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stringlengths 6
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Q3JAF1 | MGRVLVTIFVLFWPIGSFAAINLDRIVAVVNEDIVLESELEQMVRTVQDQLAAQGTSLPPGYVLERQVLERLVMEQLQLQLAARTGIQVGDETLNEALGRIAQDNGLTLSQFRNVLEQDGYDFPAFRENIRKELIISQLHKREVNDRVSVSKAEIDNFLTNQKKRGNQDAQYHLAHILITVPEAASPEQVQAAKAKAEQVLQQLREGADFQKVAVTYSDGQQALEGGDLGWRKMGQLPTLFVDVVPQLQAGDISKLIRSPSGFHIVKLLDYRGEGQQQLVTQTQARHILLRADELASEREVQLRLSQLRQRILSGDDFSELAQAHSDDKASALKGGDLGWVSPGQMIPRFEEAMRSLEPGEISEPFKTQFGWHVVQVLDRRQENMTEEFNRNRAKMEIRQRKVEEELENWLRQLRDEAYVEYRLDN | 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-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48473
Sequence Length: 426
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Subcellular Location: Periplasm
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Q145L3 | MKKLRLATLAAGLAAAASFLSVAPVQAQALSGSGGQTVDTIAAVVNNGVITRRELDERMGLITRRLNQQNAPVPPMDQLRQQVLNQMVLERIQLQKAKEDGITIDDATVQKTLERLAAANNLTLDVYRSRIEAQGVPWTTFTSDARTELTLSRLREKEVDSKVTVSDAEVANYIASQRGPNAGLTSDLHLQHIFLKAPLNASETDIEAAQRKAQALLAEAKGGANFEKLAKSNSQAPDASKGGDTGFVSPSKLPPEFVKAASALRPGEVNPDLIRTSDGFEIVRLVDRRAGQGTSSDAPKLVQTHVRHILLRVGDGMSEPQARQKLLEIKNEIAAGGDFAKFAHTYSQDGSSSQGGDLGWISPGETVPEFERAMNSLQDGQISDPVRSEYGYHLIQVLGRRESEGSVAQQMDLARQAIGQRKAEQAYADWLRELRDTAYVEVKPTLSSTQ | 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-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 48785
Sequence Length: 450
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Subcellular Location: Periplasm
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Q121Q4 | MTNDRLFAGIARVLSVRPLAAALALLLTLPLIGVQAQSLRPSSGLRLPTPAASAGAAAGSASGQRQADFIVAVVNSEPITNSEVRTKLVRTEQQIIQQGSPLPPRRELVPQVLERLISDKAQLQLARSAGMRVDDNAVEAAVQTVARQNQISVDELRRRLKADGIAYSQFESDLRDELLVSRLRQREVDLRVTVTEQDIDQFLREQEGGTELSSLALNLAQILVAVPENATPGQVAALQAKAQQVMDKARGGADFAALANEFSDSPTRGTGGLMGLREADRYPPLFVESTKSLKVGGLAGPIRSGAGFHILKVIEKRQAGMPGSVITQTHARHILLRLSPKQGETAATEKLAALRKRILAGQADFAALARENSEDASAKQGGDLGWANPGMFVPEFEKVMNGLAPNQISDPLVSRFGVHLIQVLERREAQMSQRDQREMARNVLRGKKQEEAYVLWAQEVRGRAYVEYRESPQ | 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-associated steps of protein maturation.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 51442
Sequence Length: 473
Domain: The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Subcellular Location: Periplasm
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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 | MATARAKARGSEAGARCHRAPGPPPRPKARRTARRRRAETLTARRSRPSAGERRAGSQRAWSGAPRAAVFGDECARGALFKAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVAKGVEYYLVKWKGWPDSTNTWEPLRNLRCPQLLRQFSDDKKTYLAQERKCKAVNSKSLQPAIAEYIVQKAKQRIALQRWQDYLNRRKNHKGMIFVENTVDLEGPPLDFYYINEYRPAPGISINSEATFGCSCTDCFFDKCCPAEAGVVLAYNKKQQIKIQPGTPIYECNSRCRCGPECPNRIVQKGTQYSLCIFKTSNGCGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFSVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKGSGEASSDSIDHSPAKKRVRTQCKCGAETCRGYLN | 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 functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.
PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation.
Catalytic Activity: L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 54098
Sequence Length: 477
Domain: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates in stable binding to heterochromatin (By similarity).
Subcellular Location: Nucleus
EC: 2.1.1.355
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Q28CQ7 | MAAARGAWCVPCLASIETLQELCRKEMLICTNIGITRKNLNNYEVEYLCDYRIEKGVEKFFVKWKGWPESCNTWEPTRNLKCPTLLKQFYSDLYNYFCALKPNKKGFLKNSIKSLDPSLSDYIVKKAKQRIALRRWEEELNRKKTHSGTLFVENTVDLEGPPMDFYYINDYKASPGVNTLGEAIVGCDCSDCFKGKCCPTEAGVLFAYNEHRQIKIPPGRPIYECNSRCKCGPDCPNRVVQKGPPYSLCIFRTDNGRGWGVKTLQKIKKNSFVMEYVGEVITSEEAERRGQQYDSRGITYLFDLDYEADEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDVRLPRIALFSTRNIKAGEELTFDYQMKGSGDFSTDSIDMSPAKKRVRIACKCGAATCRGYLN | 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 functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes (By similarity).
Catalytic Activity: L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 46350
Sequence Length: 406
Domain: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates in stable binding to heterochromatin (By similarity).
Subcellular Location: Nucleus
EC: 2.1.1.355
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Q9FF80 | MERNGGHYTDKTRVLDIKPLRTLRPVFPSGNQAPPFVCAPPFGPFPPGFSSFYPFSSSQANQHTPDLNQAQYPPQHQQPQNPPPVYQQQPPQHASEPSLVTPLRSFRSPDVSNGNAELEGSTVKRRIPKKRPISRPENMNFESGINVADRENGNRELVLSVLMRFDALRRRFAQLEDAKEAVSGIIKRPDLKSGSTCMGRGVRTNTKKRPGIVPGVEIGDVFFFRFEMCLVGLHSPSMAGIDYLVVKGETEEEPIATSIVSSGYYDNDEGNPDVLIYTGQGGNADKDKQSSDQKLERGNLALEKSLRRDSAVRVIRGLKEASHNAKIYIYDGLYEIKESWVEKGKSGHNTFKYKLVRAPGQPPAFASWTAIQKWKTGVPSRQGLILPDMTSGVESIPVSLVNEVDTDNGPAYFTYSTTVKYSESFKLMQPSFGCDCANLCKPGNLDCHCIRKNGGDFPYTGNGILVSRKPMIYECSPSCPCSTCKNKVTQMGVKVRLEVFKTANRGWGLRSWDAIRAGSFICIYVGEAKDKSKVQQTMANDDYTFDTTNVYNPFKWNYEPGLADEDACEEMSEESEIPLPLIISAKNVGNVARFMNHSCSPNVFWQPVSYENNSQLFVHVAFFAISHIPPMTELTYDYGVSRPSGTQNGNPLYGKRKCFCGSAYCRGSFG | 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
Sequence Mass (Da): 74471
Sequence Length: 670
Domain: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity.
Subcellular Location: Nucleus
EC: 2.1.1.368
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Q93YF5 | MEQGLRSDGNNPPSIDKTRVLDVKPLRCLAPVFPSPNGMSSVSTPQPSPFVCVPPTGPFPPGVAPFYPFVAPNDSGRPGESSQQTPSGVPNQGGPFGFAQPISPVPLNSFRTPTTANGNSGRSRRAVDDDDYSNSQDQNDQFASGFSVHVNNVEDSGTGKKRGRPKKPRRAQQAEGLTPVEVDVEPLLTQLLTSFKLVDLDQVKKADGDKELAGRVLLVFDLFRRRMTQIDESRDGPGSGRRPDLKASNMLMTKGVRTNQTKRIGNAPGIEVGDIFFFRMELCLVGLHAPTMAGIDYMSVKLTMDEEPLAVSIVSSGGYDDDGGDGDVLIYTGQGGVQRKDGQVFDQKLERGNLALEKSVHRANEVRVIRGVKDVAYPTGKIYIYDGLYKIQESWAEKNKVGCNVFKYKLLRVPGQPEAFKVWKSIQQWKDGVASRVGVILPDLTSGAESQPVCLVNDVDDEKGPAYFTYIPSLKYSKPFVMPRPSPSCHCVGGCQPGDSNCACIQSNGGFLPYSSLGVLLSYKTLIHECGSACSCPPNCRNRMSQGGPKARLEVFKTKNRGWGLRSWDPIRGGGFICEYAGEVIDAGNYSDDNYIFDATRIYAPLEAERDYNDESRKVPFPLVISAKNGGNISRFMNHSCSPNVYWQLVVRQSNNEATYHIAFFAIRHIPPMQELTFDYGMDKADHRRKKCLCGSLNCRGYFY | 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)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 77401
Sequence Length: 704
Domain: The SET domain is required for methyltransferase activity and ectopic effect on plant growth.
Subcellular Location: Nucleus
EC: 2.1.1.-
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O22781 | MSTLLPFPDLNLMPDSQSSTAGTTAGDTVVTGKLEVKSEPIEEWQTPPSSTSDQSANTDLIAEFIRISELFRSAFKPLQVKGLDGVSVYGLDSGAIVAVPEKENRELIEPPPGFKDNRVSTVVVSPKFERPRELARIAILGHEQRKELRQVMKRTRMTYESLRIHLMAESMKNHVLGQGRRRRSDMAAAYIMRDRGLWLNYDKHIVGPVTGVEVGDIFFYRMELCVLGLHGQTQAGIDCLTAERSATGEPIATSIVVSGGYEDDEDTGDVLVYTGHGGQDHQHKQCDNQRLVGGNLGMERSMHYGIEVRVIRGIKYENSISSKVYVYDGLYKIVDWWFAVGKSGFGVFKFRLVRIEGQPMMGSAVMRFAQTLRNKPSMVRPTGYVSFDLSNKKENVPVFLYNDVDGDQEPRHYEYIAKAVFPPGIFGQGGISRTGCECKLSCTDDCLCARKNGGEFAYDDNGHLLKGKHVVFECGEFCTCGPSCKSRVTQKGLRNRLEVFRSKETGWGVRTLDLIEAGAFICEYAGVVVTRLQAEILSMNGDVMVYPGRFTDQWRNWGDLSQVYPDFVRPNYPSLPPLDFSMDVSRMRNVACYISHSKEPNVMVQFVLHDHNHLMFPRVMLFALENISPLAELSLDYGLADEVNGKLAICN | 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 cytosine, but PubMed:19043555 see no significant effect on histone methylation when the gene is mutated. According to PubMed:19043555, the protein does not bind S-adenosyl-L-methionine and lacks methyltransferase activity. Instead, it may function downstream of DRM2 in RNA-directed DNA methylation, binding to methylated DNA and recruiting DNA-directed RNA polymerase V to chromatin .
Sequence Mass (Da): 72848
Sequence Length: 651
Domain: Although both SET and pre-SET domains are present, the absence of the post-SET domain may explain the lack of methyltransferase activity. Besides, the Cys residues in the SET domain that normally bind a zinc ion are not conserved.
Subcellular Location: Nucleus
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Q5QD03 | MATIQLTDQQRKVLHEVACTTAAPVLDTASKDKIKQLLDDYDMRKAAMGSKPGANMVLPGQVLGEAGPFLDYGHPPGVALGDKFKDRGQVMVAGVHGTTVRGIHAPNAGSEHFVRGAYSVLMSGVYVDDEDMGEAFWYTGEGGMDGKKQVKDQQMASGSNAALKNNCDTRTPVRVVRGFVQEAGGGEGGGGGEGGGGAKKGKGGKGGGKKEKGLVYEGLYLVLECKMEPSKDGPQVCKFLMHGLPGHSTVSAKVEYNIFGNAGSAYSLHARRLAGAGAPAGGKRARKAAQDEKARELARQWMLSEIRRQYPGPELQLEDVSGGQEAVPIPVINQVNSERLPTDFAYTREYAWAPGVYQLVAPALRLADEEMLQFSREGDRGGVCGIAFNRHIAALDRRLEQEGRLPQGYEAHLEEQYNAAGCLMVTDPCGVHECGDGCSAKACRRNMQLSAGVQLPLEVFMTESKGWGVRCREEVPAGAFVCCYVGQLITDAMAEVRKGVDHYLFDLDFFAHIYAEIAEKGMQAVAEEIPLHKIPPVLSVGMIRQAQINAADAARRLPEQQPQQQQPQQQQQQPAAGGAAPGGAAAGEQAAGGAEGGGAYGGGGAAAAATAAGTAPGAGDNMDGVEGPAAQRSGGEEAAAGPGSSGAAGGCGYRLDGMVTREGLAQAAHALAEACDALARSVADGASTNLGGENILAAIEAAKARAAAAATTSGGAAAADQHQLEQLDRAAALAAASKAAADAVKAGDPGAFYLQPIISRDEEKAAERAAAAAAAAAAAAGVPPALPSTSDVGNGGTTGSGGGGGAFSNRGPAGCAVGSPRALAARSGMEAAAQAAGGAASGPVAGPGAVEDHGEEYAPMLVIDARTTGNVGRFINHSCDGNLTIQAVFAGVYRSTLLYHVGLYACRNIPQLEELSYNYGYHKQQQQQQQAQRGGAAEKQFVMQCNCGAVGCIGNLM | 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 Mass (Da): 98344
Sequence Length: 957
Subcellular Location: Nucleus
EC: 2.1.1.367
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Q8GZB6 | MAGKRKRANAPDQTERRSSVRVQKVRQKALDEKARLVQERVKLLSDRKSEICVDDTELHEKEEENVDGSPKRRSPPKLTAMQKGKQKLSVSLNGKDVNLEPHLKVTKCLRLFNKQYLLCVQAKLSRPDLKGVTEMIKAKAILYPRKIIGDLPGIDVGHRFFSRAEMCAVGFHNHWLNGIDYMSMEYEKEYSNYKLPLAVSIVMSGQYEDDLDNADTVTYTGQGGHNLTGNKRQIKDQLLERGNLALKHCCEYNVPVRVTRGHNCKSSYTKRVYTYDGLYKVEKFWAQKGVSGFTVYKYRLKRLEGQPELTTDQVNFVAGRIPTSTSEIEGLVCEDISGGLEFKGIPATNRVDDSPVSPTSGFTYIKSLIIEPNVIIPKSSTGCNCRGSCTDSKKCACAKLNGGNFPYVDLNDGRLIESRDVVFECGPHCGCGPKCVNRTSQKRLRFNLEVFRSAKKGWAVRSWEYIPAGSPVCEYIGVVRRTADVDTISDNEYIFEIDCQQTMQGLGGRQRRLRDVAVPMNNGVSQSSEDENAPEFCIDAGSTGNFARFINHSCEPNLFVQCVLSSHQDIRLARVVLFAADNISPMQELTYDYGYALDSVHGPDGKVKQLACYCGALNCRKRLY | 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 an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements.
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-homocysteine
Sequence Mass (Da): 70056
Sequence Length: 624
Domain: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity.
