ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q3JAF1 | MGRVLVTIFVLFWPIGSFAAINLDRIVAVVNEDIVLESELEQMVRTVQDQLAAQGTSLPPGYVLERQVLERLVMEQLQLQLAARTGIQVGDETLNEALGRIAQDNGLTLSQFRNVLEQDGYDFPAFRENIRKELIISQLHKREVNDRVSVSKAEIDNFLTNQKKRGNQDAQYHLAHILITVPEAASPEQVQAAKAKAEQVLQQLREGADFQKVAVTYSDGQQALEGGDLGWRKMGQLPTLFVDVVPQLQAGDISKLIRSPSGFHIVKLLDYRGEGQQQLVTQTQARHILLRADELASEREVQLRLSQLRQRILSGDDFSE... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q145L3 | MKKLRLATLAAGLAAAASFLSVAPVQAQALSGSGGQTVDTIAAVVNNGVITRRELDERMGLITRRLNQQNAPVPPMDQLRQQVLNQMVLERIQLQKAKEDGITIDDATVQKTLERLAAANNLTLDVYRSRIEAQGVPWTTFTSDARTELTLSRLREKEVDSKVTVSDAEVANYIASQRGPNAGLTSDLHLQHIFLKAPLNASETDIEAAQRKAQALLAEAKGGANFEKLAKSNSQAPDASKGGDTGFVSPSKLPPEFVKAASALRPGEVNPDLIRTSDGFEIVRLVDRRAGQGTSSDAPKLVQTHVRHILLRVGDGMSEP... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q121Q4 | MTNDRLFAGIARVLSVRPLAAALALLLTLPLIGVQAQSLRPSSGLRLPTPAASAGAAAGSASGQRQADFIVAVVNSEPITNSEVRTKLVRTEQQIIQQGSPLPPRRELVPQVLERLISDKAQLQLARSAGMRVDDNAVEAAVQTVARQNQISVDELRRRLKADGIAYSQFESDLRDELLVSRLRQREVDLRVTVTEQDIDQFLREQEGGTELSSLALNLAQILVAVPENATPGQVAALQAKAQQVMDKARGGADFAALANEFSDSPTRGTGGLMGLREADRYPPLFVESTKSLKVGGLAGPIRSGAGFHILKVIEKRQAG... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q9PIK6 | MKEILITNDDGYESEGLKKLIKMLTKEFKAKITIVAPASEKSACSHSITLTKPLRFVKVGKRFYKLDDGTPADCVYLALHALYKKRLPDLVISGINKGANVGEDITYSGTCAGAMEAVLQGIPAIALSQFYKKSEKELDYKNALQITKKIIQNIFDKGFPLEKKEFLNINFPAKSKIKGIKICKAGKRVYNFEAHSNVNPRGVEYYWLAAANLDFEDEKNSDIALLKKGYATITPIMLDLTAYERMKKVKKWLKANDE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 29013
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q3ADI0 | MRILLTNDDGIYAPGIKALRQVLEKEGKYELTVVAPDREKSATGHGITVHRPLRAFDITFKNSKVRGVSVDGTPADCVKLAVEALLDKPPDLVLSGINSGPNLGTDVLYSGTVSAAIEAMINGIPAIAISMGSFAFEDEEYLRAAEIFARLLPRILEHPWPRDTILNINIPNVPLEEIKGIAITRLGVRKYINVFEERKDPRGLSYYWMSGEAVNYENGQDTDTAALARKEISITPVHFDLTNYHYLNELKTWVKALEGALATG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 29104
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q9A6T5 | MRILLTNDDGIHAPGLQALEKIARALSDDVWICAPEYEQSGASRALTLADPIRVRKLDSRRFAVEGTPTDCVMMAVQHLIEGGRPDLVLSGVNRGQNIAEDVTLSGTVAGAIEGMAMGIPSIALSQSMNYFHDEIVAHWETAEAFAPGIIQRLLEVGWPADVVMNVNFPALPPESVKAVEVTRQGFRDGHMRHMDKRTDLRGRDYYWMGFTAKASQPAEGTDLRAVYEGRISVTPLHIDLTHNETVHTLKGVLGGAPPRKVGA | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28671
Sequence Length: 263
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q3J3D0 | MRILITNDDGINAPGLEVLEQIALELAGPEGEVWTVAPAFEQSGVSHAISYTHPMMIAKLGPRRYAAEGSPADCVLAALYDVLQGARPDLVLSGVNRGNNSAENVLYSGTVGGALEAALQGLPAIALSQFLGPETEGLADPFECARTHGARIVRLLLERGLWDGEDYRLFYNVNFPPVPAANLRGHRVAAQGFRRDTSFGVEPHMSPSGRRFLWIRGGAQQSPTLPGTDAAVNLEGFVSITPLRADLTAHDRLAELEALIG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27888
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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B8G513 | MYILVTNDDGYQSPGLAALRAVLSEIGEVAVVAPDRNWSAAGHYRKLFDPLRAWEGTLSDGSPALICDGTPADCVALAILGLLDRKPDLVVSGINLGANLGTDLLYSGTVAAAMEGIVFGVPGLAVSQIRPKDGQWDFRAAQVAVRRLVMLIRERGLPPELLLNLNIPAVTPETLRGIKVSRLGRRVYRDELVVRYDPRGRPYYWIDGAEPEDHCEEGTDIAAISEGYASLTPVQMDLTSHRWLEELRRWEWE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27891
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q2RJD1 | MLILVTNDDGINAPGIKALSRSLARVGRVAVVAPEKERSAIGHGITMHKPLRATEVTWEGPVEMALAVNGTPADCVKLALDALLDEEPSLVVSGINMGANLGTDVLYSGTVSGALEGCINGRPSLAVSLAGEGGVDFSFAADFTSRLAGVIIKRGLPAGTLLNLNIPCLPPGEIKGLAITRLGRRRYCNTITRRLDPRGRAYYWLAGEVEDLDQEPDTDIGALGQGRISITPLHLDLTNYSYQQELAAYLSFLWPGQGNR | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27647
Sequence Length: 260
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q1D402 | MSNKPKRILVSNDDGYFSEGLQALVEAVSPLGEVWVVAPDREQSAASHAISLHRPLRIKEVRERWFAVDGTPADCAYLAINHLLKDDRPVLMVSGINHGANLAEDIMYSGTVAAAMEGALLGVPAIAFSLVARRNFDFAPGARFARSLVSSALSRPLPPRMLLNVNIPGGVEPEGYVVTRQGRHSYGFEVVENEDPRGRKYYWIGGSDYQHEDIPGSDCNAVFRDKRVSVTPLHFELTDHGRLPDLSGWQVDGFNRHEPDGA | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28829
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q3INV7 | MDVLLTNDDGIDAVGIRALYDALAEVADVTAVAPADDQSAVGRQLSRTVELHDHELGYAVEGTPADCVIAGLGALDLDPDIVVAGCNEGANLGEYVLGRSGTVSAAVEAAFFGVPAIAASVYFPAGDVTIEEFDPDKTDFAEASRAVRYLVDNAIGAGVFDAADYLNVNAPLPPETGHAPMEITEPSHVYEMDGERDGETVRIQDHIWERMAEGTIPDPPGTDRRAVVEGRVSVSPLTAPHPTTGHEGLAGLAEKYQ | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 26966
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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B2A4J5 | MKVLLTNDDGIYAPGIFAMAKEIASRDEFEAVVVAPDREQSATGHAITVHKPLRVNNVKKLGEKLEIPFYSVNGTPSDCVKLAVESVMDEKPDLVISGINRGANLGTDVLYSGTVSGAMEAAILNIKSIAVSLVDYDYEDYSTAASYTAYIANIIKDNPEEFENGTLLNVNVPAVEANQLKGVKITRQGFRQYENIFEKRFDPRGKAYYWMAGKVIEDTSDIKTDVASVKENYVSVTPIKYDLTDYNLYNSLSNWEFDD | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28723
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q9JYP8 | MNVLISNDDGYLSEGIAVLARVTAEFANVRVVAPERDRSGVSNSLTLERPLQLKQAQNGFYYVNGTPTDCIHIGQSVFSDFQADFVFSGINRGANMGDDTLYSGTVAAATEAYLMGIPAVAFSLNDASGRYWATAEQALWTLLAHFFKNPPQSPILWNINIPAVAPEDVRGIKIARLGRRHHGQNVIPARNPRGEQIYWIGPVGEVSDREEGTDFGECGAGFITVTPLQIDLTAYPDMAETAAFWHAD | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27034
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A6Q4L7 | MKRILITNDDGFESLGLRALIEALRDIAQLTIVVPANEKSACGHSLTLTKPLRFVEIEDNFYKLEDGTPTDCVYLALSSLYPDGEKPDIIVSGINRGANMGEDITYSGTVAGAMEGAIYDIPSIAISQVCNSNCEETEMEVGYEQAKYVARDLVEKIFQQGWPAGHRRCLNVNVPPTKEFKGYKITRAGYRVYFNQAHLHRNPRGIEYWWLGLHPLDWIPGKERDCDFEAVKEGFVSITPIKADLTAYEEIPKLKSWL | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 29021
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q9PF20 | MRVLVSNDDGVDAPGIKILADALRNAGHEVMVVAPDRDRSGASNSLTLDTPIRAKQIDMHTYSVAGTPTDCVHLALTGLLNYDPDIVVSGINNTGNLGDDVIYSGTVSAAMEGRFLGLPAVAVSLVTLYREGQQAPQYETAAHAAINIVAQLKTDPLPADTILNVNVPDVTWQQMRGFKVTRLGNRHRSAPCLTQTDPRGHTIYWIGPAGPEQDAGPGTDFDAVRNTYISITPIHVDLTRYQALENVTRWTDRLTAHMDWPT | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28391
Sequence Length: 262
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q9EQQ0 | MATARAKARGSEAGARCHRAPGPPPRPKARRTARRRRAETLTARRSRPSAGERRAGSQRAWSGAPRAAVFGDECARGALFKAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVAKGVEYYLVKWKGWPDSTNTWEPLRNLRCPQLLRQFSDDKKTYLAQERKCKAVNSKSLQPAIAEYIVQKAKQRIALQRWQDYLNRRKNHKGMIFVENTVDLEGPPLDFYYINEYRPAPGISINSEATFGCSCTDCFFDKCCPAEAGVVLAYNKKQQIKIQPGTPIYECNSRCRCGPECPNRIVQKGTQYSLC... | Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functio... |
Q28CQ7 | MAAARGAWCVPCLASIETLQELCRKEMLICTNIGITRKNLNNYEVEYLCDYRIEKGVEKFFVKWKGWPESCNTWEPTRNLKCPTLLKQFYSDLYNYFCALKPNKKGFLKNSIKSLDPSLSDYIVKKAKQRIALRRWEEELNRKKTHSGTLFVENTVDLEGPPMDFYYINDYKASPGVNTLGEAIVGCDCSDCFKGKCCPTEAGVLFAYNEHRQIKIPPGRPIYECNSRCKCGPDCPNRVVQKGPPYSLCIFRTDNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQQYDSRGITYLFDLDYEADEFTVDAARYGN... | Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functio... |
Q9FF80 | MERNGGHYTDKTRVLDIKPLRTLRPVFPSGNQAPPFVCAPPFGPFPPGFSSFYPFSSSQANQHTPDLNQAQYPPQHQQPQNPPPVYQQQPPQHASEPSLVTPLRSFRSPDVSNGNAELEGSTVKRRIPKKRPISRPENMNFESGINVADRENGNRELVLSVLMRFDALRRRFAQLEDAKEAVSGIIKRPDLKSGSTCMGRGVRTNTKKRPGIVPGVEIGDVFFFRFEMCLVGLHSPSMAGIDYLVVKGETEEEPIATSIVSSGYYDNDEGNPDVLIYTGQGGNADKDKQSSDQKLERGNLALEKSLRRDSAVRVIRGLKE... | Function: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.
