 | MEVNNRVVVGMSGGVDSSVTAYLLKEQGFEVIGVTMRVWVDPYGKARDDDKSCCSLKAIHDAKKVAEILGIPHYTVNLSEVFYDKIVKYFIDEYLKGRTPNPCVFCNRFIKFGDLLEKAHELGAYYIATGHYVRKEYDEDRKRYLLKKGLDFKKDQSYMLYRLTQEQLKHALFPLGNYTKEEVRALAEKIGLPVADKRESQEICFIPDNDYKAFIKRQIKKDVKPGEFRDIHGNFLGYHKGIINYTIGQRKGLGLSSDRPLYVVDIDPENNVVIVGHQEDVWGEELISSNNNFISIEKLEEEIKVTAKIRYTAKEDEAII... | 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): 41666
S... |
Q896F5 | MVKKMKKKVVVGMSGGVDSSVTAYLLKEQGYDVIGMTMKVFPGNYHDGSKEKIEDIMKSAKEVCDFLEIPFVEVDLIEEFNKKVATPFMQDYIEGRTPNPCVYCNKHIKFDAFLNKAIELGADYIATGHYANIIEKDGRTLIYRAEDENKDQTYMLYNLKQHQLKHILMPCGDYNKEQIREIAKKIGLKIHNKKDSEEICFIPDDDHGRYIRENCKKKIQEGNFVDEKGKVLGRHKGIINYTIGQRKGLGIALGKPAYVIDIIPEKNQVVLGEEEKIFNNILIAKDVNFIPFDELKEKIKLEAKIRYSAKGEIAEIEPLE... | 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): 41266
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Q8R5X3 | MVETKSIAPEFKKYLKFDSNNSNIRVGVAMSGGVDSSTVAYLLKQQGYDIFGVTMKTFKDEDSDAKKVCDDLGIEHYILDVRDEFKEKVVDYFVNEYMNGRTPNPCMVCNRYIKFGKMLDFILSKDASFMATGHYTKLKNGLLSVGDDSNKDQVYFLSQIEKNKLSKIIFPVGDLEKTKLRELAEQLGVRVYSKKDSQEICFVDDGKLKQFLIENTKGKAEKPGNIVDKNGNILGKHKGFSFYTIGQRKGLGISSEEPLYVLAFDRKTNNIIVGQNEDLFRDELIATRLNLFSVSSLEGLDNLECFAKTRSRDILHKCLL... | 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): 40882
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Q2LWA6 | MISVMAPGSEKTGKVETILKKRVLLAISGGVDSSVAALLLKEEGYEVAGVTMCLGVREEENKVRCCGREAIEDARGVCEILGIPHYVLDYAPLLETCVIDKFVREYRLGRTPNPCIDCNRYLKFGHLLDSARTMGFDYLATGHYAKIERKESRWILKKAKDLVKDQTYFLYPIPVAALEHILFPLADRTKDEVREIARQALLPIAEKPESQDLCFVTQDSYRDFLQEQGCPVHPGPIVDRSGRVLGEHSGTVFYTIGQRHGLGISSPFPLYVVAIDVAGNSVIVSGKEDVYAQGLVAGEMNWLTPERPQEAEARIRHRKR... | 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): 41427
S... |
B0KC14 | MKKNNRVVVGMSGGVDSSVSAYLLKEQGFDVIGVTMQIWQDKDEEAVRVEGGCCSLSAVNDARRVANKIGIKYYVMNFKDVFKEKVIDYFVDEYLKGRTPNPCIACNKYIKFEELLKRAWMIDAYYVATGHYAIKEYDEERGRYLLKKSVDTSKDQTYVLYNLTQTQLEHILFPLGKYKKDEVRELAKNLGLPVASKPDSQEICFVTDNDYGKFIRENAKEEIKPGEFRDTRGRFLGYHKGIIHYTIGQRKGLGISVGKPLYVVDIDAENNVVVLGYGDEVFGDELISYNNNFISIDKLEREMRVKAKIRYNAKEQDAVI... | 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): 41541
S... |
A8ES36 | MNKNKKIVVGMSGGVDSSVTALLLKQQGYDVVGLFMRNWEYGIKGSQCPNRIEFEDAKKVGALIGIEVRGKDFVKEYRDRVFDVFLEGLKQGLTPNPDILCNKEIKFNVFLNEAKSMGADMIATGHYAKIAKYKDHFVLDTPKDNTKDQSYFLHALSSEQLSHAMFPLGDLTKKEVREIARAHNLPVSDKKDSTGICFIGNQKFDEFITQHLQAIPGDILDENGKVIGKHKGLVCYTLGQRKGIGLGGIKGNESENNTHKPWFVASKDVVNNTLTIVQDTNHPLLMSKTVEASHMHWVLEEAPKVGDKLMAQVRYRQQKQ... | 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): 40963
S... |