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8VZ17 | MEMGVMENLMVHTEISKVKSQSNGEVEKRGVSVLENGGVCKLDRMSGLKFKRRKVFAVRDFPPGCGSRAMEVKIACENGNVVEDVKVVESLVKEEESLGQRDASENVSDIRMAEPVEVQPLRICLPGGDVVRDLSVTAGDECSNSEQIVAGSGVSSSSGTENIVRDIVVYADESSLGMDNLDQTQPLEIEMSDVAVAKPRLVAGRKKAKKGIACHSSLKVVSREFGEGSRKKKSKKNLYWRDRESLDSPEQLRILGVGTSSGSSSGDSSRNKVKETLRLFHGVCRKILQEDEAKPEDQRRKGKGLRIDFEASTILKRNGKFLNSGVHILGEVPGVEVGDEFQYRMELNILGIHKPSQAGIDYMKYGKAKVATSIVASGGYDDHLDNSDVLTYTGQGGNVMQVKKKGEELKEPEDQKLITGNLALATSIEKQTPVRVIRGKHKSTHDKSKGGNYVYDGLYLVEKYWQQVGSHGMNVFKFQLRRIPGQPELSWVEVKKSKSKYREGLCKLDISEGKEQSPISAVNEIDDEKPPLFTYTVKLIYPDWCRPVPPKSCCCTTRCTEAEARVCACVEKNGGEIPYNFDGAIVGAKPTIYECGPLCKCPSSCYLRVTQHGIKLPLEIFKTKSRGWGVRCLKSIPIGSFICEYVGELLEDSEAERRIGNDEYLFDIGNRYDNSLAQGMSELMLGTQAGRSMAEGDESSGFTIDAASKGNVGRFINHSCSPNLYAQNVLYDHEDSRIPHVMFFAQDNIPPLQELCYDYNYALDQVRDSKGNIKQKPCFCGAAVCRRRLY | 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(9)-[histone H3] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 87477
Sequence Length: 790
Domain: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity.
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q9C5P0 | MVSTPPTLLMLFDDGDAGPSTGLVHREKSDAVNEEAHATSVPPHAPPQTLWLLDNFNIEDSYDRDAGPSTGPVHRERSDAVNEEAHATSIPPHAPPQTLWLLDNFNIEDSYDRDAGPSTSPIDREASHEVNEDAHATSAPPHVMVSPLQNRRPFDQFNNQPYDASAGPSTGPGKRGRGRPKGSKNGSRKPKKPKAYDNNSTDASAGPSSGLGKRRCGRPKGLKNRSRKPKKPKADDPNSKMVISCPDFDSRITEAERESGNQEIVDSILMRFDAVRRRLCQLNYRKDKILTASTNCMNLGVRTNMTRRIGPIPGVQVGDIFYYWCEMCLVGLHRNTAGGIDSLLAKESGVDGPAATSVVTSGKYDNETEDLETLIYSGHGGKPCDQVLQRGNRALEASVRRRNEVRVIRGELYNNEKVYIYDGLYLVSDCWQVTGKSGFKEYRFKLLRKPGQPPGYAIWKLVENLRNHELIDPRQGFILGDLSFGEEGLRVPLVNEVDEEDKTIPDDFDYIRSQCYSGMTNDVNVDSQSLVQSYIHQNCTCILKNCGQLPYHDNILVCRKPLIYECGGSCPTRMVETGLKLHLEVFKTSNCGWGLRSWDPIRAGTFICEFTGVSKTKEEVEEDDDYLFDTSRIYHSFRWNYEPELLCEDACEQVSEDANLPTQVLISAKEKGNVGRFMNHNCWPNVFWQPIEYDDNNGHIYVRIGLFAMKHIPPMTELTYDYGISCVEKTGEDEVIYKGKKICLCGSVKCRGSFG | 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-homocysteine
Sequence Mass (Da): 84528
Sequence Length: 755
Domain: Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity.
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q9T0G7 | MGSSHIPLDPSLNPSPSLIPKLEPVTESTQNLAFQLPNTNPQALISSAVSDFNEATDFSSDYNTVAESARSAFAQRLQRHDDVAVLDSLTGAIVPVEENPEPEPNPYSTSDSSPSVATQRPRPQPRSSELVRITDVGPESERQFREHVRKTRMIYDSLRMFLMMEEAKRNGVGGRRARADGKAGKAGSMMRDCMLWMNRDKRIVGSIPGVQVGDIFFFRFELCVMGLHGHPQSGIDFLTGSLSSNGEPIATSVIVSGGYEDDDDQGDVIMYTGQGGQDRLGRQAEHQRLEGGNLAMERSMYYGIEVRVIRGLKYENEVSSRVYVYDGLFRIVDSWFDVGKSGFGVFKYRLERIEGQAEMGSSVLKFARTLKTNPLSVRPRGYINFDISNGKENVPVYLFNDIDSDQEPLYYEYLAQTSFPPGLFVQQSGNASGCDCVNGCGSGCLCEAKNSGEIAYDYNGTLIRQKPLIHECGSACQCPPSCRNRVTQKGLRNRLEVFRSLETGWGVRSLDVLHAGAFICEYAGVALTREQANILTMNGDTLVYPARFSSARWEDWGDLSQVLADFERPSYPDIPPVDFAMDVSKMRNVACYISHSTDPNVIVQFVLHDHNSLMFPRVMLFAAENIPPMTELSLDYGVVDDWNAKLAICN | 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 function downstream of DRM2 in RNA-directed DNA methylation, binding to methylated DNA and recruiting DNA-directed RNA polymerase V to chromatin .
Sequence Mass (Da): 72174
Sequence Length: 650
Domain: Although both SET and pre-SET domains are present, the absence of the post-SET domain may explain the lack of methyltransferase activity. Besides, the Cys residues in the SET domain that normally bind a zinc ion are not conserved.
Subcellular Location: Nucleus
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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 domains are present, the absence of the post-SET domain may alter the methyltransferase activity.
Subcellular Location: Nucleus
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Q9FNC7 | MAPNLHIKKAFMAMRAMGIEDARVKPVLKNLLALYEKNWELIAEDNYRVLADAIFDSHEDQAIQESEEKKADEVKEDEGCAAEVDRGKKKLHESIEDDEDVMAESDRPLKRLRRRGEGGSALASPSLGSPTLEGPSINDEENAPILLPYHPVPIENDHDAGELILTKVEPITNMPLSSIPDSVDRGDSSMLEIDKSNGHVEEKAGETVSTADGTTNDISPTTVARFSDHKLAATIEEPPALELASSASGEVKINLSFAPATGGSNPHLPSMEELRRAMEEKCLRSYKILDPNFSVLGFMNDICSCYLDLATNGRDSANQLPKNLPFVTTNIDALKKSAARMAYTSQASNDVVEICSNEHMRDAENGAVGDSMALVVVPECQLSADEWRLISSVGDISLGKETVEIPWVNEVNDKVPPVFHYIAQSLVYQDAAVKFSLGNIRDDQCCSSCCGDCLAPSMACRCATAFNGFAYTVDGLLQEDFLEQCISEARDPRKQMLLYCKECPLEKAKKEVILEPCKGHLKRKAIKECWSKCGCMKNCGNRVVQQGIHNKLQVFFTPNGRGWGLRTLEKLPKGAFVCELAGEILTIPELFQRISDRPTSPVILDAYWGSEDISGDDKALSLEGTHYGNISRFINHRCLDANLIEIPVHAETTDSHYYHLAFFTTREIDAMEELTWDYGVPFNQDVFPTSPFHCQCGSDFCRVRKQISKGKNVKKRA | 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 SUVR1 and associates with the SNF2-related chromatin-remodeling proteins CHR19, CHR27, and CHR28, thereby mediating nucleosome positioning and transcriptional silencing. Does not possess histone-lysine methyltransferase activity in vitro, and the conserved catalytic sites of SUVR2 are dispensable for its function in transcriptional gene silencing.
Sequence Mass (Da): 79363
Sequence Length: 717
Domain: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.
Subcellular Location: Nucleus
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Q9SRV2 | MQRLRESPPPKTRCLGEASDIIPAADRFLRCANLILPWLNPRELAVVAQTCKTLSLISKSLTIHRSLDAARSLENISIPFHNSIDSQRYAYFIYTPFQIPASSPPPPRQWWGAAANECGSESRPCFDSVSESGRFGVSLVDESGCECERCEEGYCKCLAFAGMEEIANECGSGCGCGSDCSNRVTQKGVSVSLKIVRDEKKGWCLYADQLIKQGQFICEYAGELLTTDEARRRQNIYDKLRSTQSFASALLVVREHLPSGQACLRINIDATRIGNVARFINHSCDGGNLSTVLLRSSGALLPRLCFFAAKDIIAEEELSFSYGDVSVAGENRDDKLNCSCGSSCCLGTLPCENT | 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; some of these Cys residues contribute to the binding of two zinc ions within the cluster.
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8W595 | MISLSGLTSSVESDLDMQQAMLTNKDEKVLKALERTRQLDIPDEKTMPVLMKLLEEAGGNWSYIKLDNYTALVDAIYSVEDENKQSEGSSNGNRGKNLKVIDSPATLKKTYETRSASSGSSIQVVQKQPQLSNGDRKRKYKSRIADITKGSESVKIPLVDDVGSEAVPKFTYIPHNIVYQSAYLHVSLARISDEDCCANCKGNCLSADFPCTCARETSGEYAYTKEGLLKEKFLDTCLKMKKEPDSFPKVYCKDCPLERDHDKGTYGKCDGHLIRKFIKECWRKCGCDMQCGNRVVQRGIRCQLQVYFTQEGKGWGLRTLQDLPKGTFICEYIGEILTNTELYDRNVRSSSERHTYPVTLDADWGSEKDLKDEEALCLDATICGNVARFINHRCEDANMIDIPIEIETPDRHYYHIAFFTLRDVKAMDELTWDYMIDFNDKSHPVKAFRCCCGSESCRDRKIKGSQGKSIERRKIVSAKKQQGSKEVSKKRK | 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 silencing of pseudogenes and transposons. 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-homocysteine
Sequence Mass (Da): 55855
Sequence Length: 492
Domain: In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.
Subcellular Location: Nucleus
EC: 2.1.1.-
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P32944 | MSSLDEDEEDFEMLDTENLQFMGKKMFGKQAGEDESDDFAIGGSTPTNKLKFYPYSNNKLTRSTGTLNLSLSNTALSEANSKFLGKIEEEEEEEEEGKDEESVDSRIKRWSPFHENESVTTPITKRSAEKTNSPISLKQWNQRWFPKNDARTENTSSSSSYSVAKPNQSAFTSSGLVSKMSMDTSLYPAKLRIPETPVKKSPLVEGRDHKHVHLSSSKNASSSLSVSPLNFVEDNNLQEDLLFSDSPSSKALPSIHVPTIDSSPLSEAKYHAHDRHNNQTNILSPTNSLVTNSSPQTLHSNKFKKIKRARNSVILKNRELTNSLQQFKDDLYGTDENFPPPIIISSHHSTRKNPQPYQFRGRYDNDTDEEISTPTRRKSIIGATSQTHRESRPLSLSSAIVTNTTSAETHSISSTDSSPLNSKRRLISSNKLSANPDSHLFEKFTNVHSIGKGQFSTVYQVTFAQTNKKYAIKAIKPNKYNSLKRILLEIKILNEVTNQITMDQEGKEYIIDYISSWKFQNSYYIMTELCENGNLDGFLQEQVIAKKKRLEDWRIWKIIVELSLALRFIHDSCHIVHLDLKPANVMITFEGNLKLGDFGMATHLPLEDKSFENEGDREYIAPEIISDCTYDYKADIFSLGLMIVEIAANVVLPDNGNAWHKLRSGDLSDAGRLSSTDIHSESLFSDITKVDTNDLFDFERDNISGNSNNAGTSTVHNNSNINNPNMNNGNDNNNVNTAATKNRLILHKSSKIPAWVPKFLIDGESLERIVRWMIEPNYERRPTANQILQTEECLYVEMTRNAGAIIQEDDFGPKPKFFI | 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 growth, actin organization or bud formation. Inhibits the activity of B-type cyclins in replication initiation strongly for CLB2, moderately for CLB3 and CLB4, and there is no apparent inhibition for CLB5 and CLB6, correlating with the normal expression timing of those cyclins. Hyperphosphorylation and degradation of SWE1 when all checkpoint requirement are met releases CLB2-CDC28 from inhibition and allows for progression through the cell cycle. SWE1-dependent CDC28 phosphorylation is also required for pachytene arrest upon activation of the recombination checkpoint during meiosis. Also involved in the regulation of nitrogen starvation- and short chain alcohol-induced filamentous growth, or filamentous differentiation in response to slowed DNA synthesis. Can act both on serines and on tyrosines.
PTM: Ubiquitinated by the SCF(MET30) complex, leading to its degradation by the proteasome.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 92468
Sequence Length: 819
Subcellular Location: Bud neck
EC: 2.7.11.1
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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 does not affect mammal F11 sodium channels.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 9383
Sequence Length: 83
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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Q90ZH7 | MHRSSYCREETTLCQGVNSTWVPPADTVPEASLTPHSPPAPDSPAPSPKPGYGYSACEEKPGDPRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGQSWKNLTSAEKRPFVEEAERLRVQHLQDHPNYKYRPRRKKQAKKLKRMDPSHHLRNEGYTGGQPMVNLSHFRELHPLGGSGELESYGLPTPEMSPLDVLEPSEPAFFPPHMREDPDPGLFRTYQHEMDFSQEKTLREISLPYSTSPSHMGSFLRTPTPSAFYYKPHGGSSARTPLGQLSPPPEAPALDAMDHLNHAELWGDFDLNEFDQYLNMSRTQGPGYSFPMSKLGGPRTIPCEENSLISALSDASTAMYYTPCITG | 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 interact to initiate cardiogenesis. Also acts as an antagonist of beta-catenin signaling.
Sequence Mass (Da): 40585
Sequence Length: 361
Domain: Binds target DNA via the HMG box domain.