Catalytic Activity: L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-homocysteine
S... |
Q93YF5 | MEQGLRSDGNNPPSIDKTRVLDVKPLRCLAPVFPSPNGMSSVSTPQPSPFVCVPPTGPFPPGVAPFYPFVAPNDSGRPGESSQQTPSGVPNQGGPFGFAQPISPVPLNSFRTPTTANGNSGRSRRAVDDDDYSNSQDQNDQFASGFSVHVNNVEDSGTGKKRGRPKKPRRAQQAEGLTPVEVDVEPLLTQLLTSFKLVDLDQVKKADGDKELAGRVLLVFDLFRRRMTQIDESRDGPGSGRRPDLKASNMLMTKGVRTNQTKRIGNAPGIEVGDIFFFRMELCLVGLHAPTMAGIDYMSVKLTMDEEPLAVSIVSSGGYD... | Function: Histone methyltransferase. Methylates in vitro both 'Lys-9' and 'Lys-27' of histone H3. Required for in vivo dimethylation of 'Lys-9'. H3 'Lys-9' methylation represents a specific tag for epigenetic control for plant development and transcriptional repression.
Catalytic Activity: N(6)-methyl-L-lysyl(27)-[hist... |
O22781 | MSTLLPFPDLNLMPDSQSSTAGTTAGDTVVTGKLEVKSEPIEEWQTPPSSTSDQSANTDLIAEFIRISELFRSAFKPLQVKGLDGVSVYGLDSGAIVAVPEKENRELIEPPPGFKDNRVSTVVVSPKFERPRELARIAILGHEQRKELRQVMKRTRMTYESLRIHLMAESMKNHVLGQGRRRRSDMAAAYIMRDRGLWLNYDKHIVGPVTGVEVGDIFFYRMELCVLGLHGQTQAGIDCLTAERSATGEPIATSIVVSGGYEDDEDTGDVLVYTGHGGQDHQHKQCDNQRLVGGNLGMERSMHYGIEVRVIRGIKYENSI... | Function: Histone methyltransferase family member that plays a central role in gene silencing . Together with MORC6 and SUVH9, regulates the silencing of some transposable elements (TEs) . According to PubMed:15775980, it is required for normal methylation of 'Lys-9' and 'Lys-27' of histone H3, 'Lys-20' of H4, and cyto... |
Q5QD03 | MATIQLTDQQRKVLHEVACTTAAPVLDTASKDKIKQLLDDYDMRKAAMGSKPGANMVLPGQVLGEAGPFLDYGHPPGVALGDKFKDRGQVMVAGVHGTTVRGIHAPNAGSEHFVRGAYSVLMSGVYVDDEDMGEAFWYTGEGGMDGKKQVKDQQMASGSNAALKNNCDTRTPVRVVRGFVQEAGGGEGGGGGEGGGGAKKGKGGKGGGKKEKGLVYEGLYLVLECKMEPSKDGPQVCKFLMHGLPGHSTVSAKVEYNIFGNAGSAYSLHARRLAGAGAPAGGKRARKAAQDEKARELARQWMLSEIRRQYPGPELQLEDV... | Function: Histone methyltransferase. Monomethylates specifically 'Lys-9' of histone H3. H3 'Lys-9Me1' (H3K9me1) functions as an epigenetic mark of repressed chromatin.
Catalytic Activity: L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine
Sequence ... |
Q8GZB6 | MAGKRKRANAPDQTERRSSVRVQKVRQKALDEKARLVQERVKLLSDRKSEICVDDTELHEKEEENVDGSPKRRSPPKLTAMQKGKQKLSVSLNGKDVNLEPHLKVTKCLRLFNKQYLLCVQAKLSRPDLKGVTEMIKAKAILYPRKIIGDLPGIDVGHRFFSRAEMCAVGFHNHWLNGIDYMSMEYEKEYSNYKLPLAVSIVMSGQYEDDLDNADTVTYTGQGGHNLTGNKRQIKDQLLERGNLALKHCCEYNVPVRVTRGHNCKSSYTKRVYTYDGLYKVEKFWAQKGVSGFTVYKYRLKRLEGQPELTTDQVNFVAGR... | Function: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with... |
Q8VZ17 | MEMGVMENLMVHTEISKVKSQSNGEVEKRGVSVLENGGVCKLDRMSGLKFKRRKVFAVRDFPPGCGSRAMEVKIACENGNVVEDVKVVESLVKEEESLGQRDASENVSDIRMAEPVEVQPLRICLPGGDVVRDLSVTAGDECSNSEQIVAGSGVSSSSGTENIVRDIVVYADESSLGMDNLDQTQPLEIEMSDVAVAKPRLVAGRKKAKKGIACHSSLKVVSREFGEGSRKKKSKKNLYWRDRESLDSPEQLRILGVGTSSGSSSGDSSRNKVKETLRLFHGVCRKILQEDEAKPEDQRRKGKGLRIDFEASTILKRNGK... | Function: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. Seems to act preferentially on dsMRNA.
Catalytic Activity: N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(... |
Q9C5P0 | MVSTPPTLLMLFDDGDAGPSTGLVHREKSDAVNEEAHATSVPPHAPPQTLWLLDNFNIEDSYDRDAGPSTGPVHRERSDAVNEEAHATSIPPHAPPQTLWLLDNFNIEDSYDRDAGPSTSPIDREASHEVNEDAHATSAPPHVMVSPLQNRRPFDQFNNQPYDASAGPSTGPGKRGRGRPKGSKNGSRKPKKPKAYDNNSTDASAGPSSGLGKRRCGRPKGLKNRSRKPKKPKADDPNSKMVISCPDFDSRITEAERESGNQEIVDSILMRFDAVRRRLCQLNYRKDKILTASTNCMNLGVRTNMTRRIGPIPGVQVGDI... | Function: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.
Catalytic Activity: N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocyst... |
Q9T0G7 | MGSSHIPLDPSLNPSPSLIPKLEPVTESTQNLAFQLPNTNPQALISSAVSDFNEATDFSSDYNTVAESARSAFAQRLQRHDDVAVLDSLTGAIVPVEENPEPEPNPYSTSDSSPSVATQRPRPQPRSSELVRITDVGPESERQFREHVRKTRMIYDSLRMFLMMEEAKRNGVGGRRARADGKAGKAGSMMRDCMLWMNRDKRIVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLTGSLSSNGEPIATSVIVSGGYEDDDDQGDVIMYTGQGGQDRLGRQAEHQRLEGGNLAMERSMYYGIEVRVIRGLKYENEVSS... | Function: Histone methyltransferase family member that plays a role in gene silencing . Together with MORC6 and SUVH2, regulates the silencing of some transposable elements (TEs) . According to PubMed:19043555, the protein does not bind S-adenosyl-L-methionine and lacks methyltransferase activity. Instead, it may funct... |
Q3EC60 | MGLVGLHSGTIDMEFIGVEDHGDEEGKQIAVSVISSGKNADKTEDPDSLIFTGFGGTDMYHGQPCNQKLERLNIPLEAAFRKKSIVRVVRCMKDEKRTNGNIYIYDGTYMITNRWEEEGQNGFIVFKFKLVREPDQKPAFGIWKSIQNWRNGLSIRPGLILEDLSNGAENLKVCLVNEVDKENGPALFRYVTSLIHEVINNIPSMVDRCACGRRSCGSKHVFREKLSVSSSLVISAKKSGNVARFMNHSCSPNVFWQSIAREQNGLWCLYIGFFAMKHIPPLTELRYDYGKSRGGGKKMCLCRTKKCCGSFG | Function: Histone methyltransferase family member that may lack methyltransferase activity. May methylate 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression (Potential).
