ID H6SII4_PARPM Unreviewed; 432 AA. AC H6SII4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 10-JUN-2026, entry version 66. 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:CCG06750.1}; GN ORFNames=RSPPHO_00124 {ECO:0000313|EMBL:CCG06750.1}; OS Pararhodospirillum photometricum DSM 122. OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodospirillales; Rhodospirillaceae; Pararhodospirillum. OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG06750.1, ECO:0000313|Proteomes:UP000033220}; RN [1] {ECO:0000313|EMBL:CCG06750.1, ECO:0000313|Proteomes:UP000033220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220}; RA Duquesne K., Sturgis J.; RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able CC to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- CC seryl-tRNA(Sec), which will be further converted into selenocysteinyl- CC tRNA(Sec). {ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + CC diphosphate + H(+); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742, CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; CC Evidence={ECO:0000256|ARBA:ARBA00047929, ECO:0000256|HAMAP- CC Rule:MF_00176}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + CC diphosphate + H(+); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; CC Evidence={ECO:0000256|ARBA:ARBA00048823, ECO:0000256|HAMAP- CC Rule:MF_00176}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. CC {ECO:0000256|ARBA:ARBA00005045, 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|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N- CC 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 family. CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000256|ARBA:ARBA00010728, CC ECO:0000256|HAMAP-Rule:MF_00176}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; HE663493; CCG06750.1; -; Genomic_DNA. DR AlphaFoldDB; H6SII4; -. DR STRING; 1150469.RSPPHO_00124; -. DR KEGG; rpm:RSPPHO_00124; -. DR PATRIC; fig|1150469.3.peg.169; -. DR eggNOG; COG0172; Bacteria. DR HOGENOM; CLU_023797_1_1_5; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000033220; Chromosome DSM 122. 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:L-selenocysteine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00770; SerRS_core; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 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; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR002317; Ser-tRNA-ligase_type_1. DR InterPro; IPR015866; Ser-tRNA-synth_1_N. DR InterPro; IPR042103; SerRS_1_N_sf. DR InterPro; IPR033729; SerRS_core. DR InterPro; IPR010978; tRNA-bd_arm. DR NCBIfam; TIGR00414; serS; 1. DR PANTHER; PTHR43697:SF1; SERINE--TRNA LIGASE; 1. DR PANTHER; PTHR43697; SERYL-TRNA SYNTHETASE; 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; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF46589; tRNA-binding arm; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00176}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00176}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00176}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00176}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00176}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00176}; Reference proteome {ECO:0000313|Proteomes:UP000033220}. FT DOMAIN 180..417 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT COILED 39..104 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 238..240 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" FT BINDING 238 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" FT BINDING 269..271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176, FT ECO:0000256|PIRSR:PIRSR001529-2" FT BINDING 269 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" FT BINDING 292 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176, FT ECO:0000256|PIRSR:PIRSR001529-1" FT BINDING 356..359 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176, FT ECO:0000256|PIRSR:PIRSR001529-2" FT BINDING 390 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" FT BINDING 392 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176" SQ SEQUENCE 432 AA; 47220 MW; AC0899D93864E34D CRC64; MFCLQGFLIM HDLKVIRDTP AAFDAALARR GIAPVADALL ALDQQRRAAQ TALNDMQARR NEVSRAIGDI RKAGGTAEAE TQEVAALKAR MSETEDEVRR LGEALDQQLL TLPNRVDDTV PDGSDETANV EVRRWGTPRA FDFAVRDHVD LGQGLDGMDF EAAARLSGAR FVVLKGALAR LERALAQYML DLHITEHAYT EVQTPALVRE PALLGTGQLP KFAEDLFRLE QGYYLIPTAE VTLTNLVNGQ ILPLSALPLR MTALTQCFRA EAGAAGRDTR GMIRQHQFEK VEMVSIVAPE DSDAELERMT GCAEAVLQGL GLPYRVVALC SGDIGFSARK TYDLEVWLPA QGCYREISSC SNTGDFQARR MNARFKVEGE KGTRFVHTLN GSGLAVGRTL VAVLENYQNA DGSVSVPPVL RPYMGGLERI GS //