GCW_04010
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Uniprot: A0A0F6CLI6
Description: glutamyl-tRNA synthetase EC number: 6.1.1.17 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). {ECO:0000256|HAMAP-Rule:MF_00022}. Cofactor: Enzyme regulation: Function [CC]: 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). {ECO:0000256|HAMAP-Rule:MF_00022}. Pathway: Active site: Binding site: BINDING 255 255 ATP. {ECO:0000256|HAMAP-Rule:MF_00022}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): gltX Gene names (synonym): Mass: 57,874 Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00022}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; glutamate-tRNA ligase activity [GO:0004818]; tRNA binding [GO:0000049]; glutamyl-tRNA aminoacylation [GO:0006424] Gene ontology IDs: GO:0000049; GO:0004818; GO:0005524; GO:0005737; GO:0006424 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. {ECO:0000256|HAMAP-Rule:MF_00022, ECO:0000256|RuleBase:RU363037}. Protein families: Class-I aminoacyl-tRNA synthetase family Coiled coil: Domain [FT]: DOMAIN 3 323 tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}. Motif: MOTIF 10 20 "HIGH" region. {ECO:0000256|HAMAP-Rule:MF_00022}.; MOTIF 252 256 "KMSKS" region. {ECO:0000256|HAMAP-Rule:MF_00022}. Region: EMBL: CP006916 ProteinModelPortal: MEROPS: EnsemblBacteria KO: AHB99958 UniPathway: K01885 CDD: Gene3D: HAMAP: 1.10.10.350;1.10.1160.10;3.40.50.620 InterPro: MF_00022_B PANTHER: IPR008925;IPR020751;IPR001412;IPR004527;IPR000924;IPR020061;IPR020058;IPR014729 PIRSF: PRINTS: PROSITE: PR00987 Pfam: PS00178 ProDom: PF00749 SMART: SUPFAM: TIGRFAMs: SSF48163 968006-969503(-) >nucleotide sequence ATCATACAAAGCAATCACTTTGTTTAACTCTGGACCGTGCTTTTTATTAGATAAAACAAT TCTTAATGGCATATATAAGTTCTTACCACCTAAAGGTTTTTCTAAAACCAAATCACCTAG TTTAATTTGGTGAGCTAACCAATTAATAATCTCTTTAACGTTATGGTCATTAACCTGATC AAGTTGATCAATCTTCTCTTTAAATGAGATTAAAAGTTGACGATAATTTGGATTAGATTT TAAGAAATCTAGATCAGCTTGATCAAGGTTAGATAACCCAACATGGGGAACAAAACTTTC TTTAATGATCTCGTTGATCTGATAACCATACTGTAATTGGTTTTTAAACATCAAGCAGAT CTCATTAACTTTAGTTTTAATCTCATCATATTCATTAAGATCAACATATGGTTTGATGAA TGCTAAATACATAACATCATCCATATTTTTGATGTATTCAGATGAGATTCAATTTAGTTT TTTAATGTCAAAAAAAGAAGGGGCTGCACTTAAGTTTTTAATCGTAAACGATTTAACCAA CGTAGGTAAATCTAAGATCTCAATATTATCTGGGTGAGATCAACCTAATAAAGCAATAAA GTTAACTAGTGCATCTGCTAAATAACCTTTTTTTCTAAACCCTTCAACGAACTGTTCAAC CGCTAAATTTCTTTTAGATAATTTCTTACCAGTTTCATCAACAATGATTGATAGATGACC ATAAACAAATTCATTTTTGAACCCTAAAGCTTCTTTGATCGCTAACTGATAGGGAGTATT TGAGATATGCTCTTCTCCTCTTAAGATATGTGAGATCTTCATATCATGGTCATCGATCAC AACCGCAAAGTTGTACGTCGCGATCTGATTTGATTTTAAGATCACAGGGTCGCTCATTGA ACTAGTATTAAAGATTAAGTTCCCACGAATTAAATCGTTTCAAGAATATTCCTTATTTTC TTTTAATAATAATCTGATCGTAAAAGGAATCTTATCAGCCAAATTTTTTTGAATCTGCTC TTCTGAAAGAAGAAAACACTTTCTTGAATAAATTGGTGGTTTATACTGTTTTAATAAGTC TCCACGGTGTTTTTGTAGTTCTTCAGGTGTACAAAAACAACGGTATGCTTTTTTTTCTTC TAAAAGTTGGTAGGCATATTTTTGGTAAACTTCTAGTTTTTCAGACTGACGATAAGGTCC GCTTCGAGTCGGGTTTCAAATTGATTCGTCAGCAAAAATGTTTAATCACTTTAGGTTATA AAGTTGGTTCTCAGCACCATCTTCAACGTTTCTTTCAATGTCCGTATCTTCGATACGAAC AATAAATTCCCCGTTGTTGTGCTTGGCAAATAAATAATTAAATAAAGCTGTGCGTGCACC GCCAATGTGGAAATGCCCTGTTGGCGATGGTGCGTATCTGGTTCTAATCTTAGACAT >protein sequence NLKWLNIFADESIWNPTRSGPYRQSEKLEVYQKYAYQLLEEKKAYRCFCTPEELQKHRGD LLKQYKPPIYSRKCFLLSEEQIQKNLADKIPFTIRLLLKENKEYSWNDLIRGNLIFNTSS MSDPVILKSNQIATYNFAVVIDDHDMKISHILRGEEHISNTPYQLAIKEALGFKNEFVYG HLSIIVDETGKKLSKRNLAVEQFVEGFRKKGYLADALVNFIALLGWSHPDNIEILDLPTL VKSFTIKNLSAAPSFFDIKKLNWISSEYIKNMDDVMYLAFIKPYVDLNEYDEIKTKVNEI CLMFKNQLQYGYQINEIIKESFVPHVGLSNLDQADLDFLKSNPNYRQLLISFKEKIDQLD QVNDHNVKEIINWLAHQIKLGDLVLEKPLGGKNLYMPLRIVLSNKKHGPELNKVIALYDK QTILKNLDDAINYLTNAK |
© Fisunov Lab of Proteomics, 2016.