Sequence Mass (Da): 35023
Sequence Length: 312
Domain: Although both SET and pre-SET do... |
Q9FNC7 | MAPNLHIKKAFMAMRAMGIEDARVKPVLKNLLALYEKNWELIAEDNYRVLADAIFDSHEDQAIQESEEKKADEVKEDEGCAAEVDRGKKKLHESIEDDEDVMAESDRPLKRLRRRGEGGSALASPSLGSPTLEGPSINDEENAPILLPYHPVPIENDHDAGELILTKVEPITNMPLSSIPDSVDRGDSSMLEIDKSNGHVEEKAGETVSTADGTTNDISPTTVARFSDHKLAATIEEPPALELASSASGEVKINLSFAPATGGSNPHLPSMEELRRAMEEKCLRSYKILDPNFSVLGFMNDICSCYLDLATNGRDSANQL... | Function: Probable inactive histone-lysine methyltransferase that acts as regulator of transctiptional gene silencing independently of histone H3K9 methylation. Contributes to transcriptional gene silencing at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-independent target loci. Forms a complex with... |
Q9SRV2 | MQRLRESPPPKTRCLGEASDIIPAADRFLRCANLILPWLNPRELAVVAQTCKTLSLISKSLTIHRSLDAARSLENISIPFHNSIDSQRYAYFIYTPFQIPASSPPPPRQWWGAAANECGSESRPCFDSVSESGRFGVSLVDESGCECERCEEGYCKCLAFAGMEEIANECGSGCGCGSDCSNRVTQKGVSVSLKIVRDEKKGWCLYADQLIKQGQFICEYAGELLTTDEARRRQNIYDKLRSTQSFASALLVVREHLPSGQACLRINIDATRIGNVARFINHSCDGGNLSTVLLRSSGALLPRLCFFAAKDIIAEEELSF... | Function: Histone methyltransferase.
Catalytic Activity: L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38773
Sequence Length: 354
Domain: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; s... |
Q8W595 | MISLSGLTSSVESDLDMQQAMLTNKDEKVLKALERTRQLDIPDEKTMPVLMKLLEEAGGNWSYIKLDNYTALVDAIYSVEDENKQSEGSSNGNRGKNLKVIDSPATLKKTYETRSASSGSSIQVVQKQPQLSNGDRKRKYKSRIADITKGSESVKIPLVDDVGSEAVPKFTYIPHNIVYQSAYLHVSLARISDEDCCANCKGNCLSADFPCTCARETSGEYAYTKEGLLKEKFLDTCLKMKKEPDSFPKVYCKDCPLERDHDKGTYGKCDGHLIRKFIKECWRKCGCDMQCGNRVVQRGIRCQLQVYFTQEGKGWGLRTL... | Function: Histone methyltransferase that converts monomethylated 'Lys-9' of histone H3 (H3K9me1) to dimethylated 'Lys-9' (H3K9me2) in the absence of bound ubiquitin, and to trimethylated 'Lys-9' (H3K9me3) in the presence of bound ubiquitin. Acts in a locus-specific manner and contributes to the transcriptional silencin... |
P32944 | MSSLDEDEEDFEMLDTENLQFMGKKMFGKQAGEDESDDFAIGGSTPTNKLKFYPYSNNKLTRSTGTLNLSLSNTALSEANSKFLGKIEEEEEEEEEGKDEESVDSRIKRWSPFHENESVTTPITKRSAEKTNSPISLKQWNQRWFPKNDARTENTSSSSSYSVAKPNQSAFTSSGLVSKMSMDTSLYPAKLRIPETPVKKSPLVEGRDHKHVHLSSSKNASSSLSVSPLNFVEDNNLQEDLLFSDSPSSKALPSIHVPTIDSSPLSEAKYHAHDRHNNQTNILSPTNSLVTNSSPQTLHSNKFKKIKRARNSVILKNREL... | Function: Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and inhibiting the mitosis-promoting cyclin B-bound CDC28 at 'Tyr-19'. SWE1-mediated inhibition of CDC28 acts in a cell size or morphogenesis checkpoint to delay mitosis in response to defects in gro... |
B9G2E6 | MVPDLIRNVVGIVGNVISFGLFLSPVPTFWRIIKNKDVRDFKADQYLATLLNCMLWVFYGLPIVHPNSILVVTINGIGLVIEAVYLTIFFLFSDKKNKKKMGVVLATEALFMAAVALGVLLDAHTHQRRSLIVGILCVIFGTIMYSSPLTIMSQVVKTKSVEYMPLLLSVVSFLNGLCWTSYALIRFDIFITIPNGLGVLFALMQLILYAIYYRTTPKKPSTTGPHPRSRIRTSSYQPSPPSPRAPASSPLSARTTTSMAAMSPSISRLSHKLA | Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30283
Sequence Length: 274
Subcellular Location: Cell membrane
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E7CLP2 | MKILIFIIASFMLIGVECKEGYPMGRDGCKISCVINNNFCKVECQAKWRQSDGYCYFWGLSCYCTNLPEDAQVWDSSTNKCGG | Function: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is lethal to insects (A.domestica). It is not toxic to mice and ... |
Q90ZH7 | MHRSSYCREETTLCQGVNSTWVPPADTVPEASLTPHSPPAPDSPAPSPKPGYGYSACEEKPGDPRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGQSWKNLTSAEKRPFVEEAERLRVQHLQDHPNYKYRPRRKKQAKKLKRMDPSHHLRNEGYTGGQPMVNLSHFRELHPLGGSGELESYGLPTPEMSPLDVLEPSEPAFFPPHMREDPDPGLFRTYQHEMDFSQEKTLREISLPYSTSPSHMGSFLRTPTPSAFYYKPHGGSSARTPLGQLSPPPEAPALDAMDHLNHAELWGDFDLNEFDQYLNMSRTQGP... | Function: Transcription factor. Binds to the consensus DNA sequence 5'-AACAAT-3'. Also binds 5'-CACAAT-3' and 5'-AATAAT-3' but with a lower affinity. Acts partially redundantly with sox7 during cardiogenesis, acting indirectly through nodal-signaling to induce mesodermal, organizer and endodermal tissues, which then in... |
A8MBI2 | MPILNESLLRTRIFIGRGFRRSRCPYCGHHYWTLNPSQDNCGDQPCTPYGFIGNPPGTYRPESIKDVRERFLSFFEKRGHTRVARYPVVARWRNDVYLVGASIYDFQPWVTEGVVPPPANPLTISQPSIRLTDVDKVGRSGRHLTGFEMMAHHAFNFPGKEIYWINETVEYAHEFFTRELGFRDDEVTYKENIWEGGGNAGESFEVLVRGLELATLVFMHYRVIGDEYREMPIRIVDTGYGLERIYWVLTGKPTIYEAVFEGFLNKARQLLGLPKPDEKVLASLAIHMGQLDPEVLALDKAYVEVAKRIGIDSSELINFI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
Q8RAH4 | MEKLGMNEIREKFLSFFESKGHLRLPSFSLVPKNDKSLLLINSGMAPLKPYFTGKETPPSRRVTTCQRCIRTPDIERVGKTARHATFFEMLGNFSFGDYFKKEAIPWAWEFVAEVLKLPVDRLWVTIYEEDDEAFEIWNKIVGLPPERIVRMGKEDNFWEIGTGPCGPCSEIYFDRGEEKGCGKPDCGIGCDDCDRYVEFWNLVFTQFNKDEQGNYHRLPNPNIDTGMGLERIAAIMQGVDTIFDVDVIRGIRDFISDLAEVEYGKDADKDVSIRVITDHIRGITFMISDGILPSNEGRGYVLRRLLRRAARHGKLLGLN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A0RPR0 | MDIRKEYLDFFKSKGHEIITSAPLVPDDATLLFTNAGMVPFKSIFTGDVPRPNPPIRTSCQTCIRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGEYFKKDAISYAWEFVTEVLKLPKDKLYVTVHEKDDEAYELWQKFIQKDRIYRFGDKDNFWAMGDTGPCGPCSEIFYDQGSEHFNSDEDYMGGDGDRFLEIWNLVFMQFERSKDGTMTPLPKPSIDTGMGLERVTAIKEDKFSNYDSSLFMPLINEVAKLCHKQYEYKTGASYRVISDHIRSVTFLLAQGVNFDKEGRGYVLRRILRRAVRHGYLLGIKEPFMYKL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A6WCF7 | MQTAEIRRRWLDFFERKEHTVVPSASLVSSDPSLMFTVAGMVPFIPYLTAQVPAPYKRATSVQKCLRTLDIDEVGKTTRHGTFFQMNGNFSFGDYFKREAVAFAWELLTTPEADGGLGFDPERLWTTVYLDDDEAFQLWREVGMPAERIQRRGKADNYWNTGQPGPGGPCSEIYFDRGPAYGAEGGPEADEDRYIEIWNLVFMQYQLSAVRTKVDFDVEGELPAKNIDTGMGLERVAFLKQGVDNMYEIDEVRPVLDKAAELSGRRYGAVHEDDVRMRVVADHVRSALMLIGDGVTPGNEGAGYVLRRLVRRAVRAMRLL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
