ID A0A1V4TZJ2_9EURY Unreviewed; 425 AA. AC A0A1V4TZJ2; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 05-JUL-2017, entry version 2. 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:OPX66025.1}; GN ORFNames=A4E36_02127 {ECO:0000313|EMBL:OPX66025.1}; OS Methanoregulaceae archaeon PtaB.Bin009. OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; OC Methanoregulaceae. OX NCBI_TaxID=1811720 {ECO:0000313|EMBL:OPX66025.1}; RN [1] {ECO:0000313|EMBL:OPX66025.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PtaB.Bin009 {ECO:0000313|EMBL:OPX66025.1}; RA Nobu M.K., Narihiro T., Liu M., Kuroda K., Mei R., Liu W.-T.; RT "Diverse syntrophic catabolism for escaping thermodynamic limitations RT and driving niche segregation."; RL Submitted (FEB-2017) 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: 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 -!- 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:OPX66025.1}. 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; MVQC01000133; OPX66025.1; -; Genomic_DNA. DR UniPathway; UPA00906; UER00895. 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; 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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00176}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00176, ECO:0000313|EMBL:OPX66025.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00176}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00176}. FT DOMAIN 179 412 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE: FT PS50862}. FT NP_BIND 263 265 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}. FT NP_BIND 350 353 ATP. {ECO:0000256|HAMAP-Rule:MF_00176}. FT REGION 232 234 Serine binding. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT BINDING 279 279 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT BINDING 286 286 Serine. {ECO:0000256|HAMAP-Rule: FT MF_00176}. FT BINDING 387 387 Serine. {ECO:0000256|HAMAP-Rule: FT MF_00176}. SQ SEQUENCE 425 AA; 48694 MW; FCE076B4AB5BE35E CRC64; MLDLKFIREN PDAVRQDLAR RGDEEKRAWV DDLIENDRRS RVLKVQADEL RRRRNSIARE INEERKAGRD TGALKKEASE LPGRIREIEA ELDEITATVR FYLMRLPNIL HDSVPVGKDD TENVELRRVG SPRTPGFPLA SHGQLASDRG WADFERAARA AGAGFYYLKG NLALLDLALQ RFAIDLLAEK GFVPVIPPYM INRRSYEGVT DLSDFEKVMY KIEDDDAYLI ATSEHPIGAM YQDEIFEERD LPLRLAGISP CFRREIGSHG LDTKGLFRVH QFHKVEQFVF CRPEDSWEIH EELLANAEEI FSSLGLPYRV VNICTGDIGT VAAKKYDIEV WMPREEAYRE VVSCSNCTSY QAVRANIRVR DPHDFESKRF LHTLNSTAVA TTRTIRAILE NYQEEGGAVM VPPALRPYMN DLEYL //