Q8A2F1 | MMEENKRVLLGMSGGTDSSVAAMRLLEAGYEVTGVTFRFYELNDSTEYLEDARHLAERLGIRHITYDAREIFRKQIIEYFVHEYMVGHTPVPCTLCNNYLKWPLLSKIADEMGIFYIATGHYVRKVKVDDTCYITYAADSDKDQTFFLWGLKQDILRRMLLPMGDITKVEARAFAAERGFQKVAVKRDSLGVCFCPMDYRSFLKMWLVSNCQPQVSVGQPQVSAGQTWSAEVRRGRFVDEKGDFIAWHEGYPFYTVGQRRGLGIHLNRAVFVKEIRPEKNEVVLASLQALEKTEMLLKDWNIVNRERLLGHADIIVKIRY... | 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): 42348
S... |
Q11UP4 | MSKKGRVLVAMSGGIDSSVAAVMLHEQGYEVIGMTMKTWDYANLGGSKKETGCCSLDSINDARNIAVSLGFPHYIVDIREEFGDYVINHFNKEYLDGRTPNPCVLCNTHIKWDSLLRRADKMDCDFIATGHYAQVRSENNRFVISKGLDENKDQSYALWGISQQSLSRTMFPLGHLHKTDIRAMAAERGFMDLVNKSESYEICFVPDNDYRGFLKRRNPGLEEEVRGGEFVMEDGTVVGKHEGYPFYTIGQRKGLGITLGYPVFVTEIQKENNRVVLGREEGLNRNGMWVDQLIMSKYENLKGIQKQSITKVRYNDDGTS... | 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): 41459
S... |
A5FR85 | MSDSSELVMVAMSGGVDSSVTAMLLLEQGYNVAGVSLQLKSNNEPYGNGYNLKLINRAREVAAALNIPHYVVDLSDIFSQRVIADFCQQYSQGRTPNPCIRCNYYVKIGALLNKIQDFKADYLATGHYARIVSDENGTHLLRGADGKKDQSYFLYTLPPESLSRLMFPLGQKYKKDIVRLATNMKLPVSQKESQDVCFIPDGDYKSFLATRMGFTPGKILDTTGKILGEHQGLPLYTVGQRQGLGLASNEKLFVSDMNADANTITVAGHDQLYTSRILLSNFIWRESGIPLDTSGMIVKVRYKAAPAEVKKISQSGDFYI... | 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): 39077
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Q9RTK1 | MTAFPAAPDLAPPSRAAQGERVLCAMSGGVDSSVTASLLKEQGYQVIGAMMRFWPDDKRTDTFDSCCSPDAAYEARRVAEQVGVPFYLLDYREPFQRHIVGPFLEEYARGRTPNPCVNCNTKVKFDELVKKAKMLGCRYVATGHYVKRVDNAQGEVEFHRGDDPRKDQTYFLWGTPRDALPYILFPVGELEKPQVREIAAERGLLTAQKPESQNICFVPGKVQDFVAEHLPQAQGYIREIATGEVVGEHLGTQFYTLGQKKGLGLYQSHRVRHVVHLDPDSNTVWVGDYDDCLWTGLKATDANYLLDLAELPTELEVQVR... | 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): 42184
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B1I677 | MATVAVALSGGVDSSTTALLMKEAGHRVFTLTMATNDRVAAEAARVSAFLGLPHHVLDISGLFEQRVIGPFCAAYLEGRTPNPCIACNRDLKYGTLFRQAVEWGADYFATGHYARVRFEPEPGRYVLLRARDPRKDQSYVLFYLDQERLARLLLPLGDLTKETVREKARAAGIPFTAAESQEICFVAGDDYRTFIRRRCGQAVAEGPFVDRQGNVLGRHRGIPFYTIGQRRGLGLALGRPVFVLGFNRERNAVIVGPEEELWHTAFLAVDVHYILPQPAGGTLIEAQIRYRAKAAPARLYPQPPDAARVVFEKPQRAITP... | 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): 37813
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A9A0S9 | MPLMNPLNPWPLESSNPLIAVLVSGGIDSLVAAHLLKQSGADVTAIHFLTGYEPEDRAGRLEKLFTQMDIPVFIFDCRTVFQSNVVDYFTAAYLRGETPNPCMVCNSRIKFGACMDYARSLGADAVATGHYCRTTKDPDGVRLWKGADPAKEQSYFLAFLSQDQLGRARFPLERMTKDQVRAHAARHGLVPIESKESQDVCFIRGEECADFIEAQVPAIPGPGPIEDMTGRLIGTHSGLHRFTVGQRRGINCPAEQPYYVAALDMARNCLKVGFRQDLFVPVCRVAQVNWIPDRPKGSMNVSVKIRYNQTEVPARLTALG... | 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): 39281
S... |
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