B1L762 | MQGIEVEFLRSRGYVRKRCPKCGEYFWTLKDRETCGEAPCEPYTFIGRGRQNKSLEEVREDFLRFFERRGHTRINRYPVIARWREDLFLTSASIVDFQPFITAGIVPPPANPLTISQPCIRLKDIDKVGPTMGRHLSIFEMMAHHAFNTKDKFVYWIDRTVELFHEYATSVLGIPEEEITYKEGIWEGGGNAGPDLEPIAGGLEIATLVFMQYRIENGSYVPMDTRVVDTGYGLERITWFLRGDPTGFHAVYGALLHEFMDKLGVSEPDLSLLSEYSKVSSILRELEKGRSISSLRREAALLIGVSEEELEEKIAPLEAV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
Q1G947 | MKKLNSSEFRQMFLDFFAEHGHMVMQSASLIPKDDPTLLWINSGVATMKKYFDGSVVPKNRRITSSQKSIRTNDIENVGKTARHQTLFEMLGNFSVGDYFKEEAIPWAWEFLTSPDWLDLDKDKLYVTVYPKDTEAHRIWHEVVGLPESHIVQLEDNFWDIGEGPCGPDSEIFYDRGQENNDVPEDDPENYPGGENARYLEIWNIVFSEFNHLPDGSYVEQPHKNIDTGMGLERVLSILQDAPTNFETDLFLPIIHATEEMSAGKKYGANKADDISFKIIADHIRAISFAIGDGALPGNTGRGYVLRRLLRRAALNGRKL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
Q2S2B6 | MSHDPMNPHLQSSADPSRSSEEIRQDFLQFFQAKGHEVVPSASLVPDGDGTLLFTNAGMNQFKDVFLGTGQRPYSRAVDTQKCLRVSGKHNDLEEVGHDTYHHTFFEMLGNWSFGDYFKAEAIRWAWELLVERWGLAPDRLYATVHEGDDDFGLSADAEAYDLWLSETPLPEERVLYEPSKENFWMMGDTGPCGPCSELHVDLRPPEARQETPGRELVNVDHPQVMELWNLVFIQYNAQTDGSLEPLDDQHVDTGMGFERMVAVLQGKESTYDTDLFAPLLQAMADRSPREEIRGYDDLHIEDDDEHEQVRIALRVVADH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A4X5Z0 | MKTAEIRRRYLAHFEANGHAVVPSAPLPAISDPNLLFVAAGMMQFVPYFLGQQTAPYKRAVSVQKCLRTPDIDEVGKTSRHGTFFQMNGNFSFGDYFKDEAIPLAWELSTKPVDAGGLGLDPDRIWPTVYLDDDEAFQIWRSVGVPADRIVRRGKADNFWSMGIPGPCGPCSELFYDRGPEYGREGGPEVDEDRYLEFWNLVFMQFERGPGTGKEDYPILGDLPAKNIDTGMGLERMASILQGVDNLYEIDEVRPILAKAAELTGKRYGAHSGQVASESHPDDVRLRVVADHVRTALMLIGDGVIPSNEGRGYVLRRIMR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
O13914 | MTAESEVVNWPANEIRRTFLKYFEDHGHTIVPSSSVIPYDDPTLLFANAGMNQFKPIFLGTVDPSSDFAKLKRACDSQKCIRAGGKHNDLEDVGKDNYHHTMFEMLGNWSFGDYFKKEAIAMAWDLLTNVYGLKKDQLYVTYFGGHEESGLEPDLEARQLWLDIGIDESRVIPGSLKDNFWEMGDQGPCGPCSEIHYDRIGNRTVPELVNMDDPNVLEIWNIVFIQFNREKDGSLRPLPNRHVDTGMGFERLVSVIQNKTSNYDTDVFSPIFAKIQELTNARPYTGKMGDEDVDGIDTAYRVVADHVRTLTFAISDGGVP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Catalytic Activity: ATP + L... |
Q4VFY6 | MSVSAYFHHRFQQFRSLFKWIVLVVPMAVVVGSLCALFLWSLDKATAARFDHPWLIFLMPVAGFLMVLVYQHFGRGSEGGNNLIVDQIHEPGGGVPLRMAPFILVSTVLTHLVGGSAGREGTAVQLGGSVASAFARVSRLGHGEIRILLMAGIAAGFGAVFGTPIAGAVFALEVLTIGRMQYEALIPSLAAAIAADWTCHAWGIEHIHYHIGYLTGIPASTFHLDALLLAKVGLAGVIFGLAARCFSELSHAASAAFKRFCAYAPLRPVIASAVLIGLVYLLGTRQYLGLGVWSPNPDDATILGFFDPARVDYWSWLWKA... | Function: Essential for the establishment of a fully developed nitrogen-fixing root nodule symbiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48556
Sequence Length: 455
Subcellular Location: Cell inner membrane
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Q9LYL3 | MSEMEVEKPDLTLYNTMTQLKEVYKPMNPGKIGIYVCGITAYDYSHIGHARAAVSFDLLYRYLRHLGYQVTYVRNFTDVDDKAKNCGEKPLDLSNRFCEEYLLDMAALQCLLPTHQPRVSDHMEQIIKMIEKIIENGCGYAVGGDVFFSVDKSPSYGQLSGQRLDHTQAGKRVAVDSRKRNPADFALRKAAKSGEPSWESPWGHGRPGWHIEFDIHGGGADLKFPHHENEIAQTCAACEDSGVNYWLHNGHVTNNNVKMGKSLNNFFTIRQIAANYHPLALRHFLMSAQYRSPLNYSVSQLESSSDALYSLSPYREEMSG... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 55350
Sequence Length: 489
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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B3LFA4 | MEAEKMELKLYNTMTQQKEVLIPITPGKIGLYVCGITAYDFSHIGHARAAVSFDVLYRYLKHLDYDVTFVRNFTDVDDKIIDRANKNGEDPLDLSNRFCDEYLVDMGALQCLPPTHQPRVSEHMDNIIKMIEKIIEKDCGYVVEGDVFFSVDKSPNYGKLSGQLLEHTRAGERVAVDSRKRNPADFALWKAAKPDEPSWESPWGPGRPGWHIECSAMSVHYLSPKFDIHGGGADLKFPHHENEIAQTCAACEDSGVNYWLHNGHVTINNEKMAKSKHNFKTIREITASYHPLALRHFLMSAQYRSPLSFTASQLESSSEA... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 57842
Sequence Length: 511
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q54KR1 | MSENSSPKLESTSAAAASTKKPFPEWIKPKGKETELLINNSLTGGKVPFVFNESGKGRSLTWYACGPTVYDASHMGHARTYISFDIIRRIMKNYLGFNIQYVMNITDIDDKIIIRANENGISHSDLSKKWETAFFEDMKLLNVLPPDALTRVTEYVPQIVEYVEKIISNGFAYESNGSVYFDTVAFSKAHDYGKLEPNSVGNEKLAAEGEGSLTATSAVSEKRSGFDFALWKKSKPGEPVWNSPWGEGRPGWHIECSAMASDLLGGNIDIHSGGSDLKFPHHDNELAQSEAFYGNRQWINYFVHSGHLLIDGLKMSKSLK... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 74664
Sequence Length: 660
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q7KN90 | MSKRGQPAWQAPEAVDRPKLKLFNSLTRQKEDFVPLDGNNVTWYSCGPTVYDASHMGHARSYISFDILRRILSDYFGYNIHYVMNITDIDDKIIRRARQNHLFDEYAAEAQKLPLDELLGQQKEVLQRFQDTCAKNTDPDKKIMLDKTLQRMNDAVEALTKAVGKGDEREISEKRLLYLNEAKDPISDWLDSLKGAQINDNAVFEALPRYWEDQFHNDMKSLNILPPDVLTRVSEYVPQIVTFIQKIIDNGLAYAANNSVYFDVNGFDKREKHHYAKLVPEAYGDTKSLQEGEGDLSIAEDRLSEKRSANDFALWKASKA... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 84258
Sequence Length: 741
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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P49589 | MADSSGQQGKGRRVQPQWSPPAGTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITDIDDKIIKRARQNHLFEQYREKRPEAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQHAVQLATEPLEKAVQSRLTGEEVNSCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys).
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 85473
Sequence Length: 748
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q9ER72 | MAGSSAEQAADYRSILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADSRLFHVARWFRHIEALLGGPQGRDEPCRLQASKGRRVQPQWSPPAGTEPCRLRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFQYDVFYCMNITDIDDKIIRRARQNYLFEQYREQKPPATQLLKDVRDAMKPFSVKLSETTDPDKRQMLERIQNSVKLATEPLEQAVRSSLSGEEVDSKVQVLLEEAKDLLSDWLDSTGGSEVTDNSIFSKLPKFWEEEFHKDMEALNVLPPDV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys).
