SPM_004740
  | Uniprot: A0A037UKM3
Description: glutamate--tRNA ligase 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 256 256 ATP. {ECO:0000256|HAMAP-Rule:MF_00022}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): gltX Gene names (synonym): Mass: 55,853 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 4 324 tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}. Motif: MOTIF 11 21 "HIGH" region. {ECO:0000256|HAMAP-Rule:MF_00022}.; MOTIF 253 257 "KMSKS" region. {ECO:0000256|HAMAP-Rule:MF_00022}. Region: EMBL: AGBZ02000004 ProteinModelPortal: A0A037UKM3 MEROPS: EnsemblBacteria KO: KAI92047 UniPathway: 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 |
16248-17697(+) >nucleotide sequence AATACAAGAACGGCATTATTTAATTATTTATTTGCAAAACATTATGATGGTGTTTTTGTT CTACGAATTGAAGATACAGATATTGAACGAAATGTGGAAGGAGCAATTGCATCACAATTA GATAATTTACGTTGATTAGGGATTGAACCAGATGAAACAATTGATCGCCCAGGAGCTTAT GGGCCATATCGACAATTAGAACGATTAGAGCTTTATCAGAAATATGCACAAAAATTATTA ACAACAAAAAAAGCATATTATTGTTTTTGTACTCCAGCTGAACTTGACAAAGATCGTGAA GCACAATTAGCAAAAGGATATTCTTCACCACGTTATAATCGCAAGTGTTGACAATTAACT TCCGAACAAATTGCTGAAAAATTAGCGAAACAAATTCCGTATAATTTACGTTTTTTTGTT CCCGATGAAGCAAGTTATGATTTTAATGATTTAGTCCGCGGATCTGTTCATTTTGAAGGA AAAGACCTTGGTGATTGAGTCATTTTAAAATCAAATGGGATTCCAACTTATAACTTTGCG GTAGTCATTGATGATATGTTAATGGAAATTAGTCATGTTGTGCGGGGAGAAGAACATATT TCGAATACGCCAAAACAATTAATGATTTACGAAGCATTTAATGCGACCCCCCCCGTTTTT GCTCATTTAACCTTAATTGTTAATGAACAACATAAAAAGTTGTCAAAACGAGATAGTCAT TTAATGCAATTTATTAGTCAATATCGAACATTAGGATATTTACCAACAGCAATTTTTAAT TTTATTAGTTTATTGGGATGATCCCCCCCGGGTACTGTTGAAATTTTTAGTCATGATGAG TTAATTAAAATTTTTGATGAAACACGATTTAGTAAATCACCAAGTATGTTTGATGTTAAA AAATTAACTTGAATGAATAATTATTATCTTAAACAAATGTGTGATGAGGATTATCTAACT TTTGTCCGACCTTTTTTAGCAGCGGGCTATGATTTAACAAAAAAAACAACCGAATGAGTA AATATGTTATTATTAATTTATAAAAAAGAACTCCAATATGGGGCAGAAATTGTAGCATTA ACAAAACCATTTTTTGAACCAACAACAAAATTATCAGCAACAACGCAAGCAGTGCTAACA GAATTAAGTGGTTATGAAGAAATGATAACATCTTTTAAAACAGCGTTAAGTCAATTGCCA GTTTGAGATGAACCAAATATTAAGCAATTAATTAGTAAAATGGGGGAGCAATATGTTATG AAAGGAAAGAATTTATTTATGCCAATTCGAATTTTCACTTCTCATCAGGAACATGGACCA GAACTAGCAAAGGTTATTTATTTATTAGGGAAAGAACAAGTAATTAGTAATATTACTAAA TTGCAATAA >protein sequence DNLRWLGIEPDETIDRPGAYGPYRQLERLELYQKYAQKLLTTKKAYYCFCTPAELDKDRE AQLAKGYSSPRYNRKCWQLTSEQIAEKLAKQIPYNLRFFVPDEASYDFNDLVRGSVHFEG KDLGDWVILKSNGIPTYNFAVVIDDMLMEISHVVRGEEHISNTPKQLMIYEAFNATPPVF AHLTLIVNEQHKKLSKRDSHLMQFISQYRTLGYLPTAIFNFISLLGWSPPGTVEIFSHDE LIKIFDETRFSKSPSMFDVKKLTWMNNYYLKQMCDEDYLTFVRPFLAAGYDLTKKTTEWV NMLLLIYKKELQYGAEIVALTKPFFEPTTKLSATTQAVLTELSGYEEMITSFKTALSQLP VWDEPNIKQLISKMGEQYVMKGKNLFMPIRIFTSHQEHGPELAKVIYLLGKEQVISNITK LQ |
© Fisunov Lab of Proteomics, 2016.