SPM_005640
  | Uniprot: A0A037UNM1
Description: glycyl-tRNA ligase EC number: 6.1.1.14 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). {ECO:0000256|HAMAP-Rule:MF_00253, ECO:0000256|SAAS:SAAS00015999}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). {ECO:0000256|HAMAP-Rule:MF_00253, ECO:0000256|SAAS:SAAS00345537}. Pathway: Active site: Binding site: BINDING 98 98 Substrate. {ECO:0000256|HAMAP-Rule:MF_00253}.; BINDING 168 168 Substrate. {ECO:0000256|HAMAP-Rule:MF_00253}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 200 202 ATP. {ECO:0000256|HAMAP-Rule:MF_00253}.; NP_BIND 210 215 ATP. {ECO:0000256|HAMAP-Rule:MF_00253}.; NP_BIND 284 285 ATP. {ECO:0000256|HAMAP-Rule:MF_00253}.; NP_BIND 328 331 ATP. {ECO:0000256|HAMAP-Rule:MF_00253}. Site: Gene names (primary): glyQS Gene names (synonym): Mass: 53,107 Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00253, ECO:0000256|SAAS:SAAS00006558}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; glycine-tRNA ligase activity [GO:0004820]; glycyl-tRNA aminoacylation [GO:0006426] Gene ontology IDs: GO:0004820; GO:0005524; GO:0005737; GO:0006426 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000256|HAMAP-Rule:MF_00253, ECO:0000256|SAAS:SAAS00541124}. Protein families: Class-II aminoacyl-tRNA synthetase family Coiled coil: Domain [FT]: DOMAIN 146 363 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:PS50862}. Motif: Region: REGION 215 219 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00253}.; REGION 324 328 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00253}. EMBL: AGBZ02000004 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92213 UniPathway: CDD: Gene3D: cd00774 HAMAP: 3.40.50.800 InterPro: MF_00253_B PANTHER: IPR002314;IPR006195;IPR004154;IPR027031;IPR022961;IPR033731;IPR002315 PIRSF: PTHR10745 PRINTS: PROSITE: PR01043 Pfam: PS50862 ProDom: PF03129;PF00587 SMART: SUPFAM: TIGRFAMs: SSF52954 |
191058-192426(+) >nucleotide sequence GGTAGTGAGATTTATGGCGGTTTAGCAAACAGCTGAGATTTTGGACCGTTGGGGGTTGAA TTAGAACGAAATTTAAAAAATTTATGATGACAACATTTTATTACGAAATCAAAATATAAT GTTGGTCTTGATAGTGCTATTTTAATGAACAATAATGTTTGAAAAGCTTCTGGGCACCTT GGTAATTTTGCTGACCCATTATTAGACTGTAAAAAGTGTAAAACCCGAATGCGGGCAGAT AAACTGATTGAAGATAATTATCCGAAATTAAATTGTGGTGGTTGAACTAATGAACAATTA GAAACTTTTATTACTGAAAAAAATATTTTATGTCCAAATTGTGGTGGACATGACTTTACT GAAATTCGTCAGTTTGAATTAATGTTTAAAACAAATCAAGGTGTAATTGAAGATGAAAAA TCAGTTGTTTATTTGCGGCCAGAAACAGCACAAGGAATTTTTGTCAATTTTAAAAATGTC CAACGTTCTTTACGAAAAAAAATCCCTTTTGGAGTTGGTCAAATTGGAAAGTCATTTCGT AATGAAATTACCCCGGGAAATTTTATTTTTCGTACACGTGAATTTGAACAAATGGAATTA GAATTTTTTTATGATAGTAACGAAAAGGTTGATTGATTTGAATATTGAGTTAAAGAAGTA ACCAAGTTTTTAGAATTAATTAATTTAAAATCAGAAAACTATCGTTTTCGTGAGCATAAT GCTGATGAATTAGCCCATTATGCGAAACGAACTATTGATATTGAATATAAATTTCCGTTT GGAATAGGTGAATTATGGGGGATCGCTGACCGTGGGGATTATGATTTACGTCGTCATAGT GAAATGAGTAAAAATGATTTGTCGTATTTAAATCAAGAAACAAATGAAAAAATTATGCCG CATGTAATTGAACCATCTGTTGGAGTTGGTCGTTTGCTGCTAGCTATTTTATATGATGCT TACCATGTTGAAAAAGTTGATGACAATGAGACGAGAATTGTTTTAAAATTAAGTCCGTTA TTAGCTCCGTATCAAATTGCGGTGATTCCATTAAGCAAACAATTAAACAGCGAGGCTTAT CAACTATATGAAAAACTCTTAGTTCATTTTCAGTGTACTTATGATGAAACAGGAAATATT GGAAAGCGTTATCGTCGTCAAGATGCGATTGGAACACCGTTTTGTGTAACAGTTGATTTT GATACTCAAGAAGACCAAAAAGTTACCGTTCGTAATCGTGATACAATGAAACAAGAACGA GTGGCAATTACTAATTTAGAAAGTTATTTCACCGCAGCATTAAAATAA >protein sequence VGLDSAILMNNNVWKASGHLGNFADPLLDCKKCKTRMRADKLIEDNYPKLNCGGWTNEQL ETFITEKNILCPNCGGHDFTEIRQFELMFKTNQGVIEDEKSVVYLRPETAQGIFVNFKNV QRSLRKKIPFGVGQIGKSFRNEITPGNFIFRTREFEQMELEFFYDSNEKVDWFEYWVKEV TKFLELINLKSENYRFREHNADELAHYAKRTIDIEYKFPFGIGELWGIADRGDYDLRRHS EMSKNDLSYLNQETNEKIMPHVIEPSVGVGRLLLAILYDAYHVEKVDDNETRIVLKLSPL LAPYQIAVIPLSKQLNSEAYQLYEKLLVHFQCTYDETGNIGKRYRRQDAIGTPFCVTVDF DTQEDQKVTVRNRDTMKQERVAITNLESYFTAALK |
© Fisunov Lab of Proteomics, 2016.