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 94860
Sequence Length: 831
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q5M7N8 | MTDSWERGKGRRTQPPWSAPNTQAQPGLRLYNSLTRSKELFVPQDGNKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFKYDVFYCMNITDIDDKIIKRARQRHLFQQYRERNPRPSDLLQDVSAALTPFLQRISEANDPDKRQMLERIHGSVSAALLPLQDAVSSNARAEELERLSQELMEAAVDLLSDWLDEKHGAQITDNSIFSQLPKHWESEYHRDMEALNVLPPDVLTRVSEYVPEIVAFVQRIVDNGYGYVSNGSVYFSTAKFHASEKHYYAKLVPEAVGDQKALQEGEGDLSISADRLSEKQSPNDFA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys).
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 85477
Sequence Length: 747
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q9PPB8 | MRLLDSVTKEKIKLDKKDISIYLCGPTVYDDAHLGHARSSVCFDLLRRVLLAQGNRVKFARNYTDIDDKILKKMAQSGQTLEEITEFYIKSYEEDMRVLNVLDPDFKPRATHYITAMLDLIKKLAKDGFVYTLEDGIYFDTSKDEKYLSLSNRNLEENISRLSNEVQKRNESDFVLWKFDENFYESEFGKGRPGWHTECVAMIDSIFENTLDIHAGGIDLLFPHHENEAAQCRCGCKRKLANIWLHNGFVKIDGEKMSKSLNNSFFIKDALKEFMGEALRFYLLSSHYRSHFNYSLSDLENAKKRLDKFYRLKKRLDLGE... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 53513
Sequence Length: 462
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q9AAY2 | MTLKIHDTLTREKRDFVPADPQRVTMYVCGPTVYNYAHIGNFRPVVVFDVLFRVLRHLYGEDAVVYARNVTDVDDKINQKAADEGVPISVITDRYLAAYHQDADALGALRPTLEPKATEHIGAILEMIGQLVENGSAYAAEGHVLFDTQSFADYGQLSGRPLDEMIAGARVEVAPYKRHPADFVLWKPSKENEPEWESPWGAGRPGWHIECSAMIDKALGQTIDIHAGGIDLTFPHHENEVAQSRCAHKTSVLANYWMHNGFLDMSGEKMSKSLGNVIIPHELLETTPGEVIRWALLSAHYRQPLDWTPELLEQSKKSLD... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 50881
Sequence Length: 463
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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B9KRV8 | MTEIRLTNTKSRRKEAFEPIDRKNVRLYVCGPTVYDRAHLGNGRPVVVFDVLFRLLRHVYGEGHVTYVRNFTDVDDKINAAALARKDAGDPRSLEALIRERTDETIRWYHEDMDALGALRPTQEPRATEWIGAMIAMIEDLIAKGHAYEREGHVLFRVRSYRDYGALSGRSVDDMIAGARVEVAPFKEDPMDFVLWKPSDDELPGWDSPWGRGRPGWHIECSAMADGLLMKDLPENERSFDIHAGGIDLQFPHHENEIAQSRCAHPEGEFAKVWMHNEMLLVDGKKMSKSLGNFFTVRELIEEYRKQFAVNNIGPAIRLR... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 59052
Sequence Length: 519
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q11JR3 | MSDGFKALKLYNTLTRRDEEFVPLDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRQLYGDDHVTYVRNITDVDDKINARALRDFGEDITAGRLTLNEAIRRVTERTAAQFHADVAALGCLAPTHEPRATEFVLPRTDGKADMASLIQTLIDRGHAYAAKGEILFDTASMPDYGQLSKRRLEDQQAGARVAVDPHKRNPSDFVLWKESSAEEPGWEGRFTFEGKPLVIRGRPGWHIECSAMSAAYLGEVFDIHGGGLDLIFPHHENEIAQSRCAHGTPVMANYWLHNGFVQVEGKKMAKSEGNFVTIHDLLATEN... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 55454
Sequence Length: 497
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q1MQR5 | MHLYNTMEKKKEPLIPIISGKLGIYVCGITAYDFSHIGHARSAIVFDILVRLLRYQGYDVTFIRNFTDIDDKIINRANKEGRSSKEVAEEFINAFHEDMDRLGVLNADIEPKATDYIPEMIECCQKLLEADKAYITASGDVYFRVRSFPDYGKLSGRTPDELRIGVRIVPSEEKEDPLDFVLWKAAKPGEPSWESPWGRGRPGWHIECSAMSEKCWPLPLDIHGGGIDLIFPHHENEIAQTESIVNKPLAKIWMHNGLVQVNSEKMSKSLGNFKIVRDILEAYLPETLRFFLLKKHYRSPIDFSFEGMNETERSQKRVYE... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 55492
Sequence Length: 485
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q8F525 | MIEIQFYNSLSGRKEKFSPSDPNRVTVYSCGPTVYNFAHIGNLRAFLFVDVLRRSLKLLGYGVDMTMNITDIDDKIIRDSIASKKSIIEFTAPWTKAFFEDLKTVSAEILEHYPKATDSIPEMVDIIQKLQKKGLVYKKDESLYFSIQKFQNYGKLSKIDTSGMKTGTRYDTDEYEKEDVRDFVLWKSPKLEGETSWDTLVGTGRPGWHLECSAMIRKVYGSGVDIHTGGVDLLFPHHENEIAQSEGAFPEESFVKTWLHSEHLLVDGQKMSKSKGNFYTLRDLIQQGLDPKAIRFLLISTHYRSKLNFSTDRIAEASAN... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 54262
Sequence Length: 471
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q1WSS5 | MLQLYNTLTNQKEKFEPLNPGKVTMYVCGPTVYNYIHIGNARSAVAFDTIRRYLEYRGFEVNYVSNFTDVDDKIIKASQEMNLSVKEITEKFINAFYEDTSALNVKKATLNPRVMDNMDDIIKFIEVLVQKGYAYESAGDVYYKTRKFKDYGKLSGQLIDDLEQGASSRVDDIDQDKKQDPLDFALWKKVKQGEISWNSPWGQGRPGWHIECSVMSTKYLGDTIDIHAGGQDLEFPHHENEIAQSEAKTGKKFARYWLHNGFVTIGEEDQKMSKSLGNFVTVHDLLKKVNPQVIRFFMSTTQYRRPIRYSSANLNEAKVN... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 54475
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q1AU11 | MSVKVRDSLSGGLVEVGGDGRVGIYVCGPTVYNHIHIGNVRGHLFWDVAVRFLRSRGYRVKFVWNITDIDDKIINRANEEGVSWKEIVRRYTDSFHERLRLLGIGMPDVEPRATEHIPEMISLIEELIRRGHAYPAPNGDVYYAVETFPRYGALSKQRPEEMKITEKGQTGHKRNPLDFTLWKASKPGEPSWESPWGPGRPGWHIECSAMVEKHLPGGADIHGGGSDIRFPHHENELAQSCGAHPDRPFVRAWAHHGMVRMAAQKMAKSVGNVVDAREATLKHGRDAIRMWLLQSHYSQPIDYSDEILEEKRRSCERLLR... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 53062
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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A4F6W7 | MSLHLHDTATRTMREFHPRLAGVASIYVCGATVQGVPHIGHVRGGLNYDVLRRWLVHNGYDVRLVRNVTDIDDKILTKAADAGRPWWEWATAHERAFESAFDRLGCLPPSALPRATGHITQMIELMQRLIDKGHAYAAGGDVYFSVASYAEHYGRLSGQRLDEVQQGESTASGKRDPRDFTLWKAAKPGEPSWPTPWGDGRPGWHLECSAMSTYYLGSEFDIHGGGLDLVFPHHENELAQSTAAGDGFARYWMHNAWVTMSGEKMSKSLGNTVAIPAILQRAAAPEIRYYLVAPHYRSTIEYSEPALAEAISAYRRIDSF... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 51033
Sequence Length: 464
Subcellular Location: Cytoplasm
EC: 6.1.1.16
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Q97WE6 | MDFRIRVYNSLGRKLEEFGTVEPNLVKMYVCGPTVYDYVHIGHGRTFVVFDAISRYLRLRGYTVIRVQNITDIDDKIIKKSQEIGKDWNEIVDYFTKDYLDMLSQLKVKIDIHPRVTQHIREIIDFVQRLIDKGHAYVAPSGSVYFDVDTYPNYGELSNTKKEEWNQGEEFVKEKKHSYDFALWKAWKPGEPYWESPWGKGRPGWHIECSTMSTRYLGERFDIHGGGADLIFPHHENERAQTEALIGEKWVTYWVHSAFVTIRKEKMSKSLGNIIPLNEAIKKWGPSVLRYWYLTSHYRSPIDFSEEALEQAKSALQRIK... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
Sequence Mass (Da): 55326
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 6.1.1.16
|
