ID D9Q038_ACIS3 Unreviewed; 459 AA. AC D9Q038; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 04-FEB-2015, entry version 31. 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 AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000256|HAMAP-Rule:MF_00176}; GN OrderedLocusNames=ASAC_0269 {ECO:0000313|EMBL:ADL18676.1}; OS Acidilobus saccharovorans (strain DSM 16705 / VKM B-2471 / 345-15). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae; OC Acidilobus. OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18676.1, ECO:0000313|Proteomes:UP000000346}; RN [1] {ECO:0000313|EMBL:ADL18676.1, ECO:0000313|Proteomes:UP000000346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16705 / VKM B-2471 / 345-15 RC {ECO:0000313|Proteomes:UP000000346}; RX PubMed=20581186; DOI=10.1128/AEM.00599-10; RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I., RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans RT supports a new order, Acidilobales, and suggests an important RT ecological role in terrestrial acidic hot springs."; RL Appl. Environ. Microbiol. 76:5652-5657(2010). 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: ATP + L-serine + tRNA(Sec) = AMP + diphosphate CC + L-seryl-tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate CC + L-seryl-tRNA(Ser). {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 --------------------------------------------------------------------------- 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; CP001742; ADL18676.1; -; Genomic_DNA. DR RefSeq; YP_003815707.1; NC_014374.1. DR EnsemblBacteria; ADL18676; ADL18676; ASAC_0269. DR GeneID; 9498492; -. DR KEGG; asc:ASAC_0269; -. DR HOGENOM; HOG000035937; -. DR KO; K01875; -. DR OMA; YHTDIME; -. DR BioCyc; ASAC666510:GH9G-281-MONOMER; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000346; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.40; -; 1. DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom. 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; IPR010978; tRNA-bd_arm. DR PANTHER; PTHR11778; PTHR11778; 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:ADL18676.1}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Complete proteome {ECO:0000313|Proteomes:UP000000346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:ADL18676.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176}; KW Reference proteome {ECO:0000313|Proteomes:UP000000346}. FT NP_BIND 284 286 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}. FT NP_BIND 371 374 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}. FT REGION 253 255 Serine binding. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT BINDING 300 300 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT BINDING 307 307 Serine. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT BINDING 408 408 Serine. {ECO:0000256|HAMAP-Rule: FT MF_00176}. SQ SEQUENCE 459 AA; 52780 MW; D59E1563610261A4 CRC64; MPWSILNLLR TNPEALREVA RKRQIDVKII DEAVQLDEQW RKVQAEINEL RHQHNVISAA IPKAKGEERE KLLAQAKELS RELEDAERRL SELEAKREEA LWRLPNVVLD DVPVGGEEAT RPVRFWGTPR VYHEYLDAFK AQTEAYGFNV PYELIDWKPV GHADMLENVL KLGDTEKASE VAGSRFYYLF DDLVWLDFAL LLYAIDKLTS KGYTLVLPPY MLRYKVINSV IDLATFQDAI YKIENDDLYL IATAEHSLAA MYYNEELYDD ELPKKFVGIS PAFRREAGAA NKDLKGIFRV HQFHKVEQFV FSKPEESQKI HEELISNAEG LFQGLGIPYR VVNIASGDLG ACAVKKYDLE AWMPAQGKYR EMVSASNCTD WQAYRLNIRL IRRKGMERGE YVHTLNSTGI ASTRTITAIL ENFQEPDGTV IIPKVLRKYL EPFDAAPKDF IKPRPRKAI //