ID A0A2H6C2C9_TETHA Unreviewed; 423 AA. AC A0A2H6C2C9; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 05-DEC-2018, entry version 6. DE RecName: Full=Serine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00176}; DE EC=6.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176}; DE Short=SerRS {ECO:0000256|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000256|HAMAP-Rule:MF_00176, GN ECO:0000313|EMBL:GBD70730.1}; GN ORFNames=TEHN7118_0388 {ECO:0000313|EMBL:GBD67582.1}, TEHN7121_1276 GN {ECO:0000313|EMBL:GBD70730.1}; OS Tetragenococcus halophilus subsp. halophilus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Tetragenococcus. OX NCBI_TaxID=1513897 {ECO:0000313|EMBL:GBD70730.1, ECO:0000313|Proteomes:UP000236609}; RN [1] {ECO:0000313|EMBL:GBD67582.1, ECO:0000313|Proteomes:UP000236214} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NISL 7118 {ECO:0000313|EMBL:GBD67582.1, RC ECO:0000313|Proteomes:UP000236214}; RA Shiwa Y., Nishimura I., Yoshikawa H., Koyama Y., Oguma T.; RT "Whole genome sequencing of Tetragenococcus halophilus subsp. RT halophilus NISL 7118."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GBD70730.1, ECO:0000313|Proteomes:UP000236609} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NISL 7121 {ECO:0000313|EMBL:GBD70730.1, RC ECO:0000313|Proteomes:UP000236609}; RA Shiwa Y., Nishimura I., Yoshikawa H., Koyama Y., Oguma T.; RT "Whole genome sequencing of Tetragenococcus halophilus subsp. RT halophilus NISL 7121."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also CC able to aminoacylate tRNA(Sec) with serine, to form the CC misacylated tRNA L-seryl-tRNA(Sec), which will be further CC converted into selenocysteinyl-tRNA(Sec). {ECO:0000256|HAMAP- CC Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + CC L-seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, CC Rhea:RHEA-COMP:10128, Rhea:RHEA-COMP:9742; EC=6.1.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00176}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + CC L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, CC Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703; EC=6.1.1.11; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00176}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step CC 1/1. {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer. CC {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a CC N-terminal extension that is involved in tRNA binding. CC {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Type-1 seryl-tRNA synthetase subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:GBD70730.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BDEC01000013; GBD67582.1; -; Genomic_DNA. DR EMBL; BDED01000043; GBD70730.1; -; Genomic_DNA. DR RefSeq; WP_014125862.1; NZ_BDEI01000038.1. DR GeneID; 35861834; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000236214; Unassembled WGS sequence. DR Proteomes; UP000236609; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00770; SerRS_core; 1. DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR002317; Ser-tRNA-ligase_type_1. DR InterPro; IPR015866; Ser-tRNA-synth_1_N. DR InterPro; IPR033729; SerRS_core. DR InterPro; IPR010978; tRNA-bd_arm. DR PANTHER; PTHR43697; PTHR43697; 1. DR Pfam; PF02403; Seryl_tRNA_N; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1. DR PRINTS; PR00981; TRNASYNTHSER. DR SUPFAM; SSF46589; SSF46589; 1. DR TIGRFAMs; TIGR00414; serS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00176, KW ECO:0000313|EMBL:GBD70730.1}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000236214, KW ECO:0000313|Proteomes:UP000236609}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00176}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176}. FT DOMAIN 172 409 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE: FT PS50862}. FT NP_BIND 262 264 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}. FT NP_BIND 349 352 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}. FT REGION 231 233 Serine binding. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT COILED 45 79 {ECO:0000256|SAM:Coils}. FT BINDING 285 285 Serine. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT BINDING 384 384 Serine. {ECO:0000256|HAMAP-Rule: FT MF_00176}. SQ SEQUENCE 423 AA; 48066 MW; B95CD893603E4260 CRC64; MLDIKMIREN FEQVKEKLQT RDVPEETLTE FLRLDKKRRS LLVETEEMKK NRNNVSEKIA QAKRNKEDTS EQIAEMREVG SKIKALDKEI ATIDEKLNTI ATTLPNLPHD SVPVGKDEED NVEIRKWGAS QTFSFEPKNH WEIGENLNIL DFERGAKVSG SRFVYYKGLG ARLERALYNF MLDQHVYQQG YTEMITPYAV NSQAMFGTGQ FPKFTEDVFQ LEDSGLTLIP TAEVPLTNYY SNEILDVSQL PVYFTALSPA FRSEAGSAGR DTRGLIRLHQ FNKVEMVKFS DSQHSYDELE KMTADAESIL QKLGLSYRVM TLSTGDMGFS AAKTYDLEVW IPAQNTYREI SSCSNCEDFQ ARRAMIRYRD TEGKLHYAHT LNGSGLAVGR TVAAILENYQ NEDGSVTIPE VLVPYMGGMT KIG //