Subcellular Location: Nucleus
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A8MBI2 | MPILNESLLRTRIFIGRGFRRSRCPYCGHHYWTLNPSQDNCGDQPCTPYGFIGNPPGTYRPESIKDVRERFLSFFEKRGHTRVARYPVVARWRNDVYLVGASIYDFQPWVTEGVVPPPANPLTISQPSIRLTDVDKVGRSGRHLTGFEMMAHHAFNFPGKEIYWINETVEYAHEFFTRELGFRDDEVTYKENIWEGGGNAGESFEVLVRGLELATLVFMHYRVIGDEYREMPIRIVDTGYGLERIYWVLTGKPTIYEAVFEGFLNKARQLLGLPKPDEKVLASLAIHMGQLDPEVLALDKAYVEVAKRIGIDSSELINFIKPQEALYVLADHSRTVSWMINDGVIPSNSGVGYLARLLIRRMLKYMHVIGAQVPLTEIFNTHLNYLINDYPELKESMQLILDLVDLEEAKYKSAISQLPKLISRIKGELTINDLINLYDSHGIPPEVVRDEAAKRGVKVNVPDNFYEMLAARHQKPAKGEEGNRLDVTADDVIDLPPTRELFYEDTYAFEGKAKVLKVIKGKYIVLDSTIFYPEGGGQPADRGVLRFNGVEAKVVDVQRVGPVIVHVIDGPTPGVGDVVEMRIDSERRLGLMRMHTGTHILLQSIRRVLGKHVWQAGAQKDIPLSRLDVTHYRLPTPDEVKRIEELANEVVLSDLPVKAELMPRNEAEAKYGFIIYQGGVVPGGEVRIVKVGEGNDTYDVEACGGTHLDRTSRIGLIKIVKVDKIQEGVIRFIFTTGKYALDYVRNLEGKLDSAASKLRVGRDEVDEAVDRLIKELNNAEERSRVLARKAIEADLANIVKSMITVSGFKVAVYYEDYWVRDYLQELASKYPGDVLVLIHGNEYQVYTNGKVKAIDVAKVLNELGGKGGGSGTFAQGVFNNPVKQDDVVNTIKRKLTLTQ | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 101305
Sequence Length: 899
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q8RAH4 | MEKLGMNEIREKFLSFFESKGHLRLPSFSLVPKNDKSLLLINSGMAPLKPYFTGKETPPSRRVTTCQRCIRTPDIERVGKTARHATFFEMLGNFSFGDYFKKEAIPWAWEFVAEVLKLPVDRLWVTIYEEDDEAFEIWNKIVGLPPERIVRMGKEDNFWEIGTGPCGPCSEIYFDRGEEKGCGKPDCGIGCDDCDRYVEFWNLVFTQFNKDEQGNYHRLPNPNIDTGMGLERIAAIMQGVDTIFDVDVIRGIRDFISDLAEVEYGKDADKDVSIRVITDHIRGITFMISDGILPSNEGRGYVLRRLLRRAARHGKLLGLNDAFLYKVVDSVVENYGGAYPEIIERKDYIKKIIKLEEERFKETVDQGLAILQDYINELKAQGKTVLEGAKAFKLYDTYGFPLDLTKEILQESGITIDEEGYKEELEKQRVRARSSRKEDNSLWEQDIYSTLGDISTKFVGYEVYESEAKVLAIVKDNEVVEQAEAGDDVSIILDVTPFYAESGGQVGDSGVIEEEDTLIKVNDCKKVGNKFIHIGTVERGLISVGDKVVAKIDVSKRKGAARNHTATHLLHKALKEVLGDHVNQSGSLVAYDRLRFDFSHYQAVSKEELKKIEERVNEKIYEQLPVVVEEKNYEDALKEGAVALFTEKYGDKVRVVKIDDYSMELCGGTHVKNTSEIGIFKIVSESAVGAGLRRIEALTGIEAIKYLNEQKEILDRVSETLKAQEKEVVSKIENLQQSLKDKEREIEGLKTKIASILAETLIDSAISVDGVKVIASRVEDYDMEALKTLGDILKDRLKSAAVILASSSKDKALFVGMATKDAVEKGVNMGAVIKETCSIAEGNGGGRAEMAQGTGKNISKVKEALEKAIEIVKGQLKA | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 98363
Sequence Length: 878
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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A0RPR0 | MDIRKEYLDFFKSKGHEIITSAPLVPDDATLLFTNAGMVPFKSIFTGDVPRPNPPIRTSCQTCIRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGEYFKKDAISYAWEFVTEVLKLPKDKLYVTVHEKDDEAYELWQKFIQKDRIYRFGDKDNFWAMGDTGPCGPCSEIFYDQGSEHFNSDEDYMGGDGDRFLEIWNLVFMQFERSKDGTMTPLPKPSIDTGMGLERVTAIKEDKFSNYDSSLFMPLINEVAKLCHKQYEYKTGASYRVISDHIRSVTFLLAQGVNFDKEGRGYVLRRILRRAVRHGYLLGIKEPFMYKLVDKVVELMGEHYSYLKEKKEYVKELIKLEEERFLATIVAGLDLFNEELAKTSSNVFSGEVAFKLYDTYGFPLDLTADMLREKGLSVDEAKFDALMNEQKARAKASWKGSGDAAKESGDFKTLLEEFGENKFIGYDNLKSSSKVLALLNSEFKRVNELKNGEIGYVMLDSTPFYAQSGGQCGDTGMLGENQALDTKKYFGLNLSMIEAKNSIKIGDIVLCEVSLNRLEIRRHHSATHLLQAALRNVLGAHIAQAGSSVEADKLRFDFSHPKPVTKEELEKIENFVNEAILKGAPAKIEIMDIQNAKKSGAIALFGEKYADKVRVLTLGPSKELCGGTHVENLNEIGSFFIVRESGVSAGVRRIEAVCSKAALELSKEFRKEINDIKDSLKGADPLLSIKKLKDEIKSLQNDLKNASNTKDLDVKDINGVKVVVSKFDGDIKSKIDELKNKFDKVVVFLAGVKDGKVSLGSGSKNTSIKAGELVKTVAPIVGGGGGGRDDFATAGGKDESKIDEALNAATKFISEKL | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 94276
Sequence Length: 845
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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A6WCF7 | MQTAEIRRRWLDFFERKEHTVVPSASLVSSDPSLMFTVAGMVPFIPYLTAQVPAPYKRATSVQKCLRTLDIDEVGKTTRHGTFFQMNGNFSFGDYFKREAVAFAWELLTTPEADGGLGFDPERLWTTVYLDDDEAFQLWREVGMPAERIQRRGKADNYWNTGQPGPGGPCSEIYFDRGPAYGAEGGPEADEDRYIEIWNLVFMQYQLSAVRTKVDFDVEGELPAKNIDTGMGLERVAFLKQGVDNMYEIDEVRPVLDKAAELSGRRYGAVHEDDVRMRVVADHVRSALMLIGDGVTPGNEGAGYVLRRLVRRAVRAMRLLGVEEPALPHLLPASMEVMSASYPQLRSDFERISAVAYAEEDAFRRTLVSGTAIFETAVAQTKAAGGSSLSGERAFALHDTYGFPIDLTLEMAAEAGVGVDEPGFRALMAEQVGRAKADAKAKKTGGVDLAIYRSTLEQLPAPVVFTGYEAAAGEARISVVLQGGVSTPSAPAGTDVEVVLDRTPFYAEGGGQLADHGTVTTTSGAVLAVSDVQQPVRGLYVHKGTVTSGELVAGDAVHAVVDAGRRRSISRAHTATHLVHQVVREHLGDTATQAGSQNAPGRMRFDYRSTAQVAGDVVRDIEAVVNERIHDDLEVSAAVMDRESALNSGAMALFGEKYGEKVRVVSIGEDWSKELCGGTHTLTSQQVGLVSIVSESSIGSGARRIEALVGADAFDFLTREHLLVNQLTEVVKARPEELPDRIGALLTRLGDAEKEIARLRGGQVLALAPTIAAKPVDKFGVRVVTHDAGPVSADDLRTLVLDVRSRLGEERPSVVAVAGVAKDRPVVVVATNAEARRWGVKAGELVRTAAKTLGGGGGGKDDLAQGGGQDPSKVPAALQGIEDFVGARVTGSV | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 95953
Sequence Length: 893
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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B1L762 | MQGIEVEFLRSRGYVRKRCPKCGEYFWTLKDRETCGEAPCEPYTFIGRGRQNKSLEEVREDFLRFFERRGHTRINRYPVIARWREDLFLTSASIVDFQPFITAGIVPPPANPLTISQPCIRLKDIDKVGPTMGRHLSIFEMMAHHAFNTKDKFVYWIDRTVELFHEYATSVLGIPEEEITYKEGIWEGGGNAGPDLEPIAGGLEIATLVFMQYRIENGSYVPMDTRVVDTGYGLERITWFLRGDPTGFHAVYGALLHEFMDKLGVSEPDLSLLSEYSKVSSILRELEKGRSISSLRREAALLIGVSEEELEEKIAPLEAVFSLLDHTKALSFMIADGLVPSNVNEGYLGRLLIRRSLRILNQLGSEVPLSELAVRQAEYWSSKGFPELREAIDRIAEIVSIEEERYKEAVERGAKIISDLMREKGRLSVDDLIMLYDSHGLSPDIVRRIAGDVDVPDNFFEMIAARHEARKPEPPKVFERMDELRRYPPTKLLYYQDPYLLEFEARVLGYVDGKMILDRTAFYPEGGGQPSDIGSFEWRGIEVKVVGAEKHGGWILHSVEGDLPPAGEVVRARVDSWRRLNRMRHHTATHVILEAARRVLGSHVWQWGAQKGDEESRLDITHYKGISQEELRRIEMLANEVVMRNIPVRTLWLVRTDAERRYGFTLYQGGVVPDPVLRVVEIEGFNAQACGGTHVLRTGEIGPIKIWRARKIQDGVIRLEFSAGVPAVKRIIDYHQKIKDIAQSAGISEEEIDTFFRGMMEELKELRKERRRMMKEAEERSIERALEAYESTGRHKLSIVRLESIGIDEGIKLADKLSSDRRIVLLTKESGDRVELALLATNYGEGEVDAGSLLRELSREMGGGGGGNWKLGKGSVPKDRLDEFMGVLRKRLEGI | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 101833
Sequence Length: 895
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q1G947 | MKKLNSSEFRQMFLDFFAEHGHMVMQSASLIPKDDPTLLWINSGVATMKKYFDGSVVPKNRRITSSQKSIRTNDIENVGKTARHQTLFEMLGNFSVGDYFKEEAIPWAWEFLTSPDWLDLDKDKLYVTVYPKDTEAHRIWHEVVGLPESHIVQLEDNFWDIGEGPCGPDSEIFYDRGQENNDVPEDDPENYPGGENARYLEIWNIVFSEFNHLPDGSYVEQPHKNIDTGMGLERVLSILQDAPTNFETDLFLPIIHATEEMSAGKKYGANKADDISFKIIADHIRAISFAIGDGALPGNTGRGYVLRRLLRRAALNGRKLGIDGAFLYKLVPVVGDIMKSHYPEVSDQAEFISKVVKNEEDRFGATLEAGLTLLDDLIDKAENSEDKTISGKDAFKMFDTYGFPYELTVEAAEDKGLKVDKDGFDAEMEAQKERARKARGNLQSMGSQDETLMKIKDKSVFEYGVYEEESQLVDIIVDDKLVDKADGEKATLIFDKTPFYAERGGQVADHGDIYDQEGNLVARVVDVQHAPNDQNLHFVDVVLPLVKGQTYKLKIDRARREGLRHSHSATHLLHAALRQVLGEHTHQAGSVVEPDYLRFDFTSLDPITPRELKNVEKIVNEKIWEAIQVKTTETDPETGKKMGALALFDGKYTDKVRVVQMDDFSIEFCGGTHCDNTSQIGVFKIISEQAIGAGVRRIEAVTSKLAYEYLAGRSDILDQIQAQVKATKVDGIQSKIASLQEELRSAEKQNAAYEAQINASKAGKIFDQVKTVGDLTVIATIADVKGMNDLREIADQWKSEGKSDVLILGAKSEDKANMLISLGQKALDKGLKAGDLIKSVAAIFGGGGGGRPNMAQAGGKNPEGLQDAIDAAVSQLD | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 97400
Sequence Length: 877
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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Q2S2B6 | MSHDPMNPHLQSSADPSRSSEEIRQDFLQFFQAKGHEVVPSASLVPDGDGTLLFTNAGMNQFKDVFLGTGQRPYSRAVDTQKCLRVSGKHNDLEEVGHDTYHHTFFEMLGNWSFGDYFKAEAIRWAWELLVERWGLAPDRLYATVHEGDDDFGLSADAEAYDLWLSETPLPEERVLYEPSKENFWMMGDTGPCGPCSELHVDLRPPEARQETPGRELVNVDHPQVMELWNLVFIQYNAQTDGSLEPLDDQHVDTGMGFERMVAVLQGKESTYDTDLFAPLLQAMADRSPREEIRGYDDLHIEDDDEHEQVRIALRVVADHIRAIAFAISDGVMPSNEGRGYVIRRILRRAVRYGYQTLELEEPFLHRLVDPLIEKMGGPFDGLAEQQEFIEQAIRSEEESFLETLGTGIEFFERVVPHVTGFQDTDGEESDRLLGALREDAQAMDLLEKAYVDTDDENDILHSFARTARGGTLPGQIAFLLHDTYGFPIDLTRLMARERDLDVDMEGYETLMDRQQERARAASDFAVDQSDVQAWQSVSPGEASVFVGYDRAVVPDAEVRAVRVVETGDTQQYEVELSRTPFYAEAGGQVGDTGTLRFGDESVQVLDTQREGERIAHTVDTLPEPLDGPVEAAVDAERRNHIRAHHTATHLMHAVLRETLGDHVQQKGSLVAPDRLRFDFSHFDAVDEDTLRHIERRVNTAIQQNIPKQEARDVPIDEALDRGATALFDEQYGDRVRVITFDPDFSMELCGGTHVDATGEIGLFRFLSEGSVASGVRRVEAVAGKAALEHVESELETLTRARRQFRSLHTSLPEAIAEVQEERDRLAGEVDQLRRGQLSDQLDTFIAENAASVDGITVVTGRLDRASMDDLQELGQQFRDKLGEGAVGVLGSVGEDGEKAYVVATVADDLVDDGALRAGDLVGTLGDRLGGGGGGRPSLASAGGRDPEALDTVLDGVPALVRDRLE | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 107424
Sequence Length: 966
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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A4X5Z0 | MKTAEIRRRYLAHFEANGHAVVPSAPLPAISDPNLLFVAAGMMQFVPYFLGQQTAPYKRAVSVQKCLRTPDIDEVGKTSRHGTFFQMNGNFSFGDYFKDEAIPLAWELSTKPVDAGGLGLDPDRIWPTVYLDDDEAFQIWRSVGVPADRIVRRGKADNFWSMGIPGPCGPCSELFYDRGPEYGREGGPEVDEDRYLEFWNLVFMQFERGPGTGKEDYPILGDLPAKNIDTGMGLERMASILQGVDNLYEIDEVRPILAKAAELTGKRYGAHSGQVASESHPDDVRLRVVADHVRTALMLIGDGVIPSNEGRGYVLRRIMRRAIRSIRLLGWQERAMPELLPVARDCMSASYPELATDFGRIADYAYAEEDAFLSTLRAGTTILDTAIAETRTAGRRAISGAKAFQLHDTYGFPIDLTLEIASEQGLQVDAEGFRRLMADQRARAKADAQARKTGHVDLSAYRTVLDEGGPVTFTGYQEVSRESTVRAVLGAASPHAAAVEGETVELVLDTTPFYAEGGGQQPDLGVITVGGGQVEVLDVQQPVPGLIVHRARVLRGEVRVGETGFAEIDTDRRRAISRSHTATHLVHQTMRNFLGESATQAGSLNAPGRLRFDFNTPTGVAPSVLRDVEQQVNEALLADLEVRAFVTSLAEARRIGAMALFGEKYGEQVRVVEVGDYARELCGGTHVGRSGQLGLVKILSESSIGSGVRRVEALVGIDAFNFLAREHLLVARLAELYRVPSDQVAERVEQTVTQLRDAEKELEKLRAQLVLGGAAALAAQASEVRGVAYVGTEAPEGAAGNDVRTLAQEIRSRIDPARPAVVAVAARANGKASLVVAVNPAARSQGLSAADLVKVAFAGRGGGSPELAQGGGLPAAEAPGLLRTVENAIAGA | 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.