F4JJT9 | MSLLLRTLPLRPTRFLSATAISISNATNFFVVPKRTNPLPGTRRTFSSSPVAAASGDVVVKPVPSPPSVLRWVSRTELCGELSVNDVGKRVHLCGWVALHRVHGGLTFLNLRDHTGIVQVRTLPDEFPEAHGLINDMRLEYVVLVEGTVRSRPNESVNKKMKTGFVEVVAEHVEILNPVRTKLPFLVTTADENKDLIKEEIRLRFRCLDLRRQQMKNNIVLRHNVVKLIRRYLEDRHGFIEIETPILSRSTPEGARDYLVPSRIQSGTFYALPQSPQLFKQMLMVSGFDKYYQIARCFRDEDLRADRQPEFTQLDMEMAF... | Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence ... |
Q55C99 | MNRVILKDSKIFLNVLNKPIIKNKNCLSLLNITTSSTTSIIKNQQINQFNKRNFTNTINNNKNENINNKILNIIERSHSCGEITSKDIGKEVIIYGWINSLRNLGDNVFLVIRDGHGKVQCYVDLKQQCILKSSVPNIDINERNSIEENIKLFKLESIVSIKGKVIARPERMVNKNMSTGEIEISVDQLQLLNNCVDLPFTVEHDSTAVSEELRLKYRYVDLRRDKVQSNIRLRSKVAMAARNYLINQQFIEVETPTLFRPTPEGAREYLVPTRHQGQFYSLPQSPQQYKQLLMVGGIDRYFQLARCYRDEDLRSDRQPE... | Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence Mass (Da): 79277
Sequence Length: 692
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.12
|
Q6PI48 | MYFPSWLSQLYRGLSRPIRRTTQPIWGSLYRSLLQSSQRRIPEFSSFVVRTNTCGELRSSHLGQEVTLCGWIQYRRQNTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKDPVVVPFPTMT... | Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence Mass (Da): 73563
Sequence Length: 645
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.12
|
O94242 | MVLSRLPACLLPLVGTKVSIQGWLVATSRQVSKSISFHQLRDTHGTILQLLSTDKIILQQKREPLVSSTDFSQQKSTSVMRTLSSIPPESVVQVTGKLQRRPEHDRRPGNEFELHVEDVKLLNVAKNLQLFPGDEKPGMRIQLANRHIQLRAPKYNSYLRQRSRLAYQVHSFFNDREFCEVETPLLFKSTPEGAREFVVPSRLNPGKFYALPQSPQQYKQILMASGIGNYYQIARCFRDEDLRFDRQPEFTQIDLEMSFVDKPHEIMEVVEDLLVRLVSFAKGITLAKPFQHITYQHAIDKYGSDKPDIRFELPLKNITS... | Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence Mass (Da): 69407
Sequence Length: 611
Subcellular Location: Mitochondrion
EC: 6.1.1.12
|
P15179 | MLARSRVCLQTITRRLADFPEANAIKKKFLFRKDTSTIKQLKGLSSGQKIVLNGWIEQKPKRVGKNLIFGLLRDSNGDIIQLVDNKSLLKGFTLEDVVQAVGILSLKRKLSNEDADEYEVQLEDITVLNASNKKPAQMQDFKLSAIYPPEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGAREFLVPTRTKRSDGKPSFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSGVWSKFSKKRGLLTLDSKGTLVPAKKENGTVSIFRM... | Function: Catalyzes the attachment of aspartate to tRNA(Asp) in the mitochondrion.
Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence Mass (Da): 75461
Sequence Length: 658
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.12
|
Q2LPW5 | MPNRGAHFSISRRKDFLMDFSERVFCGHLTPDHTGRRVLLAGWVDAFRDHGGLLFIHLRDRNGIIQIVFSPEAASADVYRQAASLRAEYCVAVQGEVRKRLPGTENPHIETGDIEVFVSELTVLSESEALPFAISDKAMVAGASSAGADHVNEDLRMQYRYLDIRRPAMQKNLILRHRISQCVREFLDSRGFVEVETPVLTMSTPEGARDYLVPSRIHPRSFYALPQSPQLFKQLLMIGGMERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFLYELIEELTVRMFAIGGIALSRPFPRMTYAEAMDTTGSDRPD... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q6FEH6 | MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKVRSEFVLKITGRVRRRYEGTENSNMVSGQIEVLGKEIEVLAQSETPPFPLNDDNINISEEHRLKYRFLDIRRPEMLDRLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFDELLGIKFDKFQRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQDVEFKVFAGPAKDPKG... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q5NIQ4 | MRTHYSSDINEKLQGQKVTVCGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPDNDNFKVADSLRSEFVIKAEGVVNLRPEGQENKNISSGKVEIIGDSIEVINKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQHKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMERMIAGLFKETIGVEFATPFQVMTFADAIDKYGSDKPDLRIPLEFVNIKEDMQNEEFKVFSGPANDPQSRV... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q74D56 | MTDMLGDWKRSHLCGTLTKADVGKQVTLMGWVMRRRDHGGLIFIDLRDREGLAQIVFDPAKAPEAHREAEAVRNEYVVAIKGEVVPRPEGTVNPNMKTGEVEILVTQCKLLNRSKALPFTLDDYVDVAENLRLKHRYLDLRRTPLQQNLILRSRVSQVTRQYLTENGFLEIETPFLTKSTPEGARDFLVPSRINQGNFYALPQSPQIFKQILMISGFDRYFQVVRCFRDEDLRADRQPEFTQIDCELSFVDRDDVIAVMEGLIARIFKEAKEIDVQLPIPRMTYAEAIRRYGVDNPDVRFGLELVELTDIVKGSGFKVFA... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q7NJA4 | MRSDYCGTLRSEHIGKTVSLYGWIDGWRDHGGVIFLDLRDYTGIVQIVADPQRTPESYHLASSLRNEYVVRVEGRVSARPEHSLNPRLSTGTVEVYADTLAVLNRAETPPFAISKDEEVDEKLRLKFRYLDLRRGRMQKLLRLRHRVMQIMRRHLDERGFTEIETPVLVKSTPEGARDYLVPSRVNPGDWFALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSMEEIIALNEGLVAAILQETMGLELSLPLPRLTYAEAMVRYGSDKPDTRFGLELVEVSEVFRESSFQVLSGAVAAGGK... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q2SCK8 | MRSHYCGEVNESLVDQEVTLCGWVHRRRDHGGVIFLDLRDRDGIAQVVYDPDTNEVFQLAEQIRDEFVVKVTGRVRLRPEGKANTDMSTGMVEVLGKQLEILSTAKTPPFQLDEFVQVGEDVRLRYRYMDLRRPEMLNKLRFRSKVTSYIRNFLDGNGFMDVETPILTRATPEGARDYLVPSRTHEGSFFALPQSPQLFKQLLMMSGVDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFLNENEIMSITERLVRDMFRDLLEVELPEFPRMPFSEAMNRYGSDKPDLRIPLELVDVGDLLTNVSFNVFSGPANDPKSRV... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q8DSG3 | MKELFIGNYGLEQVGQKVTAKGWVANIRNHGKLAFIELRDREGLLQVFVDSAVADFDKLHDLHKESILAVTGEIVARDERFVNPHIKSGQVELRAETIEIIASSKLLPFELDNHAHAGEDIRQKYRYLDLRREKMTANLKLRHQVTKAIRDYLNQADFIDVETPYLTKSTPEGARDFLVPSRVFKNQFYALPQSPQMLKQLLMGAGLERYYQIVRCFRDEDLRGDRQPEFTQVDLEMSFVSEEDVRNLVEGMLKAVVKASKGIELTEAFPIISYAQAMRRFGSDKPDTRFAMELKDLTELSRGNTSLFLQKGLKKENGVV... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q31NM6 | MRTHYCGELRAEQVGTSVTLYGWVDRRRDHGGVIFVDLRDRTGTVQIVSDPERTPESYHQAEGLRNEYVVKITGRVSGRPAESLNPKLPTGEVEIYADRIEILNAVRRQLPFQVSSADEETVREDLRLRYRYLDLRRDRMNRNLQLRHQVVKAIRRFLEDEEQFIEIETPVLTKSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSQEEIIDLNERLIAHIFKTVKGIELPRPFPRLTYAEAMDRYGSDRPDTRFGLELVDVSDVVADMGFKVFSGAVK... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
