ACL_RS00050
  | Uniprot: A9NE72
Description: serine--tRNA ligase EC number: 6.1.1.11 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). {ECO:0000255|HAMAP-Rule:MF_00176}.; CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}. Pathway: PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00176}. Active site: Binding site: BINDING 285 285 Serine. {ECO:0000255|HAMAP-Rule:MF_00176}.; BINDING 385 385 Serine. {ECO:0000255|HAMAP-Rule:MF_00176}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 262 264 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}.; NP_BIND 349 352 ATP. {ECO:0000255|HAMAP-Rule:MF_00176}. Site: Gene names (primary): serS Gene names (synonym): Mass: 48,263 Subunit structure [CC]: SUBUNIT: Homodimer. The tRNA molecule binds across the dimer. {ECO:0000255|HAMAP-Rule:MF_00176}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; serine-tRNA ligase activity [GO:0004828]; selenocysteine biosynthetic process [GO:0016260]; selenocysteinyl-tRNA(Sec) biosynthetic process [GO:0097056]; seryl-tRNA aminoacylation [GO:0006434] Gene ontology IDs: GO:0004828; GO:0005524; GO:0005737; GO:0006434; GO:0016260; GO:0097056 Chain: CHAIN 1 423 Serine--tRNA ligase. /FTId=PRO_1000077184. Signal peptide: Domain [CC]: DOMAIN: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding. {ECO:0000255|HAMAP-Rule:MF_00176}. Sequence similarities: SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP-Rule:MF_00176}. Protein families: Class-II aminoacyl-tRNA synthetase family, Type-1 seryl-tRNA synthetase subfamily Coiled coil: Domain [FT]: Motif: Region: REGION 231 233 Serine binding. {ECO:0000255|HAMAP-Rule:MF_00176}. EMBL: CP000896 ProteinModelPortal: A9NE72 MEROPS: EnsemblBacteria KO: ABX80652 UniPathway: K01875 CDD: Gene3D: cd00770 HAMAP: 1.10.287.40 InterPro: MF_00176 PANTHER: IPR002314;IPR006195;IPR002317;IPR015866;IPR033729;IPR010978 PIRSF: PTHR11778 PRINTS: PIRSF001529 PROSITE: PR00981 Pfam: PS50862 ProDom: PF02403;PF00587 SMART: SUPFAM: TIGRFAMs: SSF46589 |
13186-14458(+) >nucleotide sequence AGAGGTGGTGATTTTAGCCACTTAAGACAATTAATAGATTTACAAGAAGAGCGTAAATCT GTAATTAAAGAAGTTGAAGACTTAAAAGCAAAAAGAAACGAATACTCCAAAGAAATTGGG GAACTTAAAAGACAAAAACAAGATGCTTCTCACGTGTTATTAAAAGTAGAGTCCATTAAA AGTGACATACCAGCACTTGAGTTAAAACTTGGTGAGATTGATGAAAAAATTAATAAAGAA CTCATCGTTTTACCAAATATTCCTGCTGACGATGTACCGGTTGGTAAAGATGAATCTGCA AATATTGAAATTAAAAAATGGGGTACTATTAGACATTTTGATTTTGAAGTAAAAGATCAT ACTCAATTAGGTGAAGCACTAAATATATTAGACTTTGAACGTGCAACTAAAATCACTGGT CCACGTTTTGTAGTAGATAAAGGGCTAGGTGCTAGACTGGAAAGAGCGCTTATAAACTTT ATGATAGATACACATGCGTATACACATGGTTATACCGAAATCATTCCACCGTTTATTGTA AATGATAAATCTATGTATGCAACAGGACAATTTCCTAAGTTTAAAGAAGATGCTTTTAAA TTAGAAGGATTTGATTGGTATTTAAATCCAACAGCAGAAGTACCAACTATTAACCTATTT AGAGATGAAATCATTGATAATGATGCATTACCAATTCAGTATGTAGCTTATACAACAGCA TTTAGATCAGAGGCAGGTTCTGCTGGACGAGATACTAAGGGTATTTTAAGACAACATCAA TTCAATAAAGTTGAATTAATTAAATTTGCACGACCTGAAGATTCTGAACAAGCTCATCAA GATATGTTAGCAAACTCAGAAAGAATACTACAACTATTAAATATTCCTTATCGAGTAGTT GTCTTATCAACAGGAGACATGGGCTTTGGTATGAGTAAGACATACGATATTGAAGTATGG TTACCAGGTCAAAATATGTACCGTGAAATTGGATCTATTTCAAATGCTAGAGACTTTCAA GCAAGAAGAGCCAACATTCGCTTTAAACGTTCAAAAGATGCTAAAACAGAATATGTGCAT ACATTAAACGGTTCTGGTTTAGCTGTTGGTAGAACAATGATTGCAGTACTAGAGAACTAT CAAAATCAAGATGGATCAATTACAATACCAGAAGTCTTAAAACCATATATGGGTGTAGAA GTTATTAAATAA >protein sequence ELKRQKQDASHVLLKVESIKSDIPALELKLGEIDEKINKELIVLPNIPADDVPVGKDESA NIEIKKWGTIRHFDFEVKDHTQLGEALNILDFERATKITGPRFVVDKGLGARLERALINF MIDTHAYTHGYTEIIPPFIVNDKSMYATGQFPKFKEDAFKLEGFDWYLNPTAEVPTINLF RDEIIDNDALPIQYVAYTTAFRSEAGSAGRDTKGILRQHQFNKVELIKFARPEDSEQAHQ DMLANSERILQLLNIPYRVVVLSTGDMGFGMSKTYDIEVWLPGQNMYREIGSISNARDFQ ARRANIRFKRSKDAKTEYVHTLNGSGLAVGRTMIAVLENYQNQDGSITIPEVLKPYMGVE VIK |
© Fisunov Lab of Proteomics, 2016.