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 96214
Sequence Length: 892
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Cytoplasm
EC: 6.1.1.7
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O13914 | MTAESEVVNWPANEIRRTFLKYFEDHGHTIVPSSSVIPYDDPTLLFANAGMNQFKPIFLGTVDPSSDFAKLKRACDSQKCIRAGGKHNDLEDVGKDNYHHTMFEMLGNWSFGDYFKKEAIAMAWDLLTNVYGLKKDQLYVTYFGGHEESGLEPDLEARQLWLDIGIDESRVIPGSLKDNFWEMGDQGPCGPCSEIHYDRIGNRTVPELVNMDDPNVLEIWNIVFIQFNREKDGSLRPLPNRHVDTGMGFERLVSVIQNKTSNYDTDVFSPIFAKIQELTNARPYTGKMGDEDVDGIDTAYRVVADHVRTLTFAISDGGVPNNEGRGYVLRRILRRGARYVRKKFGVPIGNFFSRLSLTVVEQMGDFFPELKRKVDDVRELLDEEEESFSRTLDRGEKMFEQYAAAAKKTPSKTLQGNDVWRLYETYGFPVDLTHLMAEEAGIKIDEPGFEAAQARSKEISKQASKGGSSGDDLLVLDVHALGALSKMDDIPETDDVFKHNSVSLKSVIKGIYHKGGFQKSTEGFNSGEQLGLLLDRTNFYAEQGGQEYDTGHIVIDGVADFRVTNVQVYAGYVLHTGFLEYGNLTVNDSVVCEYDEIRRWHLMNNHTVTHILNLALRNTLGDGIDQRGSLVSQEKLRFDFSYKSSIPIDKLLLVENYCNNVIQDNLSVYSKEVALSKAKEINGLRAVFGEVYPDPVRVVCIGVDIDTLLQEPKKPDWTKYSIEFCGGTHCDKSGEIKDFVILEENGIAKGIRRIVAVTSTEANRVSRLANEFDARIAKLEKMPFSPAKEAELKKISVDLSKLVVAAVRKHAMKERIAKITKQVQEHVKAINAAEQKEVVNVVTEYFKENPDMSFVVAKVPISANPKALSFALTYAKKNLKDKSIYLLASDDTKVAHACLVSPEAMKKLTPQEWSQKVCHSIGGRSGGKGDTCQGVGDKPLSIDVAVEEAIEFFQGKLTI | 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-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Sequence Mass (Da): 107377
Sequence Length: 959
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Subcellular Location: Mitochondrion
EC: 6.1.1.7
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Q4VFY6 | MSVSAYFHHRFQQFRSLFKWIVLVVPMAVVVGSLCALFLWSLDKATAARFDHPWLIFLMPVAGFLMVLVYQHFGRGSEGGNNLIVDQIHEPGGGVPLRMAPFILVSTVLTHLVGGSAGREGTAVQLGGSVASAFARVSRLGHGEIRILLMAGIAAGFGAVFGTPIAGAVFALEVLTIGRMQYEALIPSLAAAIAADWTCHAWGIEHIHYHIGYLTGIPASTFHLDALLLAKVGLAGVIFGLAARCFSELSHAASAAFKRFCAYAPLRPVIASAVLIGLVYLLGTRQYLGLGVWSPNPDDATILGFFDPARVDYWSWLWKAVFTIVTLSAGFKGGEVTPLFFIGAALGNALAAIFGAPADLFAALGFVAVFAGATNTPLACMIMGIELFGATHTVYLAVACFLAYICSGHTSIYLSQRLGIAKSASDNIPADTPIRHIREHRVKKRRGNANKAEEV | 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 | MSEMEVEKPDLTLYNTMTQLKEVYKPMNPGKIGIYVCGITAYDYSHIGHARAAVSFDLLYRYLRHLGYQVTYVRNFTDVDDKAKNCGEKPLDLSNRFCEEYLLDMAALQCLLPTHQPRVSDHMEQIIKMIEKIIENGCGYAVGGDVFFSVDKSPSYGQLSGQRLDHTQAGKRVAVDSRKRNPADFALRKAAKSGEPSWESPWGHGRPGWHIEFDIHGGGADLKFPHHENEIAQTCAACEDSGVNYWLHNGHVTNNNVKMGKSLNNFFTIRQIAANYHPLALRHFLMSAQYRSPLNYSVSQLESSSDALYSLSPYREEMSGDVGKTQQSAEAKEMIKKVKNALKFINVSISKLKKMQKKQRMSLVVSLVEVEKAVREVLDVLGLLTTLSYGELLKDMKQKALTRAGMGEEEVLQRIEERNMARKSKDFRRSDRIRELLAFKGIFLEDVPGDTVWRPSTPLTKPKSGLGLGMTAIVFAIVFTFLGFFFYSR | 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 | MEAEKMELKLYNTMTQQKEVLIPITPGKIGLYVCGITAYDFSHIGHARAAVSFDVLYRYLKHLDYDVTFVRNFTDVDDKIIDRANKNGEDPLDLSNRFCDEYLVDMGALQCLPPTHQPRVSEHMDNIIKMIEKIIEKDCGYVVEGDVFFSVDKSPNYGKLSGQLLEHTRAGERVAVDSRKRNPADFALWKAAKPDEPSWESPWGPGRPGWHIECSAMSVHYLSPKFDIHGGGADLKFPHHENEIAQTCAACEDSGVNYWLHNGHVTINNEKMAKSKHNFKTIREITASYHPLALRHFLMSAQYRSPLSFTASQLESSSEALYYVYQTLQDLDEGLSPYQDALSEDGGKSEQTAEGKDIIKKLKTEFESKMLDDLNTAHILTGAYQDALKFINASLSKLKKMQKKQRMSMLVSLVEIEKAAREVLDVLGLLTTLSYAEILKEMKLKTLIRAEIGEEGISQLIEERITARKNKDFAKSDEIREKLTRKGIALMDIGKETVWRPCFPSQADSST | 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 | MSENSSPKLESTSAAAASTKKPFPEWIKPKGKETELLINNSLTGGKVPFVFNESGKGRSLTWYACGPTVYDASHMGHARTYISFDIIRRIMKNYLGFNIQYVMNITDIDDKIIIRANENGISHSDLSKKWETAFFEDMKLLNVLPPDALTRVTEYVPQIVEYVEKIISNGFAYESNGSVYFDTVAFSKAHDYGKLEPNSVGNEKLAAEGEGSLTATSAVSEKRSGFDFALWKKSKPGEPVWNSPWGEGRPGWHIECSAMASDLLGGNIDIHSGGSDLKFPHHDNELAQSEAFYGNRQWINYFVHSGHLLIDGLKMSKSLKNFITIKQALEKYTSRQMRMFFILHKYDKAMNYSPESMGYAIEMEKTFVEFFHTAKQILRDSPLSLPQFWTQAEKDLNKHLQNANDQVHQFILDNFNTSDALKTLSDLVNKTNVYIRSCAEQKTNPRLNLISAIAEYITYIFSVFGLTESSTASSMIGFGSAGKGNIEEEMTPILNALTQFRSEVRASAIAKDTTSILKTCDNLRDEVLPLLGVKIDDKSATTAMWKFEDKETLKKEIEQKKEIEKKKQADKEEKEKKLKEKFEKSKIPPQQLFINETDKYSKFNELGMPTHDKEGVEITKSQLKKLQKEYDNQTKEHNNYLKSLSTSTSSPTLTSTQSPQ | 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 | MSKRGQPAWQAPEAVDRPKLKLFNSLTRQKEDFVPLDGNNVTWYSCGPTVYDASHMGHARSYISFDILRRILSDYFGYNIHYVMNITDIDDKIIRRARQNHLFDEYAAEAQKLPLDELLGQQKEVLQRFQDTCAKNTDPDKKIMLDKTLQRMNDAVEALTKAVGKGDEREISEKRLLYLNEAKDPISDWLDSLKGAQINDNAVFEALPRYWEDQFHNDMKSLNILPPDVLTRVSEYVPQIVTFIQKIIDNGLAYAANNSVYFDVNGFDKREKHHYAKLVPEAYGDTKSLQEGEGDLSIAEDRLSEKRSANDFALWKASKAGEPWWDSPWGKGRPGWHIECSAMASDIFGPTFDIHTGGVDLKFPHHDNELAQSEAAFNESEWVKYFLHTGHLTIAGCKMSKSLKNFVTIQEALKKHSATQLRLAFLLHSWKDTLDYSENTMEMATQYEKFLNEFFLNVKDLTRHVLSEEPRRQFDAWTEVEAALQKKFSNAQVQVHASLCDNIDTRSALDAIRELVSVSNVYIRDNKTRLNSLLLRNVATYITDLLHVFGAISGPRGGIGFPVSGGSGAQAAGADLETTVLPYVQSLAEFRYLVREQAKTLKAFDILKLCDDLRDNVLPNLGVRLEDKDIGKYAVKLVDRDSLLREREAKLAAEAEKAAEKERKKQAAAEAAAAKEAQRRVNPKEMFLAETEKYSAFDENGLPTHDKEGKEVSKGQIKKLQKLQQQQEQRYNEYLASIEKA | 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 | MADSSGQQGKGRRVQPQWSPPAGTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITDIDDKIIKRARQNHLFEQYREKRPEAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQHAVQLATEPLEKAVQSRLTGEEVNSCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVDITGQFEKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATVMPYLQVLSEFREGVRKIAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPTVVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDENGLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ | 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 | MAGSSAEQAADYRSILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPADSRLFHVARWFRHIEALLGGPQGRDEPCRLQASKGRRVQPQWSPPAGTEPCRLRLYNSLTRNKDVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFQYDVFYCMNITDIDDKIIRRARQNYLFEQYREQKPPATQLLKDVRDAMKPFSVKLSETTDPDKRQMLERIQNSVKLATEPLEQAVRSSLSGEEVDSKVQVLLEEAKDLLSDWLDSTGGSEVTDNSIFSKLPKFWEEEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFMNEFFLNVKDILRAPVDITGQFEKWEAEEVELNKNFYGKKTAVHEALCDNIDTRTVMEEMRALVSQCNLYMAARKAERRRPNRALLENIAMYLTHMLKIFGAIEEESPLGFPVGGPGTNLNLESTVMPYLQVLSEFREGVRKIAREKKVLEVLQLSDALRDDILPELGVRFEDHEGLPTVVKLVDRDTLLKEKEGKKRAEEEKRRKKEEAARKKQEQEAAKLAKMKIPPSEMFLSEVNKYSKFDENGLPTHDTEGKELSKGQAKKLKKLFEAQEKLYKEYLQMLQNGSLQ | 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 | MTDSWERGKGRRTQPPWSAPNTQAQPGLRLYNSLTRSKELFVPQDGNKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFKYDVFYCMNITDIDDKIIKRARQRHLFQQYRERNPRPSDLLQDVSAALTPFLQRISEANDPDKRQMLERIHGSVSAALLPLQDAVSSNARAEELERLSQELMEAAVDLLSDWLDEKHGAQITDNSIFSQLPKHWESEYHRDMEALNVLPPDVLTRVSEYVPEIVAFVQRIVDNGYGYVSNGSVYFSTAKFHASEKHYYAKLVPEAVGDQKALQEGEGDLSISADRLSEKQSPNDFALWKASKPGEPSWESPWGKGRPGWHIECSAMAGSILGESMDIHGGGFDLRFPHHDNELAQSEAYFDNDHWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALQKNTARQLRLAFLMHAWKDTLDYSSNTMESAVQYEKFMNEFFLNVKDLLRAPTDVTGQFVKWEVPELELNSCFYSKKAAVHEALCDNIDTRTVMEEMRSLVSQCNSYIASRKAAKQPPNRLLLRSVSSYLTAMLKVFGAIEGEEVIGFPIGGSDNSMNLESTVMPYLQVLSQFREGVRQIARQHKVTEVLQLSDLLRDDVLPELGVRLEDHEGLPTVVKLVDRETLLKEKEEKRKAEEEKQRKKEEAARKKQQQEAAKLEKMKVSPSQMFQLETDKYSQFDESGFPTHDTEGKELSKGQSKKLRKLYEAQEKLHKEYLQMAQNGTTG | 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
|
Q9PPB8 | MRLLDSVTKEKIKLDKKDISIYLCGPTVYDDAHLGHARSSVCFDLLRRVLLAQGNRVKFARNYTDIDDKILKKMAQSGQTLEEITEFYIKSYEEDMRVLNVLDPDFKPRATHYITAMLDLIKKLAKDGFVYTLEDGIYFDTSKDEKYLSLSNRNLEENISRLSNEVQKRNESDFVLWKFDENFYESEFGKGRPGWHTECVAMIDSIFENTLDIHAGGIDLLFPHHENEAAQCRCGCKRKLANIWLHNGFVKIDGEKMSKSLNNSFFIKDALKEFMGEALRFYLLSSHYRSHFNYSLSDLENAKKRLDKFYRLKKRLDLGEISDFDVLNDIGIKSEIAKQILEILNDDLNVSKALALLDDFISSANLELDKESKNKILKQNIKEALSELAKIFGFGFMDATLYFQWGVSKEEREEIEKLILERTEAKKNKDFNTADAIREQLNSKKITLLDTPNGTIWEKINA | 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
|
Q9AAY2 | MTLKIHDTLTREKRDFVPADPQRVTMYVCGPTVYNYAHIGNFRPVVVFDVLFRVLRHLYGEDAVVYARNVTDVDDKINQKAADEGVPISVITDRYLAAYHQDADALGALRPTLEPKATEHIGAILEMIGQLVENGSAYAAEGHVLFDTQSFADYGQLSGRPLDEMIAGARVEVAPYKRHPADFVLWKPSKENEPEWESPWGAGRPGWHIECSAMIDKALGQTIDIHAGGIDLTFPHHENEVAQSRCAHKTSVLANYWMHNGFLDMSGEKMSKSLGNVIIPHELLETTPGEVIRWALLSAHYRQPLDWTPELLEQSKKSLDRLYGALRRAKDVAPDQAMEAPAEVMSALMDDLNTPLATSAFFEVSSAIEKAVTAGDTVAIAANKARLLEAGALLGFLQADPDAWFEGDASDELKAQVEDLLAKRVAARAAKDWSAADAIRGELDALGVVVMDGPAGATWRMKD | 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
|
B9KRV8 | MTEIRLTNTKSRRKEAFEPIDRKNVRLYVCGPTVYDRAHLGNGRPVVVFDVLFRLLRHVYGEGHVTYVRNFTDVDDKINAAALARKDAGDPRSLEALIRERTDETIRWYHEDMDALGALRPTQEPRATEWIGAMIAMIEDLIAKGHAYEREGHVLFRVRSYRDYGALSGRSVDDMIAGARVEVAPFKEDPMDFVLWKPSDDELPGWDSPWGRGRPGWHIECSAMADGLLMKDLPENERSFDIHAGGIDLQFPHHENEIAQSRCAHPEGEFAKVWMHNEMLLVDGKKMSKSLGNFFTVRELIEEYRKQFAVNNIGPAIRLRFLQGHYRAPIDAARHYIEQASVKLGLWWHFISEHLDAPITDKDRRDILATSPVIEALADDLNTPLAVTYIDGLVSRLRGGIQKQGYVDAEMDDLEMVAKRARVAIEFLGFTFDDLEEHHGPVQLKRLKERQLSASADVGVRIGRLLEERAEARKARDFARSDAIRDRLQAAGVLIKDSRDGATWELEPGFDPAKLGEPE | 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