Q0AYS1 | MKRTHNATELDIHLVGREVMLNGWVDTRRDHGGLIFVDLRDRSGIIQLVFSPEVKEEAFHLAEQIRSEYVIAVRGKLSLRPEATENPNLKTGKVEVYVEDIEVLSPAKTPPFYIENDIDVDENLRLKYRYLDLRRPEMRDNLLLRHRVVKCMRDFLDSRGFIEIETPILTKSTPEGARDYLVPSRVHPGEFYALPQSPQIFKQILMVAGMEKYFQIARCFRDEDLRADRQPEFTQLDMEMSFVDEEDIIVLVEEMMAEIFFKAAGKVIRTPFPRLAYDDAMINYGSDKPDLRFGLEIVELSEMLQNTQFKVFASALQSGG... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
P73851 | MRTHYCGDLRTTHLGETVTLYGWVDRRRDHGGVIFLDLRDRQGIVQIASSPDQTPASYPVAEGLRNEYVVQVTGVVSKRPPESLNEKIPTGEIEIYADSIILLNGVNQQLPFVVSSHEAEQVREDVRLKYRYLDLRRARLSQNLQLRHQVVKAMRRFLEDQENFLEIETPILTRSTPEGARDYLVPSRVNPGEWYALPQSPQLFKQLLMVAGMDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMGQEEILDLNEALICHIFKVVKNIDLPRPFPRLTYQESMAKYGNDRPDTRFGLELVDVSDLLGNTGFKVFSAAVS... | Function: Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Catalytic Activity: ATP + L... |
A6GWB6 | MYRSHNCGELNATHINKEVTLAGWVQKSRDKGFMNWVDLRDRYGITQLMFDESRSDKTVFELAKTLGREFVIQVKGTVIEREAKNKNISTGEIEILVTQMTILNSSLTPPFTIEDETDGGEDIRMKYRYLDIRRNPVKNSLLFRHKVAMEVRKYLSDLDFCEVETPYLIKSTPEGARDFVVPSRMNEGQFYALPQSPQTFKQLLMVGGMDKYFQIVKCFRDEDLRADRQPEFTQIDCEMAFVEQEDILNIFEGLTRHLLKELKGIEVEKFPRMTYNHAMKTYGNDKPDIRFGMEFGELNEYAKHKDFPVFNAAELVVAIA... | Function: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence Mass (Da): 66453
Seque... |
Q8RGJ4 | MVYRTHNLGELRLKNIGEVVTLSGWVDTKRNVSTNLTFIDLRDREGKTQIVFNNELLSEKVLEEVQKLKSESVIRVIGEVKERSNKNPNIPTGEIEVFAKEIEILNACDTLPFQISGVDDNLSENMRLTYRYLDIRRNKMLNNLKMRHRMIMSIRNYMDNAGFLDVDTPVLTKSTPEGARDFLVPSRTNPGTFYALPQSPQLFKQLLMIGGVEKYFQIAKCFRDEDLRADRQPEFTQLDIEMSFVEKEDVMNEIEGLAKYVFKNVTGEEANYIFQRMPYAEAMDRFGSDKPDLRFGVELKDLSDIINNSSFNAFSSTVQN... | Function: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence Mass (Da): 67608
Seque... |
Q9PCC5 | MRTHFCGLIDETLIGHTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVDSRAIDQNNSELFKVASGLSYEDVLQVEGVVCARHAVNDKIKTGKVEVIATKIKILNKAAPLPFHAHENPGEDIRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDMHGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVSERDVQDFVEEMIRRVFKEVAGIELDTTFPRMTWTEAMRRFGSDKPDLRINLELIDVAALVADSTFTPFTDAVAHPNG... | Function: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Catalytic Activity: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Sequence Mass (Da): 65809
Seque... |
A5FZX8 | MTIRVRFAPSPTGMLHIGGARTALFNYLFARHHGGQFLLRVEDTDRERSTPEATKVILDALDWLDLKPDEPPVYQSTRYARHREVAEQMLAAGQAYRCYCSREELAEMRAEAERSKKPFRYDGRWRDRDPAEAPAGVDPVIRLRAPREGETVIHDLVQGEVRVKNAELDDMILLRSDGTPTYLHAVVVDDHDMGITHVIRGDDHLTNTFRQAQIYDAMGWARPNFAHIPLIHGADGAKLSKRHGAVSVLQFRDEGYLPEALCNYLLRLGWGHGDAEILPREEQVALFDLDGVGRAASRMDYAKLLHVNAVFLRAAEDERL... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 51934
Sequence ... |
A8EQW9 | MAITRFAPSPTGYLHIGGLRTSLYSYLWARKTGGEFRLRIEDTDLARNSEEAMKAIIDAFDWVGLNYDGEVFYQSKRTDIYKQYIDKLLESGNAYKCYMSKEELDALRAAQEAAKQTPRYDGTWRPEPGKELPPVPAGVEPVIRIKAPTTGTIEFDDGVKGHMKFDANQVDDYVIARSNGMPTYNFVVAIDDALMGMTDVIRGDDHLSNTPKQIVVYNALGFKVPKFYHVPMINNPEGKKLSKRDGAMDVMDYKRLGYLPEALLNFLVRLGWSNGDQEIFSMKEMLELFDPSNINKSASSYNGEKLLWLNSEYIKAVSNE... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 53551
Sequence ... |
Q2GLP6 | MITRFAPSPTGYMHVGNARTALICWLYARSKSGKFLLRIDDTDASRSEHKYIEGIKQDLDWLALDWDSCFQQSTRLERYQEVFDLLLDQGVIYPCYETQEELDMKRSMMLKMGLPPIYDRSALKMTEQEMQACSGRLPYFRLKIDQSREITWEDEVRGRVSFQAKNISDPIIKRTDGTYTYMFPSVVDDIDFAITHIIRGEDHVSNTATQICIFDILKAKVPVFVHLPLVHFRDAKISKRVGSDDIEIRHLRDIGMEPMAIKSYLARMGTSLPVEPQENHDVLVESFDIRTFNQAPIKFSLDDISRLNSRIVQCLSFDKV... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 51850
Sequence ... |
Q5NL22 | MSAGPAKNPSVVTRFAPSPTGFLHIGGARTALFNWLFARHNGGQFQLRIEDTDRVRSTKEAIDAIIDGMRWLGLDWDGDITYQFERAPRHTEVAEELLKAGKAYKCFATAEELEAMRAEQRAKKQPQRYDGRWRDRDPSEAPAGAPYVVRLKAEQEGETTLHDLVQGDVTVKNAELDDMILLRSDGTPTYMLAVVVDDHDMGVNHVIRGDDHLNNTFRQLGIIRAMNWDAPQYAHIPLIHGADGAKLSKRHGALGVEAYRDDFGYLPEAICNYLLRLGWGHGDDEIITREQAIEWFDLTSVGRSPSRFDFKKLENINGHY... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 53893
Sequence ... |
O82462 | MDGMKLSFPPESPPLSVIVALSLSASPVTIDSSAAATTVPSFVFSDGRKLNGATVLLRYVGRSAKKLPDFYGNNAFDSSQIDEWVDYASVFSSGSEFENACGRVDKYLESSTFLVGHSLSIADVAIWSALAGTGQRWESLRKSKKYQSLVRWFNSILDEYSEVLNKVLATYVKKGSGKPVAAPKSKDSQQAVKGDGQDKGKPEVDLPEAEIGKVKLRFAPEPSGYLHIGHAKAALLNKYFAERYQGEVIVRFDDTNPAKESNEFVDNLVKDIGTLGIKYEKVTYTSDYFPELMDMAEKLMREGKAYVDDTPREQMQKERM... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 81065
Sequence ... |
Q54KB8 | MSKAKDTGILRFDDTPLAATFPLVAIITSKVVGGVKIVGRKGLDSTEFSIVGTQDSLKGSYVIAKYLARTTPSLSLYGENALSASKIDEFIDKFAHLKSEKFNEFLKEMNEYLTLRAFLIGFNLTLADIVLFARIKMVKEIQEEINKLGKTIPHLNRWYGYLSQLESFVEADNAFNGKKETKASGKAGAEGTAATTEKVAPQKGAMGWVGNFEALNLPGLVEGKVVTRFPPEPSGYMHIGHCKAAIINNYYAEKYNGKIIIRFDDTNPSKEKEEYVENIIKDINNLGIKYEKITHTSDYFDLIHDYAIQMIKEGIAYCDD... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 85614
Sequence ... |
Q8SSE4 | MDGKSEFKEELINYILLKKYGKGAQDPPVYSNALKKAPQEMFPPGLVDALDSYSINLSRSEGVEFLVLLNSLVNDIRSEEVKDIIFGMINTNQMLTKLMKDKKEVERFPDTCKMYSEQFKANKPLLKEFNAGSRKEQGNLEIGEPSENVVTRFPPEPNGRLHIGHARAALLNWYFASKGNGRLLVRFDDTNPEKEEERFERGILSDLSLLGINEYTLSHTSDYFDKIIDLGVFLIGEGKAYADNTPQEVMRDERGRGVESRCRSMDVEESKRIFKEMARGNASGYCLRAKIDMSSSNKAMRDPVIFRVNESPHHRTGDKY... | Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 73964
Sequence Length: 642
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
A9CSZ1 | MLENISKSEFVNFLLEKKHNIEPKTLPILEQHIREQKLDDFFLDFSIDFTDEELNNFLSKLDYWLKNTKLNSSKADVIFGLLYSCNKFIKLIKNPTFSFVEIKQFYNDILNTNKNYIIEYNKKDKGKINIAVEGNVVTRFPPEPSGFLHIGHIKAALLNDLMAKNGKLLIRFDDTNPIKEEKMYENVIIEDLHTLGIKNYTIVRSSDHFDSLYNYAIQLIQLGLAYCDNTDQLQMREERTKGIPSKNRNTDIETNLSIFSKMSSGNCLDYCLRAKIDYTNLNKALRDPVIYRHIEKEHNITKNKYKIYPTYDFACPIIDS... | Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 73962
Sequence Length: 631
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