|
Q11JR3 | MSDGFKALKLYNTLTRRDEEFVPLDPANVRMYVCGPTVYDFAHIGNARPVIVFDVLFRLLRQLYGDDHVTYVRNITDVDDKINARALRDFGEDITAGRLTLNEAIRRVTERTAAQFHADVAALGCLAPTHEPRATEFVLPRTDGKADMASLIQTLIDRGHAYAAKGEILFDTASMPDYGQLSKRRLEDQQAGARVAVDPHKRNPSDFVLWKESSAEEPGWEGRFTFEGKPLVIRGRPGWHIECSAMSAAYLGEVFDIHGGGLDLIFPHHENEIAQSRCAHGTPVMANYWLHNGFVQVEGKKMAKSEGNFVTIHDLLATENFGGRKWPGEVLRLAILMTHYREPLDFSLRKLEEAEAVLDGWYRVVGDAKHQEGDSGAVRRALLDDLGTPAAITVLHDLRAQAARGSEAAKADLKANAVLLGLLTQSQDQWFSGKAADAAIDEAAVEERVAARLSLLRAKNFPEADRIREELSGRGIQLMDYKDPETGERRTKWEVKR | 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
|
Q1MQR5 | MHLYNTMEKKKEPLIPIISGKLGIYVCGITAYDFSHIGHARSAIVFDILVRLLRYQGYDVTFIRNFTDIDDKIINRANKEGRSSKEVAEEFINAFHEDMDRLGVLNADIEPKATDYIPEMIECCQKLLEADKAYITASGDVYFRVRSFPDYGKLSGRTPDELRIGVRIVPSEEKEDPLDFVLWKAAKPGEPSWESPWGRGRPGWHIECSAMSEKCWPLPLDIHGGGIDLIFPHHENEIAQTESIVNKPLAKIWMHNGLVQVNSEKMSKSLGNFKIVRDILEAYLPETLRFFLLKKHYRSPIDFSFEGMNETERSQKRVYECIAEVDKALERKSWDSGGSSSSILAELDEQFSLFMSALEDDCNTAAGLGHLFNIIHIVRRALDDKALYSTTDGKVVFEQFREIIRKVDILLGVFGQKPNSFLQDLKTIRIIRNKIDVNQVEELLSKRRQAREEKNFVQADEVRNTLASLGIEIRDTSEGQVWDIL | 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
|
Q8F525 | MIEIQFYNSLSGRKEKFSPSDPNRVTVYSCGPTVYNFAHIGNLRAFLFVDVLRRSLKLLGYGVDMTMNITDIDDKIIRDSIASKKSIIEFTAPWTKAFFEDLKTVSAEILEHYPKATDSIPEMVDIIQKLQKKGLVYKKDESLYFSIQKFQNYGKLSKIDTSGMKTGTRYDTDEYEKEDVRDFVLWKSPKLEGETSWDTLVGTGRPGWHLECSAMIRKVYGSGVDIHTGGVDLLFPHHENEIAQSEGAFPEESFVKTWLHSEHLLVDGQKMSKSKGNFYTLRDLIQQGLDPKAIRFLLISTHYRSKLNFSTDRIAEASANIRKIQNCLDRILELEPDIKADFYFLFSIPFVQTWKKEFEESLADDLNISKALAVVFESVKQINSLLDTNQSDSKQRIEYIQILAYFDRILGVLNFESKKDLLDSEIDSLIEERQIARKNKDFARSDAIRDQLLAQGILIEDTKEGIRWRKK | 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
|
Q1WSS5 | MLQLYNTLTNQKEKFEPLNPGKVTMYVCGPTVYNYIHIGNARSAVAFDTIRRYLEYRGFEVNYVSNFTDVDDKIIKASQEMNLSVKEITEKFINAFYEDTSALNVKKATLNPRVMDNMDDIIKFIEVLVQKGYAYESAGDVYYKTRKFKDYGKLSGQLIDDLEQGASSRVDDIDQDKKQDPLDFALWKKVKQGEISWNSPWGQGRPGWHIECSVMSTKYLGDTIDIHAGGQDLEFPHHENEIAQSEAKTGKKFARYWLHNGFVTIGEEDQKMSKSLGNFVTVHDLLKKVNPQVIRFFMSTTQYRRPIRYSSANLNEAKVNLNKLQTAYENLSYRLKDSVEGNDKEVEVNFANLEKDFVKVMDDDFNVQNGISVVYEMAKQLNVYSEKEKVYTDTINNLINTYKKVVEIFGISFSEEKELLDDTIEQLIQERNEARKNKNFKRSDEIRDLLKEQGIILEDTAQGTRWKRND | 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
|
Q1AU11 | MSVKVRDSLSGGLVEVGGDGRVGIYVCGPTVYNHIHIGNVRGHLFWDVAVRFLRSRGYRVKFVWNITDIDDKIINRANEEGVSWKEIVRRYTDSFHERLRLLGIGMPDVEPRATEHIPEMISLIEELIRRGHAYPAPNGDVYYAVETFPRYGALSKQRPEEMKITEKGQTGHKRNPLDFTLWKASKPGEPSWESPWGPGRPGWHIECSAMVEKHLPGGADIHGGGSDIRFPHHENELAQSCGAHPDRPFVRAWAHHGMVRMAAQKMAKSVGNVVDAREATLKHGRDAIRMWLLQSHYSQPIDYSDEILEEKRRSCERLLRLYREISRSEASSPLSDRLAGELRERFDAAMREDFNTPEAIAALFDAASGAGREISSRPSAAGEFASLKEALQELLGLLGFDVAGERVSEVDGVRIRHAGEAPGEVLERVARRERARRRREWPEADRLREELLREGWAIEDTAAGPVLSRR | 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
|
A4F6W7 | MSLHLHDTATRTMREFHPRLAGVASIYVCGATVQGVPHIGHVRGGLNYDVLRRWLVHNGYDVRLVRNVTDIDDKILTKAADAGRPWWEWATAHERAFESAFDRLGCLPPSALPRATGHITQMIELMQRLIDKGHAYAAGGDVYFSVASYAEHYGRLSGQRLDEVQQGESTASGKRDPRDFTLWKAAKPGEPSWPTPWGDGRPGWHLECSAMSTYYLGSEFDIHGGGLDLVFPHHENELAQSTAAGDGFARYWMHNAWVTMSGEKMSKSLGNTVAIPAILQRAAAPEIRYYLVAPHYRSTIEYSEPALAEAISAYRRIDSFVNRVRQRTGEVGHGTVPAEFAAAMDDDLSTPQAIAVVHNAIRESNAALDRGDDRAANEAAASVRTMTDILGLDPLSEQWADTRGADDAAHHALSELVGSMLQQRQQARAERDFATADAVRDRLQACGIAVEDTPDGPLWTLKDG | 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
|
Q97WE6 | MDFRIRVYNSLGRKLEEFGTVEPNLVKMYVCGPTVYDYVHIGHGRTFVVFDAISRYLRLRGYTVIRVQNITDIDDKIIKKSQEIGKDWNEIVDYFTKDYLDMLSQLKVKIDIHPRVTQHIREIIDFVQRLIDKGHAYVAPSGSVYFDVDTYPNYGELSNTKKEEWNQGEEFVKEKKHSYDFALWKAWKPGEPYWESPWGKGRPGWHIECSTMSTRYLGERFDIHGGGADLIFPHHENERAQTEALIGEKWVTYWVHSAFVTIRKEKMSKSLGNIIPLNEAIKKWGPSVLRYWYLTSHYRSPIDFSEEALEQAKSALQRIKDSMAIIRDVISEGPKFYVKDDDIKVYREILNNLNNFHTAMSNDFDTSTALSYIHEIVRLVFSTLQYSRDFLGAMLAFETLKQFNEVFGVMDEEFYPTYDKMYKIIDAVVDIRNQLRQMKLYEISDKIREELLKAGVRILDSKDKSTWRFE | 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 | MSLLLRTLPLRPTRFLSATAISISNATNFFVVPKRTNPLPGTRRTFSSSPVAAASGDVVVKPVPSPPSVLRWVSRTELCGELSVNDVGKRVHLCGWVALHRVHGGLTFLNLRDHTGIVQVRTLPDEFPEAHGLINDMRLEYVVLVEGTVRSRPNESVNKKMKTGFVEVVAEHVEILNPVRTKLPFLVTTADENKDLIKEEIRLRFRCLDLRRQQMKNNIVLRHNVVKLIRRYLEDRHGFIEIETPILSRSTPEGARDYLVPSRIQSGTFYALPQSPQLFKQMLMVSGFDKYYQIARCFRDEDLRADRQPEFTQLDMEMAFMPMEDMLKLNEDLIRKVFSEIKGIQLPDPFPRLTYADAMDRYGSDRPDTRFDLELKDVSNVFTESSFRVFTEALESGGIIKVLCVPLGAKKYSNSALKKGDIYNEAMKSGAKGLPFLKVLDNGEIEGIAALVSSLDSAGKINFVKQCGAAPGDLILFGVGPVTSVNKTLDRLRLFVAHDMDLIDHSKHSILWVTDFPMFEWNEPEQRLEALHHPFTAPKPEDMDDLPSARALAYDMVYNGVEIGGGSLRIYKRDVQEKVLEIIGISPEEAESKFGYLLEALDMGAPPHGGIAYGLDRMVMMLGGASSIRDVIAFPKTTTAQCALTRTPSEVDPKQLQDLSIRTK | 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 Mass (Da): 74517
Sequence Length: 664
Subcellular Location: Plastid
EC: 6.1.1.12
|
Q55C99 | MNRVILKDSKIFLNVLNKPIIKNKNCLSLLNITTSSTTSIIKNQQINQFNKRNFTNTINNNKNENINNKILNIIERSHSCGEITSKDIGKEVIIYGWINSLRNLGDNVFLVIRDGHGKVQCYVDLKQQCILKSSVPNIDINERNSIEENIKLFKLESIVSIKGKVIARPERMVNKNMSTGEIEISVDQLQLLNNCVDLPFTVEHDSTAVSEELRLKYRYVDLRRDKVQSNIRLRSKVAMAARNYLINQQFIEVETPTLFRPTPEGAREYLVPTRHQGQFYSLPQSPQQYKQLLMVGGIDRYFQLARCYRDEDLRSDRQPEFTQIDMELSFVNTQMIYRIIEGLVKTLWKEAGFNIDYEFPFYTYEQVLSTYGIDKPDTRYDMKLVDITDCFNKDETNINLFKNALSQASNNFKESKPVIKCIKLDQVLPTLKSKHLDQITTESNSIITVQIKSNNEWKSLISKSISEQEKTLITERMNLKEGDVLLISVGPRFQVESTLGKTRIYCANLLKELNLLKLDPQQFNFLWVVDFPLFTPSDYMNEQSALLSTHHPFTAPHPEDIDLLLNPLSTPSDYSKIRGQHYDIVINGVELGGGSIRIHNSDVQLRVLEKVLKLEPHMVQRFNHLLTALSMGCPPHGGIALGFDRLCSLLVNSNSIRDVIAFPKTSGGKELMTSSPATVTKSELDELFLIQK | 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 | MYFPSWLSQLYRGLSRPIRRTTQPIWGSLYRSLLQSSQRRIPEFSSFVVRTNTCGELRSSHLGQEVTLCGWIQYRRQNTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKDPVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDALSKPHGTVKAICIPEGAKYLKRKDIESIRNFAADHFNQEILPVFLNANRNWNSPVANFIMESQRLELIRLMETQEEDVVLLTAGEHNKACSLLGKLRLECADLLETRGVVLRDPTLFSFLWVVDFPLFLPKEENPRELESAHHPFTAPHPSDIHLLYTEPKKARSQHYDLVLNGNEIGGGSIRIHNAELQRYILATLLKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKPTDSKAERAH | 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 | MVLSRLPACLLPLVGTKVSIQGWLVATSRQVSKSISFHQLRDTHGTILQLLSTDKIILQQKREPLVSSTDFSQQKSTSVMRTLSSIPPESVVQVTGKLQRRPEHDRRPGNEFELHVEDVKLLNVAKNLQLFPGDEKPGMRIQLANRHIQLRAPKYNSYLRQRSRLAYQVHSFFNDREFCEVETPLLFKSTPEGAREFVVPSRLNPGKFYALPQSPQQYKQILMASGIGNYYQIARCFRDEDLRFDRQPEFTQIDLEMSFVDKPHEIMEVVEDLLVRLVSFAKGITLAKPFQHITYQHAIDKYGSDKPDIRFELPLKNITSLLPKQDPLISTEILVYNDLSHSLSNAESRKLCEAVGENVVVTSIREHSQLQTWVKKLPQLRQLPIVAEELNQKLQIGINSIVFMTNRPKYLVSGTTPLGKLRLLLHELLVKKKALPELDKDLLKFVWVVDFPLFSPTEEKNQSITSTHHPFTAPHWDDVHLLEKKPLSVRGLHYDIVVNGIELGGGSIRIHNPDIQRFVLKDVLKLPENRYATFEHLIRVLSSGCPPHGGIALGFDRLAALLTNAPGIREVIAFPKTSSGADLLIGSPSAIPEEMLKDYNVAITRQTQNRN | 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 | MLARSRVCLQTITRRLADFPEANAIKKKFLFRKDTSTIKQLKGLSSGQKIVLNGWIEQKPKRVGKNLIFGLLRDSNGDIIQLVDNKSLLKGFTLEDVVQAVGILSLKRKLSNEDADEYEVQLEDITVLNASNKKPAQMQDFKLSAIYPPEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGAREFLVPTRTKRSDGKPSFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSGVWSKFSKKRGLLTLDSKGTLVPAKKENGTVSIFRMTYEQAMTSYGIDKPDLRAPDLKIINLGEFNAFSHLNKKFPVFEVIILRSAFSNMEEYKERWSFLTNNSNYNYRVPIVLPIENDEQANSNWFENFHAIATFENPHLITKFLKLKKGDIVCGCTREPNHSIFENPTPLGRLRQLVLQSEHGKNIYHAVNKDVASWIVDFPLFSPVIIEDKSGKKEKLAYPEYEKDRLCSTHHPFTMVKLKDYEKLEKTPEKCLGRHYDLVVNGVELGGGSTRIHDPRLQDYIFEDILKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKSITGADLVVKSPSVIPESILEPYNIKYSNSKK | 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 | MPNRGAHFSISRRKDFLMDFSERVFCGHLTPDHTGRRVLLAGWVDAFRDHGGLLFIHLRDRNGIIQIVFSPEAASADVYRQAASLRAEYCVAVQGEVRKRLPGTENPHIETGDIEVFVSELTVLSESEALPFAISDKAMVAGASSAGADHVNEDLRMQYRYLDIRRPAMQKNLILRHRISQCVREFLDSRGFVEVETPVLTMSTPEGARDYLVPSRIHPRSFYALPQSPQLFKQLLMIGGMERYFQLARCFRDEDLRPNRQPEFTQLDIEASFIDEEFLYELIEELTVRMFAIGGIALSRPFPRMTYAEAMDTTGSDRPDLRFGLRMADVTGVFSRTSYSIFKQILQRGGSIKGINIKGQSEKLSKNVLQNEYAKEIAPSFGAKGMTWMRAEEGKLESNIVQFFSADELEALKRVFQVEDGDVLIMVADPSCAIVNSALGQLRLHLGNRLGLIPEGVFYPVWITEFPLFEPTDEGGVTSSHHPFTAPDRTDFDPGNIEELLSLRSRAYDLVVNGEELGGGSIRINDREVQRRIFAALGLTEEDVKNKFGFFLRAFDFAAPPHGGLALGMDRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVKREQLAELGLLNLGDKDVLPGDAEKEDRIDHLSWVSRIGIAEGERPVMESILAQAEELAAQVGDLAGNEEPVRSVAPVANRVREGLEAVRLSFSGTGRLLKNAPAVKGDYFKVAGILD | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 80508
Sequence Length: 723
Subcellular Location: Cytoplasm
EC: 6.1.1.23
|
Q6FEH6 | MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKVRSEFVLKITGRVRRRYEGTENSNMVSGQIEVLGKEIEVLAQSETPPFPLNDDNINISEEHRLKYRFLDIRRPEMLDRLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFDELLGIKFDKFQRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQDVEFKVFAGPAKDPKGRIAALRVPGAGALPRSAIDEYTKFVGIYGAKGLAYIKVNEIEKGVEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKVVNDAMGALRVKIGHDLKLVTCEWAPLWVVDFPMFEETDDGKWTSVHHPFTLPKSSVEDVKANPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLIMLMTGASSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQPKKED | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 66646
Sequence Length: 592
Subcellular Location: Cytoplasm
EC: 6.1.1.23
|
Q5NIQ4 | MRTHYSSDINEKLQGQKVTVCGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPDNDNFKVADSLRSEFVIKAEGVVNLRPEGQENKNISSGKVEIIGDSIEVINKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQHKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMERMIAGLFKETIGVEFATPFQVMTFADAIDKYGSDKPDLRIPLEFVNIKEDMQNEEFKVFSGPANDPQSRVIALRIPGGNDKLTRKMIDEYTKFVGIYGAKGLAYIKINSLSQGKEGLQSPIVKNISEETLFKVIDKTSAKEGDLLFFGAGKAKIVNDSMGALRAKIGEDLDLFNKDWAPLWVVDFPMFEKDDNRLYAMHHPFTAPKVSSVEDLVNTNPEELSSRAYDMVINGYEVGGGSIRIHKQDIQAKVFNLLGISDDEAREKFGFMLDALSYGTPIHGGIAFGIDRLIMLLTGTTNIRDVIAFPKTQTASCLMTEAPSTVSLEQLNELGIAVKKEER | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 66727
Sequence Length: 590
Subcellular Location: Cytoplasm
EC: 6.1.1.23
|
Q74D56 | MTDMLGDWKRSHLCGTLTKADVGKQVTLMGWVMRRRDHGGLIFIDLRDREGLAQIVFDPAKAPEAHREAEAVRNEYVVAIKGEVVPRPEGTVNPNMKTGEVEILVTQCKLLNRSKALPFTLDDYVDVAENLRLKHRYLDLRRTPLQQNLILRSRVSQVTRQYLTENGFLEIETPFLTKSTPEGARDFLVPSRINQGNFYALPQSPQIFKQILMISGFDRYFQVVRCFRDEDLRADRQPEFTQIDCELSFVDRDDVIAVMEGLIARIFKEAKEIDVQLPIPRMTYAEAIRRYGVDNPDVRFGLELVELTDIVKGSGFKVFADVAAGGGIIKGLNAKGCARFSRKEIDDLTEFVKIYGAKGLAYVKIEGGEWHSPIAKFFTAQEIADMNRAFGAEEGDLLLFVADKPKVVNDSLGKLRNQLAQILGLVDKGTFKFVWITDFPLLEWDEEEKRWAAVHHPFTAPMDEDLDKVESDPGACRAKAYDLVLNGNEIGGGSIRIHQQHIQSLMFRMLGLSEEEARAKFGFLLDALEFGTPPHGGIAFGMDRLIMLLTGSDSIRDVIAFPKTQKGACLMSDAPSPVDSKQLRELAIKVTVKQ | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 66825
Sequence Length: 594
Subcellular Location: Cytoplasm
EC: 6.1.1.23
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Q7NJA4 | MRSDYCGTLRSEHIGKTVSLYGWIDGWRDHGGVIFLDLRDYTGIVQIVADPQRTPESYHLASSLRNEYVVRVEGRVSARPEHSLNPRLSTGTVEVYADTLAVLNRAETPPFAISKDEEVDEKLRLKFRYLDLRRGRMQKLLRLRHRVMQIMRRHLDERGFTEIETPVLVKSTPEGARDYLVPSRVNPGDWFALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSMEEIIALNEGLVAAILQETMGLELSLPLPRLTYAEAMVRYGSDKPDTRFGLELVEVSEVFRESSFQVLSGAVAAGGKVVCLPVPGAEGITNTRVKPGGDLFEFVTQFGARGLLFARVREGGQVDTIGAFSKSLTPEIAAGMIEKTGAQPGHLLLFGAGDRTAVPTVLDYMGRLRLKMGEELGLIDPNRHNLLWVTDFPMFEWNAEEKRLEALHHPFTAPRPEDEHDLKTARALAYDIIWNGVEVGGGSLRIYRRALQERVFETIGLTEEEARAKFGFLLDAFEYGTPPHGGIAYGFDRFVMLIAGEQSIREVIAFPKTQRAQDLMLGAPSAVAERQLKELNVRSTLPPKTQG | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 66973
Sequence Length: 595
Subcellular Location: Cytoplasm
EC: 6.1.1.23
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Q2SCK8 | MRSHYCGEVNESLVDQEVTLCGWVHRRRDHGGVIFLDLRDRDGIAQVVYDPDTNEVFQLAEQIRDEFVVKVTGRVRLRPEGKANTDMSTGMVEVLGKQLEILSTAKTPPFQLDEFVQVGEDVRLRYRYMDLRRPEMLNKLRFRSKVTSYIRNFLDGNGFMDVETPILTRATPEGARDYLVPSRTHEGSFFALPQSPQLFKQLLMMSGVDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFLNENEIMSITERLVRDMFRDLLEVELPEFPRMPFSEAMNRYGSDKPDLRIPLELVDVGDLLTNVSFNVFSGPANDPKSRVAALRLPKGGELLSRKQIDDYTKFVGIYGAKGLPYIKVNEKAKGLDGLQSPIVKHIADAIDPLLERVGAEDGDIIFFGTDKTRVVNEALGALRVKLGHDLNLLEKQWAPLWVVDFPMFEEDGEGGWTAIHHPFTAPSCAVEMLESDPENALSRAYDMVLNGTELGGGSVRIHDSDMQETVLRILGIGQDEAREKFGFLLDALKFGCPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAMCMMTQAPGKVDPKQLRELNIRLRKTEQPE | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 66738
Sequence Length: 590
Subcellular Location: Cytoplasm
EC: 6.1.1.23
|
Q8DSG3 | MKELFIGNYGLEQVGQKVTAKGWVANIRNHGKLAFIELRDREGLLQVFVDSAVADFDKLHDLHKESILAVTGEIVARDERFVNPHIKSGQVELRAETIEIIASSKLLPFELDNHAHAGEDIRQKYRYLDLRREKMTANLKLRHQVTKAIRDYLNQADFIDVETPYLTKSTPEGARDFLVPSRVFKNQFYALPQSPQMLKQLLMGAGLERYYQIVRCFRDEDLRGDRQPEFTQVDLEMSFVSEEDVRNLVEGMLKAVVKASKGIELTEAFPIISYAQAMRRFGSDKPDTRFAMELKDLTELSRGNTSLFLQKGLKKENGVVMGICAKNAAKAFTNRQMATLKQLVMDFGVAGFATATIEKGQVTGSLKSTFKDHNTELLELFEAEDGDMIFFVTGSLKRVQEALGGLRVRLAKDLELIDNDKLNFLWVVDWPLLEWNEDLNRYQAMHHPFTQGAFEDGSDWKENPEKMMSRAYDIVLNGYEIGGGSLRIHKRSAQEAMFELLGMKKEDYERDFGFFLEALEYGFPPHGGLALGLDRLVMILAEEGNIREVIAFPKNGQGADAMLESPSLVADQQLAELRLALRD | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 66163
Sequence Length: 583
Subcellular Location: Cytoplasm
EC: 6.1.1.23
|
Q31NM6 | MRTHYCGELRAEQVGTSVTLYGWVDRRRDHGGVIFVDLRDRTGTVQIVSDPERTPESYHQAEGLRNEYVVKITGRVSGRPAESLNPKLPTGEVEIYADRIEILNAVRRQLPFQVSSADEETVREDLRLRYRYLDLRRDRMNRNLQLRHQVVKAIRRFLEDEEQFIEIETPVLTKSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSQEEIIDLNERLIAHIFKTVKGIELPRPFPRLTYAEAMDRYGSDRPDTRFGLELVDVSDVVADMGFKVFSGAVKSGGKVKILPIPDGNDRISNVRIKPGGDIFKEATEAGAAGLAYIRVRENGEIDTIGAIKDNLSDEQKAEILRRTQAQPGTLLLFGAGSTDIVNKSLDRVRQFLGKELGLIDPEALNLLWVVDFPMVEWNADEKRYEALHHPFTAPNPQDLEDLTTARAQAYDIVLNGLEIGGGSLRIYQRDIQERVFETIGLSHEEAQAKFGFLLEAFDFGTPPHGGIAYGLDRLVMLLTGEESIRDAIAFPKTQQARCLLTEAPADVSDRQLKELYVASTWQPPIKERD | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 68095
Sequence Length: 599
Subcellular Location: Cytoplasm
EC: 6.1.1.23
|
Q0AYS1 | MKRTHNATELDIHLVGREVMLNGWVDTRRDHGGLIFVDLRDRSGIIQLVFSPEVKEEAFHLAEQIRSEYVIAVRGKLSLRPEATENPNLKTGKVEVYVEDIEVLSPAKTPPFYIENDIDVDENLRLKYRYLDLRRPEMRDNLLLRHRVVKCMRDFLDSRGFIEIETPILTKSTPEGARDYLVPSRVHPGEFYALPQSPQIFKQILMVAGMEKYFQIARCFRDEDLRADRQPEFTQLDMEMSFVDEEDIIVLVEEMMAEIFFKAAGKVIRTPFPRLAYDDAMINYGSDKPDLRFGLEIVELSEMLQNTQFKVFASALQSGGVVRALNAKGCGSFTRREIDALGAMAVENGAKGMAWILVQENELRSPITKFLSEEEIEQILMTTGAEAGDLILFGADQAEIVARVMGILRLELGRKKGLIAEEELNFVWVTDFPLLEYDEEEKRYQAKHHPFTSPRLEDIEIMDSEPGRVKARAYDLVLNGTELGGGSIRIHRREWQEKMFSVLGMSQEEARDKFGFMLEAFEYGTPPHGGIAFGVDRLLMLLAGRNSVRDVMAFPKTQSASCPMTEAPSTVSARQLRELALRIREK | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 66867
Sequence Length: 586
Subcellular Location: Cytoplasm
EC: 6.1.1.23
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P73851 | MRTHYCGDLRTTHLGETVTLYGWVDRRRDHGGVIFLDLRDRQGIVQIASSPDQTPASYPVAEGLRNEYVVQVTGVVSKRPPESLNEKIPTGEIEIYADSIILLNGVNQQLPFVVSSHEAEQVREDVRLKYRYLDLRRARLSQNLQLRHQVVKAMRRFLEDQENFLEIETPILTRSTPEGARDYLVPSRVNPGEWYALPQSPQLFKQLLMVAGMDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMGQEEILDLNEALICHIFKVVKNIDLPRPFPRLTYQESMAKYGNDRPDTRFGLELVDVSDLLGNTGFKVFSAAVSSGGSIKAIRVPGGNETISNVRIKPGGDLFKEATEAGAKGIAYIRVRDNGEIDTIGAIKENLDEAQVKTLLQLTQAEAGDLLLFGAGDTATVDKSLSRLRLVLGEQLGLIDPDAINLLWITDFPMFEWNSDEKRFEALHHPFTAPHPDDLGDLKTARAQAYDLVMNGVEIGGGSLRIYQREVQEKVFATIGLSPEEAHEKFGFLLDAFEYGTPPHGGIAYGLDRLVMLLAKEDSIRDVIAFPKTQQASCLLTEAPAAVDKKQLKELSVASTYVPKVKVDD | 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-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
Sequence Mass (Da): 67209
Sequence Length: 599
Subcellular Location: Cytoplasm
EC: 6.1.1.23
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A6GWB6 | MYRSHNCGELNATHINKEVTLAGWVQKSRDKGFMNWVDLRDRYGITQLMFDESRSDKTVFELAKTLGREFVIQVKGTVIEREAKNKNISTGEIEILVTQMTILNSSLTPPFTIEDETDGGEDIRMKYRYLDIRRNPVKNSLLFRHKVAMEVRKYLSDLDFCEVETPYLIKSTPEGARDFVVPSRMNEGQFYALPQSPQTFKQLLMVGGMDKYFQIVKCFRDEDLRADRQPEFTQIDCEMAFVEQEDILNIFEGLTRHLLKELKGIEVEKFPRMTYNHAMKTYGNDKPDIRFGMEFGELNEYAKHKDFPVFNAAELVVAIAVPGVGEYSRKEIDALIEWVKRPQVGASGMVYVKCNEDGTYKSSVDKFYDQGDLSHWAKTTGAKAGDMIFVLSGPADKTRAQLSALRMELATRLGLRNPAEFAPLWVVDFPLLEFDEESGRYHAMHHPFTSPKPEDMHLLETDPKSVRANAYDMVLNGNEIGGGSIRIHDKNTQALMFKYLGFTEEEAKNQFGFLMDAFQFGAPPHGGLAFGLDRLVAILGGQETIRDFIAFPKNNSGRDVMIDAPSIIDDSQLKELHIQLDLK | 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
Sequence Length: 583
Subcellular Location: Cytoplasm
EC: 6.1.1.12
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Q8RGJ4 | MVYRTHNLGELRLKNIGEVVTLSGWVDTKRNVSTNLTFIDLRDREGKTQIVFNNELLSEKVLEEVQKLKSESVIRVIGEVKERSNKNPNIPTGEIEVFAKEIEILNACDTLPFQISGVDDNLSENMRLTYRYLDIRRNKMLNNLKMRHRMIMSIRNYMDNAGFLDVDTPVLTKSTPEGARDFLVPSRTNPGTFYALPQSPQLFKQLLMIGGVEKYFQIAKCFRDEDLRADRQPEFTQLDIEMSFVEKEDVMNEIEGLAKYVFKNVTGEEANYIFQRMPYAEAMDRFGSDKPDLRFGVELKDLSDIINNSSFNAFSSTVQNGGLVKAVVAPNANEKFSRKVISEYEEYVKTYFGAKGLAYIKLTADGIASPIAKFLSEEEMKAIIEKTEAKTGDVIFIVADKKKVVHSALGALRLRIGKDLELINKDDFKFLWVVDFPMFDYDEEEQRYKAEHHPFTSIKAEDLDKFLAGQTEDIRTNTYDLVLNGSEIGGGSIRIFNPQIQSMVFDRLGLSQEEAKAKFGFFLDAFKYGAPPHGGLAFGIDRWLMVMLKEESIRDVIPFPKTNKGQCLMTEAPNTVDEKQLEELFIKSTYEK | 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