C4VBI7 | MAVENAINFREICSLLDISESYKCTINAFLDNVEKCTDKHYNDALNLLDTFFSNEVKSNSLVNDLIFCIINSNFDFLKVFKSNKLRLENLQIVYESAFNENKPFLKEFSAKDKINKEVKKNLYSTPAVTRFAPEPSGCLHIGHLKALLVNYNLAEKSNGTLLLRFDDTNPVKNYEKYEKEILRDLDTLGITGLKISHSSDYFELLVDEAVSLINKNLAYVDNTDQETMRIERFEGIESKMRNINNSESLKIFKELLQGRAPGYCLRAKIDMSNPNKSMRDPVIYRASDKMHGRCKLYKAFPTYDFVCPIVDSIEGVTVVC... | Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 70755
Sequence Length: 614
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
P46655 | MPSTLTINGKAPIVAYAELIAARIVNALAPNSIAIKLVDDKKAPAAKLDDATEDVFNKITSKFAAIFDNGDKEQVAKWVNLAQKELVIKNFAKLSQSLETLDSQLNLRTFILGGLKYSAADVACWGALRSNGMCGSIIKNKVDVNVSRWYTLLEMDPIFGEAHDFLSKSLLELKKSANVGKKKETHKANFEIDLPDAKMGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKEEFQDSILEDLDLLGIKGDRITYSSDYFQEMYDYCVQMIKDGKAYCDDTPTEKMREERMDGVASARRDRSV... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl-t... |
Q9FEA2 | MASLVYGTPWLRVRSLPELAPAFLRRRQSSLFYCSRRSFAVVACSTPVNNGGSVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLERSTRESEAAVLQDLSWLGLDWDEGPGVSGDFGPYRQSERNALYKQYAEKLLESGHVYRCFCSSEELVKMKENAKLKQLPPVYTGKWATASDAEIEQELEKGTPFTYRFRVPKEGSLKINDLIRGEVCWNLDTLGDFVVMRSNGQPVYNFCVTVDDATMAISHVIRAEEHLPNTLRQALIYKALKFPMPQFAHVSLILAPDRSKLSKRHGATSVGQYREMGYL... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 63466
Sequence ... |
Q5ZJ66 | MAGMLREVCGAAASGLRVRFGPSPTGFLHLGGLRTALYNYVFAKQQRGTFVLRVEDTDQGRVVAGAAESIEDMLHWAGIPPDESPRRGGPFGPYQQSLRLDLYRAASEALLDRGAAYRCFCTPQRLELLRKEALRNQQTPRYDNRCRHLTPKEVAEKLAQGLDWVVRFRLERGVEPFQDLVYGWNKHEVAEVEGDPVILKADGFPTYHLANVVDDHHMGISHVLRGTEWLTSTSKHLLLYKAFGWDPPQFGHLPLLLNKDGSKLSKRQGDIFLERFAQEGYLPEALLDMITNCGSGFAEKQMGRTLEELISQFEIGRITT... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 56954
Sequence ... |
Q0P499 | MKILRGVSRQMCTSRPEVRVRFAPSPTGFLHLGGLRTALYNFLFSRQRRGVFILRLEDTDQKRLVPGAAEHIEDMLEWAGIPPDESSRRGGDYGPYVQSERLHLYTEAASSLLNTGHAYYCFCSNQRLELLKKEAQRSGHAPRYDNRCRRLQPQQVEQKLAAGVPAVVRFKLHTGTEEFQDLVFGWTGHAVGAVEGDPVILKADGYPTYHLASVVDDHHMRISHVLRGCEWLISSAKHLQLYRALRWTPPTYAHLPLLLNRDGSKLSKRQGDIFLQSFRDRGVLPETLLDLVTHAGSGFSDNRMGRRLDELIRDFNISKI... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 57023
Sequence ... |
Q5JPH6 | MAALLRRLLQRERPSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVPAFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAE... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 58689
Sequence ... |
Q9HDX9 | MLSYTSCAKLICSRYIVSKISFYSLKRCNSTAVVRTRFAPSPTGFLHLGSLRTALFNYLWAKKSNGKFILRLEDTDQKRKVTGSDLEIYKVLKQFNLQWDEGPIVGGPYGPYEQSSRLQIYQKYAQHLIETGRAYVSYSVPIATTKIDSSTKYHEISIDDLTDAQRKLYKSKKFPYVVRFRMKEPSPFTDLVYGKIAIKSDSREIEESNNFVILKSDGFPTYHFANVVDDHLMHITHVIRGEEWVPSTIKHIQLYEAFGWKPPKFAHLPLLVNPDGSKLSKRQNDAHVSSLLQEGFLPEAILNFIALMGWSSRQKSDFLP... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 60645
Sequence ... |
Q11PQ4 | MSDTNKQVRVRFAPSPTGPLHIGGVRTALYNYLFARKMGGKMLLRIEDTDQNRFVPGAEAYIQEALAWVGIVIDEGAGVGGPHAPYKQSERKPMYREYAEKLIAEGNAYYAFDTSEELEAMKERLKAAKVASPSYNMVTRMQMNNSLTLPEDEVKRRLDAGDEYVIRLKVPRKEEIRLNDMIRGWVVVHSSTIDDKVLLKSDGMPTYHLANIVDDHLMEITHVIRGEEWLPSAPLHVLLYRFLGWEDTMPQFAHLPLLLKPDGNGKLSKRDADAGGFPIFPLDWKDPASGDTWIGFKQQGYLQEATTNFLAFLGWNPGTQ... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 58622
Sequence ... |
Q3Z6S3 | MTNEVRVRYAPSPTGYPHLGNIRTAMFNWLFARHNGGKFIVRIEDTDRERYVEGAVESILESLNWLGLDWDEGPDKGGDYGPYYQSERLFLYRQAAERLVTEGKAYYCHCSSERLDKMREEQIARKEPPGYDRCCRDLCLGQKEGAVIRFKIPLEGQTTFIDLIRGEVTFDNAKQDDFVILKSDGFPTYHLASVVDDHAMQISHVLRAEEWLPSTPKHLMLYKALGYTPPQYAHLPMILGPDRSKLSKRHGATSTIEYKQAGYLPETMVNFLSLLGWAYDDKTELFSRKQLIEYFCLEKVSKTAAIFNYEKLDWMNGMYI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(... |
Q9RX30 | MSAPSSPRVTRIAPSPTGDPHVGTAYIGLFNHTLARQSGGRFILRVEDTDRNRYVPDSEKRIFQMMQWLNLTPDESPLQGGPNGPYRQSERFDLYGDYARQLVQSGHAYYAFETSDELAALREEAQKAGHVIAIPSRDLGAAQAQARVDAGEPAVIRLKVDRDGETVVNDLLRDPIHFANKEIDDKVLLKADGFPTYHLANVVDDRLMQVTHVVRAEEWITSTPIHVLLYRAFGWPEPVFAHMPLLRNADKSKISKRKNPTSVEWYQNQGFLPEAMLNFLATMGWTHPDGQEIFDLAEFERVFRLEDVTLGGPVFDLAKL... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 54689
Sequence ... |
B1I4Z1 | MDTVRVRFAPSPTGSLHIGGARTALFNWLFARHHGGAFILRLEDTDTGRNIDEAAAQIVSSLRWLGIDWDEGYDRGGPFGPYRQSERFELYREEARRLLANGDAYWCYCTPEDLAAQREEARQRGEVPRYDGRCRQLTDDARREKEAAGIRPALRVKMPKTGTTVVKDRIRGEIGFDNATLDDIIVMKSNGGPTYNFACVVDDGAMRISHVIRAEEHLSNTPKQIVLFNLLGYALPEFVHVPMILAPDRSKLSKRHGATAVDEFRADGFLPEALINYLALLGWSPGSEQEQFTVEELVASFSLDAVSKHAAIYDVKKLTW... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 55843
Sequence ... |
Q250Q8 | MLKVRFAPSPTGPLHIGGARSALFNYLLARKEDGVFIVRSEDTDLERSSRESEHNIMEALRWLNIQWDEGIEVGGDNGPYRQTERLALYQEYTDRLLASGDAYYCYCSEEELEQERQDLMAKGETPRYLGKCRHLSAAERQTYEAAGRKPVVRFRVPEGRQILINDRVRGEVVFDSDGIGDYVIVKSDGIPTYNFAVVIDDTTMNITHVIRGEEHLSNTPRQVLIYQALGLPTPEFAHISLILNTEGKKMSKRDGDTAVIDYQAKGYLPEAVVNFIALMGWSPPGEEEFFTLEEMTQAFSLERVSKSPAVFDLNKLNYMN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(... |
A8ZWA3 | MKQIITRFPPSPTGHLHIGGARTALFNWLYARHTGGRFILRIEDTDVERSTTQSAEGIIKSLEWLGIDWDEGPYFQSRRMEVYAEYIQRLLASGHAYYCTCSPERLKERRERALAEGRNPTYDGTCREKALPPSDDAVVRFRTPDTGKTVLDDRVKGGIAFDNAEIGDFIIQRSDQTPTYNFAVVVDDITMGINTIIRGDDHVTNTPRQILMYRALDSELPLFAHVPMVLGRDRSRLSKRHGAMSVLEYRDTGYLPDGLINALVRLGWSHGDQEFFTRKELIELFSLEHIGTSAGVFDPDKLLAINAEHIKKSDPAALAP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(... |
B2A4B3 | MTNKARLRFAPSPTGQIHIGNIRTALFNWLYSRHIDGEFILRVEDTDMNRSVEEYEQIIFRALSWLGLDWDEGPQKGGDFGPYRQSERKDIYHKYANKLLEAGKAYYCYCTEEELEEMREAQRARGEMPRYSGKCADLSSEERAELENEGRKSVIRFKVPENQTIRVNDLVKGEVDFESDGIGDFILIKSDDMASYNFACVVDDYLMNITHVLRGEDHLSNTPKQVMIYEALGFETPEFGHLSLILGPDKAKLSKRHGDTFIGEYREKGYLPEAMVNFLALLGWSPPGEDELFTQDELIRLFDIGRVSKSAAVFDVDKLN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(... |
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