Sequence Length: 592
Subcellular Location: Cytoplasm
EC: 6.1.1.12
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Q9PCC5 | MRTHFCGLIDETLIGHTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVDSRAIDQNNSELFKVASGLSYEDVLQVEGVVCARHAVNDKIKTGKVEVIATKIKILNKAAPLPFHAHENPGEDIRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDMHGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVSERDVQDFVEEMIRRVFKEVAGIELDTTFPRMTWTEAMRRFGSDKPDLRINLELIDVAALVADSTFTPFTDAVAHPNGRVAALRIPSGAVLSRKQIDEYAAYTAKYGATGLAYAKLAPIGEITSPIAKFFSEDAFAALLSHIGAEKGDIVFFGAGNYNKVSDFMGALRLKAGKDFALITADWRPLWVTDFPMFEWDEEAQRYVALHHPFTAPAAIDDIDELRAHARTALSRGYDMVLNGNEIGGGSIRIHRPEMQRAVFELLGITEDEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALIAGTESIRDVIPFPKTTGAQCLMTDAPSSISEEQLSEIHVITKKPTP | 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
Sequence Length: 589
Subcellular Location: Cytoplasm
EC: 6.1.1.12
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A5FZX8 | MTIRVRFAPSPTGMLHIGGARTALFNYLFARHHGGQFLLRVEDTDRERSTPEATKVILDALDWLDLKPDEPPVYQSTRYARHREVAEQMLAAGQAYRCYCSREELAEMRAEAERSKKPFRYDGRWRDRDPAEAPAGVDPVIRLRAPREGETVIHDLVQGEVRVKNAELDDMILLRSDGTPTYLHAVVVDDHDMGITHVIRGDDHLTNTFRQAQIYDAMGWARPNFAHIPLIHGADGAKLSKRHGAVSVLQFRDEGYLPEALCNYLLRLGWGHGDAEILPREEQVALFDLDGVGRAASRMDYAKLLHVNAVFLRAAEDERLAADVVARLERDHGFPVSTEAAGRIAMLMPGLKDRARTLAELAESALFVVREAPLPMTEKAEALLTEAARDDLAALLLDFDKTDFSKAALHEAMKAYAEREEKKLGAIAQPLRAALTGSTVSPPIDAVMEALGPIEVRKRIFSVLGE | 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 Length: 466
Subcellular Location: Cytoplasm
EC: 6.1.1.17
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A8EQW9 | MAITRFAPSPTGYLHIGGLRTSLYSYLWARKTGGEFRLRIEDTDLARNSEEAMKAIIDAFDWVGLNYDGEVFYQSKRTDIYKQYIDKLLESGNAYKCYMSKEELDALRAAQEAAKQTPRYDGTWRPEPGKELPPVPAGVEPVIRIKAPTTGTIEFDDGVKGHMKFDANQVDDYVIARSNGMPTYNFVVAIDDALMGMTDVIRGDDHLSNTPKQIVVYNALGFKVPKFYHVPMINNPEGKKLSKRDGAMDVMDYKRLGYLPEALLNFLVRLGWSNGDQEIFSMKEMLELFDPSNINKSASSYNGEKLLWLNSEYIKAVSNERLIEELKFFDLDLSNYPKKNEILDLAKQRAQTLVELKKSITDIIDIPTSYEESGVKKFIKEDTKELLEKYLLLLESNKNSLDSVEKIEEFTKPFINDNGLKFPQLFQPIRIALTGGTQAPSVYDIIFILGYDEIFKRINEALKRNFQNT | 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 Length: 469
Subcellular Location: Cytoplasm
EC: 6.1.1.17
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Q2GLP6 | MITRFAPSPTGYMHVGNARTALICWLYARSKSGKFLLRIDDTDASRSEHKYIEGIKQDLDWLALDWDSCFQQSTRLERYQEVFDLLLDQGVIYPCYETQEELDMKRSMMLKMGLPPIYDRSALKMTEQEMQACSGRLPYFRLKIDQSREITWEDEVRGRVSFQAKNISDPIIKRTDGTYTYMFPSVVDDIDFAITHIIRGEDHVSNTATQICIFDILKAKVPVFVHLPLVHFRDAKISKRVGSDDIEIRHLRDIGMEPMAIKSYLARMGTSLPVEPQENHDVLVESFDIRTFNQAPIKFSLDDISRLNSRIVQCLSFDKVKDRFVQQGLECTEEFWYLIRDNVNTVEDVREWINICNSQITTAIDDKDRTFISEAKALLPDTELDEEVCKAWLQRIKETSNRSTRDVLLPLRLATTGVTTGPGLAQLLPFIGRAEVVRRLECASKGHNAN | 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 Length: 450
Subcellular Location: Cytoplasm
EC: 6.1.1.17
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Q5NL22 | MSAGPAKNPSVVTRFAPSPTGFLHIGGARTALFNWLFARHNGGQFQLRIEDTDRVRSTKEAIDAIIDGMRWLGLDWDGDITYQFERAPRHTEVAEELLKAGKAYKCFATAEELEAMRAEQRAKKQPQRYDGRWRDRDPSEAPAGAPYVVRLKAEQEGETTLHDLVQGDVTVKNAELDDMILLRSDGTPTYMLAVVVDDHDMGVNHVIRGDDHLNNTFRQLGIIRAMNWDAPQYAHIPLIHGADGAKLSKRHGALGVEAYRDDFGYLPEAICNYLLRLGWGHGDDEIITREQAIEWFDLTSVGRSPSRFDFKKLENINGHYIREADDQRLTDLVKPRVEKTLEQGLSSTEQALLLQAMPFLKPRAKNLNELAENSLFLFEKRPLKLEEKAAKQLENTSGSLLAILRKTLGDLPAWDSESLEKALHDVAEQADLKMGKVAQPLRAALTGRTVSPGIFDVMILLGQDESLARLDDQLSLSPTHS | 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 Length: 481
Subcellular Location: Cytoplasm
EC: 6.1.1.17
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O82462 | MDGMKLSFPPESPPLSVIVALSLSASPVTIDSSAAATTVPSFVFSDGRKLNGATVLLRYVGRSAKKLPDFYGNNAFDSSQIDEWVDYASVFSSGSEFENACGRVDKYLESSTFLVGHSLSIADVAIWSALAGTGQRWESLRKSKKYQSLVRWFNSILDEYSEVLNKVLATYVKKGSGKPVAAPKSKDSQQAVKGDGQDKGKPEVDLPEAEIGKVKLRFAPEPSGYLHIGHAKAALLNKYFAERYQGEVIVRFDDTNPAKESNEFVDNLVKDIGTLGIKYEKVTYTSDYFPELMDMAEKLMREGKAYVDDTPREQMQKERMDGIDSKCRNHSVEENLKLWKEMIAGSERGLQCCVRGKFNMQDPNKAMRDPVYYRCNPMSHHRIGDKYKIYPTYDFACPFVDSLEGITHALRSSEYHDRNAQYFKVLEDMGLRQVQLYEFSRLNLVFTLLSKRKLLWFVQTGLVDGWDDPRFPTVQGIVRRGLKIEALIQFILEQGASKNLNLMEWDKLWSINKRIIDPVCPRHTAVVAERRVLFTLTDGPDEPFVRMIPKHKKFEGAGEKATTFTKSIWLEEADASAISVGEEVTLMDWGNAIVKEITKDEEGRVTALSGVLNLQGSVKTTKLKLTWLPDTNELVNLTLTEFDYLITKKKLEDDDEVADFVNPNTKKETLALGDSNMRNLKCGDVIQLERKGYFRCDVPFVKSSKPIVLFSIPDGRAAK | 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 Length: 719
Subcellular Location: Cytoplasm
EC: 6.1.1.17
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Q54KB8 | MSKAKDTGILRFDDTPLAATFPLVAIITSKVVGGVKIVGRKGLDSTEFSIVGTQDSLKGSYVIAKYLARTTPSLSLYGENALSASKIDEFIDKFAHLKSEKFNEFLKEMNEYLTLRAFLIGFNLTLADIVLFARIKMVKEIQEEINKLGKTIPHLNRWYGYLSQLESFVEADNAFNGKKETKASGKAGAEGTAATTEKVAPQKGAMGWVGNFEALNLPGLVEGKVVTRFPPEPSGYMHIGHCKAAIINNYYAEKYNGKIIIRFDDTNPSKEKEEYVENIIKDINNLGIKYEKITHTSDYFDLIHDYAIQMIKEGIAYCDDTPQVKMSEERDNAIESVHRNNSVEKNLEMFDEMKKATEQGVKCVLRAKLDMAHIDKAFRDPAIYRCNSTPHHRTGDKYKVYPLYDFACPIVDSVEGITHALRSNEYNNKRNLYNHYLEILHLENKPYISDYSRLSFFNVLLSKRKLQHFVDTGLVSGWTDPRLPTLQGITRRGLTVAALKEFILSQGASAANTTLDLGKLFVGNKAVLEPTCPRYTAIAKATAVKFTLSNGPTLPEVKDCLKYAKDPSMGTKKVTFSNNLLLEGDDCNQIKEGEEVTLMNWGNAIVETLQRNENGDVVSMTGKLHLEGDVKKTDKKLSWLSSDCADTVTVVLQDYDYIITKPKLEDGDDLDTFTNKNSKFEIEAFTDENILTLKLNDKIQFERRGFFNVDQVGDGVKPYILIYIPSGPIKPAGAALYPFKKVEKVAAPVNPKPTAKKQEKQSKK | 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 Length: 764
Subcellular Location: Cytoplasm
EC: 6.1.1.17
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Q8SSE4 | MDGKSEFKEELINYILLKKYGKGAQDPPVYSNALKKAPQEMFPPGLVDALDSYSINLSRSEGVEFLVLLNSLVNDIRSEEVKDIIFGMINTNQMLTKLMKDKKEVERFPDTCKMYSEQFKANKPLLKEFNAGSRKEQGNLEIGEPSENVVTRFPPEPNGRLHIGHARAALLNWYFASKGNGRLLVRFDDTNPEKEEERFERGILSDLSLLGINEYTLSHTSDYFDKIIDLGVFLIGEGKAYADNTPQEVMRDERGRGVESRCRSMDVEESKRIFKEMARGNASGYCLRAKIDMSSSNKAMRDPVIFRVNESPHHRTGDKYKVYPTYDFACPIVDSLEGITLSLRANEYRDRNQQYYWFIDNLRLRNRPKIHDFSRLNFENTVLSKRKLKYYVDNGFVSGWDDPRLATIAGIKRLGMNMEALREYILMQGVSQKTCTISWDKVWAINRKKIDPVSARYFCVQQRDAVEVSIDNTSEYTMDVPKHKKNGDLGTKEVFYSSQILLSQEDGRVLQDNEEFTLMNWGNAIVKSKTVENGTVTKMEVSLNPDGDFKLTKNKMSWVSKRGSVTVELAEYGNLMNDEDTEDLALRFNRNSVKKEYWYAESAIINVREGEVIQFERNGFYYCDGFLVFNLLPFTKQKRTGN | 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 | MLENISKSEFVNFLLEKKHNIEPKTLPILEQHIREQKLDDFFLDFSIDFTDEELNNFLSKLDYWLKNTKLNSSKADVIFGLLYSCNKFIKLIKNPTFSFVEIKQFYNDILNTNKNYIIEYNKKDKGKINIAVEGNVVTRFPPEPSGFLHIGHIKAALLNDLMAKNGKLLIRFDDTNPIKEEKMYENVIIEDLHTLGIKNYTIVRSSDHFDSLYNYAIQLIQLGLAYCDNTDQLQMREERTKGIPSKNRNTDIETNLSIFSKMSSGNCLDYCLRAKIDYTNLNKALRDPVIYRHIEKEHNITKNKYKIYPTYDFACPIIDSLDGVTLALRTNEYRDRNEQYYWFLEKLNLPNKPKIYDFSRLNFENTVLSKRQMKFYVDNHFVSGWDDPRLSTLRGILRLGMDIDTLKEYIINQGSSQKSSVISWDKVWSLNKKNIDHKSARYSAIPKLYCVECLILDKNNNEIITKTEDIPKFKKNLSLGNKTIIKSSHILISQEDANILNNNEEFTLMNWGNMKVKEKQIVNGIIIKIILEENLAGDVKTTKNKLTWVNKENIIEFKILEYDTLQNDKNTDNLAEKFNTNSKKEEIWLGEKALISVSPKTYIQIERIGFFICDKPLEFILIPYTKQKRMR | 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 | MAVENAINFREICSLLDISESYKCTINAFLDNVEKCTDKHYNDALNLLDTFFSNEVKSNSLVNDLIFCIINSNFDFLKVFKSNKLRLENLQIVYESAFNENKPFLKEFSAKDKINKEVKKNLYSTPAVTRFAPEPSGCLHIGHLKALLVNYNLAEKSNGTLLLRFDDTNPVKNYEKYEKEILRDLDTLGITGLKISHSSDYFELLVDEAVSLINKNLAYVDNTDQETMRIERFEGIESKMRNINNSESLKIFKELLQGRAPGYCLRAKIDMSNPNKSMRDPVIYRASDKMHGRCKLYKAFPTYDFVCPIVDSIEGVTVVCRANEYKDRNEQYKWFLENLELENKPEFNDFSKLNLEDTVLSKRKIDKLISDSLVTGWDDPRLATIQGIKRLGMHMTALKDYINLQGASNKTNVISWDKIWAMNKKVIDPLSPRFMAVEKINCVRVFITNFEGLKYTKNIPLNKKNTSLGSKDVLFSDTLLFSQEDGFVLKENEEFTLMNWGNAIVEKKVVENSIVTELYIKLHLEGDYKSTTNKISWVSESGAVTATGIEYGKLLVNEEFNINSKIDKQYYVESSITNLSTDMKHVQFERIGFFYCDSPCVFHLVPFTKQKRTY | 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 | MPSTLTINGKAPIVAYAELIAARIVNALAPNSIAIKLVDDKKAPAAKLDDATEDVFNKITSKFAAIFDNGDKEQVAKWVNLAQKELVIKNFAKLSQSLETLDSQLNLRTFILGGLKYSAADVACWGALRSNGMCGSIIKNKVDVNVSRWYTLLEMDPIFGEAHDFLSKSLLELKKSANVGKKKETHKANFEIDLPDAKMGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKEEFQDSILEDLDLLGIKGDRITYSSDYFQEMYDYCVQMIKDGKAYCDDTPTEKMREERMDGVASARRDRSVEENLRIFTEEMKNGTEEGLKNCVRAKIDYKALNKTLRDPVIYRCNLTPHHRTGSTWKIYPTYDFCVPIVDAIEGVTHALRTIEYRDRNAQYDWMLQALRLRKVHIWDFARINFVRTLLSKRKLQWMVDKDLVGNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPIAPRHTAIVNPVKIHLEGSEAPQEPKIEMKPKHKKNPAVGEKKVIYYKDIVVDKDDADVINVDEEVTLMDWGNVIITKKNDDGSMVAKLNLEGDFKKTKHKLTWLADTKDVVPVDLVDFDHLITKDRLEEDESFEDFLTPQTEFHTDAIADLNVKDMKIGDIIQFERKGYYRLDALPKDGKPYVFFTIPDGKSVNKYGAKK | 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-tRNA(Gln) substrate for the tRNA-dependent amidotransferase (AdT), which generates mitochondrial glutaminyl-tRNA(Gln) by transamidation of glutamyl-tRNA(Gln).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Mass (Da): 80843
Sequence Length: 708
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
Q9FEA2 | MASLVYGTPWLRVRSLPELAPAFLRRRQSSLFYCSRRSFAVVACSTPVNNGGSVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLERSTRESEAAVLQDLSWLGLDWDEGPGVSGDFGPYRQSERNALYKQYAEKLLESGHVYRCFCSSEELVKMKENAKLKQLPPVYTGKWATASDAEIEQELEKGTPFTYRFRVPKEGSLKINDLIRGEVCWNLDTLGDFVVMRSNGQPVYNFCVTVDDATMAISHVIRAEEHLPNTLRQALIYKALKFPMPQFAHVSLILAPDRSKLSKRHGATSVGQYREMGYLPQGMVNYLALLGWGDGTENEFFTLEDLVEKFSIERVNKSGAIFDSTKLRWMNGQHLRALPNEKLTKLVGERWKSAGILTESEGSFVNEAVELLKDGIELVTDSDKVLLNLLSYPLHATLASPEAKPAVEDKLHEVAASLIAAYDSGEIPSALEEGQGAWQKWVKAFGKSLKRKGKSLFMPLRVLLTGKLHGPEMGTSIVLIYKAGSPGIVVPQAGFVSMEERFKILREIDWEALNKDESVPLESTATVST | 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 Length: 570
Subcellular Location: Plastid
EC: 6.1.1.17
|
Q5ZJ66 | MAGMLREVCGAAASGLRVRFGPSPTGFLHLGGLRTALYNYVFAKQQRGTFVLRVEDTDQGRVVAGAAESIEDMLHWAGIPPDESPRRGGPFGPYQQSLRLDLYRAASEALLDRGAAYRCFCTPQRLELLRKEALRNQQTPRYDNRCRHLTPKEVAEKLAQGLDWVVRFRLERGVEPFQDLVYGWNKHEVAEVEGDPVILKADGFPTYHLANVVDDHHMGISHVLRGTEWLTSTSKHLLLYKAFGWDPPQFGHLPLLLNKDGSKLSKRQGDIFLERFAQEGYLPEALLDMITNCGSGFAEKQMGRTLEELISQFEIGRITTHSALLDLEKLPEFNRMHLTRHIENEGLRQKLIQELQLLVEDVYGDQEVDKEVLEKEYVEQVLLLRKGHISHLKDLVSDNYSYLWVRPSVSREQLQMISAEVDEIGKLVLGLMTKPAAVWTIEELNKDLRSLQKQTRETKYSSMMKLLRLALSGQQHGPSVAEMMVTLGPREVCGRISKVLSS | 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 Length: 502
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.17
|
Q0P499 | MKILRGVSRQMCTSRPEVRVRFAPSPTGFLHLGGLRTALYNFLFSRQRRGVFILRLEDTDQKRLVPGAAEHIEDMLEWAGIPPDESSRRGGDYGPYVQSERLHLYTEAASSLLNTGHAYYCFCSNQRLELLKKEAQRSGHAPRYDNRCRRLQPQQVEQKLAAGVPAVVRFKLHTGTEEFQDLVFGWTGHAVGAVEGDPVILKADGYPTYHLASVVDDHHMRISHVLRGCEWLISSAKHLQLYRALRWTPPTYAHLPLLLNRDGSKLSKRQGDIFLQSFRDRGVLPETLLDLVTHAGSGFSDNRMGRRLDELIRDFNISKITTHSALLDLDKLEEFSRLHLQRRIEDPQQCVWLCEELKQMVKHTHSSEISAAAVLEPEYIERVLQLRKGHISSLQDLLSSTHSYLWVRPRVSQTQLQSESAHAKDIATAVMQMVLAGGSLVSMERLSSELKQISSRTNSTHSSVMKVLRLLLSAQQRGPSVAEMMLSLGEQEVCVRLQKALEL | 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 Length: 503
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.17
|
Q5JPH6 | MAALLRRLLQRERPSAASGRPVGRREANLGTDAGVAVRVRFAPSPTGFLHLGGLRTALYNYIFAKKYQGSFILRLEDTDQTRVVPGAAENIEDMLEWAGIPPDESPRRGGPAGPYQQSQRLELYAQATEALLKTGAAYPCFCSPQRLELLKKEALRNHQTPRYDNRCRNMSQEQVAQKLAKDPKPAIRFRLEQVVPAFQDLVYGWNRHEVASVEGDPVIMKSDGFPTYHLACVVDDHHMGISHVLRGSEWLVSTAKHLLLYQALGWQPPHFAHLPLLLNRDGSKLSKRQGDVFLEHFAADGFLPDSLLDIITNCGSGFAENQMGRTLPELITQFNLTQVTCHSALLDLEKLPEFNRLHLQRLVSNESQRRQLVGKLQVLVEEAFGCQLQNRDVLNPVYVERILLLRQGHICRLQDLVSPVYSYLWTRPAVGRAQLDAISEKVDVIAKRVLGLLERSSMSLTQDMLNGELKKLSEGLEGTKYSNVMKLLRMALSGQQQGPPVAEMMLALGPKEVRERIQKVVSS | 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 Length: 523
Subcellular Location: Mitochondrion matrix
EC: 6.1.1.17
|
Q9HDX9 | MLSYTSCAKLICSRYIVSKISFYSLKRCNSTAVVRTRFAPSPTGFLHLGSLRTALFNYLWAKKSNGKFILRLEDTDQKRKVTGSDLEIYKVLKQFNLQWDEGPIVGGPYGPYEQSSRLQIYQKYAQHLIETGRAYVSYSVPIATTKIDSSTKYHEISIDDLTDAQRKLYKSKKFPYVVRFRMKEPSPFTDLVYGKIAIKSDSREIEESNNFVILKSDGFPTYHFANVVDDHLMHITHVIRGEEWVPSTIKHIQLYEAFGWKPPKFAHLPLLVNPDGSKLSKRQNDAHVSSLLQEGFLPEAILNFIALMGWSSRQKSDFLPMKELIDLFSIDKLTKSSSIVAFEKLYFLNKNYLRRAISDVNRLDELIELVQPRLIQKFSHSSRSHDKSYTKKLLLLLKNKVHTIKEFEKIVFYFYEASDLQQIRSLVSSLITVEELPKILTTILNKFETIEWNTHEIQISLKEIAMEHQMPLKKIQSLLRYGLCGNLPGGGISDTISLLGKETVKSRLERLLLSLKHELPKRSCIV | 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 Length: 526
Subcellular Location: Mitochondrion
EC: 6.1.1.17
|
Q11PQ4 | MSDTNKQVRVRFAPSPTGPLHIGGVRTALYNYLFARKMGGKMLLRIEDTDQNRFVPGAEAYIQEALAWVGIVIDEGAGVGGPHAPYKQSERKPMYREYAEKLIAEGNAYYAFDTSEELEAMKERLKAAKVASPSYNMVTRMQMNNSLTLPEDEVKRRLDAGDEYVIRLKVPRKEEIRLNDMIRGWVVVHSSTIDDKVLLKSDGMPTYHLANIVDDHLMEITHVIRGEEWLPSAPLHVLLYRFLGWEDTMPQFAHLPLLLKPDGNGKLSKRDADAGGFPIFPLDWKDPASGDTWIGFKQQGYLQEATTNFLAFLGWNPGTQQELFTMDELIEAFTVERIGKSGTKFDINKAKWYNQQYMRQLPDETLTRLLKEEADKHQAKYDAAKLPLIAQMLKERLTFAKDYWIEGQFFFEAPETFDEKVASTKWNAEAVTVISAYKEALAAYTGEFNAENVKHVLHEVLEKADVKIGKIMQALRLALTGAGAGPDLMQFIEIVGKEEAIKRMQFALITLSEKVNS | 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 Length: 517
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
Q3Z6S3 | MTNEVRVRYAPSPTGYPHLGNIRTAMFNWLFARHNGGKFIVRIEDTDRERYVEGAVESILESLNWLGLDWDEGPDKGGDYGPYYQSERLFLYRQAAERLVTEGKAYYCHCSSERLDKMREEQIARKEPPGYDRCCRDLCLGQKEGAVIRFKIPLEGQTTFIDLIRGEVTFDNAKQDDFVILKSDGFPTYHLASVVDDHAMQISHVLRAEEWLPSTPKHLMLYKALGYTPPQYAHLPMILGPDRSKLSKRHGATSTIEYKQAGYLPETMVNFLSLLGWAYDDKTELFSRKQLIEYFCLEKVSKTAAIFNYEKLDWMNGMYIRTLSAPDLASRAIPFLEKDERIAASGRLNFDYTTKVMPLIQERVKKLSELAELCWFIYSDNISYDPASLIDKKLTKDESLCALKAAFARLEALANFDAVSMEEHIRPLAAELELKPGQLFGMLRTASTGQQVAPPLFQTMEVLGRERCLGRIAMAIARLSELPS | 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(Glu)
Sequence Mass (Da): 55256
Sequence Length: 484
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
Q9RX30 | MSAPSSPRVTRIAPSPTGDPHVGTAYIGLFNHTLARQSGGRFILRVEDTDRNRYVPDSEKRIFQMMQWLNLTPDESPLQGGPNGPYRQSERFDLYGDYARQLVQSGHAYYAFETSDELAALREEAQKAGHVIAIPSRDLGAAQAQARVDAGEPAVIRLKVDRDGETVVNDLLRDPIHFANKEIDDKVLLKADGFPTYHLANVVDDRLMQVTHVVRAEEWITSTPIHVLLYRAFGWPEPVFAHMPLLRNADKSKISKRKNPTSVEWYQNQGFLPEAMLNFLATMGWTHPDGQEIFDLAEFERVFRLEDVTLGGPVFDLAKLRWYNGKYLREVLSEDDVARRLHAFLMQNKVTLPSVDGPQDPYFRAVTHLMIPRLEVFADFMDKTLYFWSEDYPVNEKAQKAIDAGKELLPELAARLKNLPTFDAASIKEMFHAYAEEKGLKMGKVMPPIRAAVAGTMESPDLPEMLEALGRERVLARVEKAAR | 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 Length: 483
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
B1I4Z1 | MDTVRVRFAPSPTGSLHIGGARTALFNWLFARHHGGAFILRLEDTDTGRNIDEAAAQIVSSLRWLGIDWDEGYDRGGPFGPYRQSERFELYREEARRLLANGDAYWCYCTPEDLAAQREEARQRGEVPRYDGRCRQLTDDARREKEAAGIRPALRVKMPKTGTTVVKDRIRGEIGFDNATLDDIIVMKSNGGPTYNFACVVDDGAMRISHVIRAEEHLSNTPKQIVLFNLLGYALPEFVHVPMILAPDRSKLSKRHGATAVDEFRADGFLPEALINYLALLGWSPGSEQEQFTVEELVASFSLDAVSKHAAIYDVKKLTWLNAQYLNSLPQARVVEAVRPFMQEAGYLSATPNPAELDYLSRVVEAVRSRVHTLAELRDASAYFYRSDFEYDDKGVRKHFTKPGVTNILARGRDALSRLPAGRFTVEGTEEAFRQVIEELGVSGGTLIHPTRLALSGRTVGPGLFDIIAVLGKEECLLRLDRAIAWIGANVNNANRTDACS | 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 Length: 501
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
Q250Q8 | MLKVRFAPSPTGPLHIGGARSALFNYLLARKEDGVFIVRSEDTDLERSSRESEHNIMEALRWLNIQWDEGIEVGGDNGPYRQTERLALYQEYTDRLLASGDAYYCYCSEEELEQERQDLMAKGETPRYLGKCRHLSAAERQTYEAAGRKPVVRFRVPEGRQILINDRVRGEVVFDSDGIGDYVIVKSDGIPTYNFAVVIDDTTMNITHVIRGEEHLSNTPRQVLIYQALGLPTPEFAHISLILNTEGKKMSKRDGDTAVIDYQAKGYLPEAVVNFIALMGWSPPGEEEFFTLEEMTQAFSLERVSKSPAVFDLNKLNYMNAHYIKQADPERLTDLAVPYLREMGAIPQGTLSEEERAWVTHYVQAIINHLSYMAQVKDFVHYVQGGEAPTPEGEALEILQGEQVPAVLDLFVEKLKSLEAIRVDTVKPLFKQITKETKLGGKQVFMPIRIALTGQMHGPELYDIVPLLGLENVLSRLAGTKALLAGSR | 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(Glu)
Sequence Mass (Da): 54926
Sequence Length: 488
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
A8ZWA3 | MKQIITRFPPSPTGHLHIGGARTALFNWLYARHTGGRFILRIEDTDVERSTTQSAEGIIKSLEWLGIDWDEGPYFQSRRMEVYAEYIQRLLASGHAYYCTCSPERLKERRERALAEGRNPTYDGTCREKALPPSDDAVVRFRTPDTGKTVLDDRVKGGIAFDNAEIGDFIIQRSDQTPTYNFAVVVDDITMGINTIIRGDDHVTNTPRQILMYRALDSELPLFAHVPMVLGRDRSRLSKRHGAMSVLEYRDTGYLPDGLINALVRLGWSHGDQEFFTRKELIELFSLEHIGTSAGVFDPDKLLAINAEHIKKSDPAALAPHLLPLLKEKGYAAENNDYLHNAIHTLLLRSKTLKEMADKAAFYYEDPLSYDPAATAKFLVPENMEILEMLAEKLATLDSLTEKDQEPAFTAVMEKTGKKFGKIAQPVRVALTGRTESPGIFETIEALGRRKTLERLADAVEMIKKST | 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(Glu)
Sequence Mass (Da): 52586
Sequence Length: 467
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
B2A4B3 | MTNKARLRFAPSPTGQIHIGNIRTALFNWLYSRHIDGEFILRVEDTDMNRSVEEYEQIIFRALSWLGLDWDEGPQKGGDFGPYRQSERKDIYHKYANKLLEAGKAYYCYCTEEELEEMREAQRARGEMPRYSGKCADLSSEERAELENEGRKSVIRFKVPENQTIRVNDLVKGEVDFESDGIGDFILIKSDDMASYNFACVVDDYLMNITHVLRGEDHLSNTPKQVMIYEALGFETPEFGHLSLILGPDKAKLSKRHGDTFIGEYREKGYLPEAMVNFLALLGWSPPGEDELFTQDELIRLFDIGRVSKSAAVFDVDKLNWMNSHYIKEADTERLLNLSKEYLINSDLVSQEQLEHDWEWFVSAVDLVKEKIDMLSELPPQLKIFYGDDVDLKGEEVEFLEKDHVPELLSEVINQFNDLDSFEDPKAIKKAVNKAGKQVGVKGKQLFMPVRIAVSGQMHGPELDQLISLLGRERAINRVNSTLSQIQS | 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(Glu)
Sequence Mass (Da): 55984
Sequence Length: 488
Subcellular Location: Cytoplasm
EC: 6.1.1.17
|
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