SYSC_CAEEL
ID SYSC_CAEEL Reviewed; 487 AA.
AC Q18678;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable serine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.11;
DE AltName: Full=Seryl-tRNA synthetase;
DE Short=SerRS;
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN Name=sars-1 {ECO:0000312|WormBase:C47E12.1};
GN Synonyms=srs-2 {ECO:0000312|WormBase:C47E12.1};
GN ORFNames=C47E12.1 {ECO:0000312|WormBase:C47E12.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Ser); 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Sec); 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 -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
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DR EMBL; Z68882; CAA93105.1; -; Genomic_DNA.
DR PIR; T20008; T20008.
DR RefSeq; NP_501804.1; NM_069403.5.
DR AlphaFoldDB; Q18678; -.
DR SMR; Q18678; -.
DR BioGRID; 42962; 14.
DR IntAct; Q18678; 1.
DR STRING; 6239.C47E12.1.1; -.
DR iPTMnet; Q18678; -.
DR EPD; Q18678; -.
DR PaxDb; Q18678; -.
DR PeptideAtlas; Q18678; -.
DR PRIDE; Q18678; -.
DR EnsemblMetazoa; C47E12.1.1; C47E12.1.1; WBGene00005663.
DR EnsemblMetazoa; C47E12.1.2; C47E12.1.2; WBGene00005663.
DR GeneID; 177859; -.
DR KEGG; cel:CELE_C47E12.1; -.
DR UCSC; C47E12.1.1; c. elegans.
DR CTD; 177859; -.
DR WormBase; C47E12.1; CE05445; WBGene00005663; sars-1.
DR eggNOG; KOG2509; Eukaryota.
DR GeneTree; ENSGT00940000153792; -.
DR HOGENOM; CLU_023797_0_0_1; -.
DR InParanoid; Q18678; -.
DR OMA; SPCFRRE; -.
DR OrthoDB; 726296at2759; -.
DR PhylomeDB; Q18678; -.
DR UniPathway; UPA00906; UER00895.
DR PRO; PR:Q18678; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00005663; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; -; 1.
DR Gene3D; 3.30.930.10; -; 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 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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..487
FT /note="Probable serine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000122194"
FT BINDING 271..273
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 302..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 391..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
SQ SEQUENCE 487 AA; 55220 MW; EC4AA5B811E5BB07 CRC64;
MVLDIDMFRT EKGGNPEIIR KSQQDRFKDP KLVDEVIELD EKWRKERFVA DQLNRQKNAI
SKAIGEKMKK KEPQGTDDSV ADDIVARLAE LKIDELSQLT VVQLKKLRVL VDEKSVQTAA
AVIANENARH EKLIQIGNLI HSSVVVSKDE ANNKIERTFG DLSTKKKYSH VDLVVMVDGF
DGERGTVVAG GRGYFLKGPL VFLEQAIIQL ALQRLNVKGY VPLYTPFFMR KEVMQEVAQL
SQFDDELYKV SSKGSEIAGD TSVDEKYLIA TSEQPIAAYH RNEWIKETEL PIKYAGVSTC
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVLC SPNDNESWTL FDEMIGNAES YYQELQIPYQ
VVNIVSGELN NAAAKKFDLE AWFPGSGAYR ELVSCSNCLD YQSRRLKVRY GQTKKLSGEV
PFVHMLNATM CATTRVICAI LENNQTEEGI NVPTAIQQWM PENYRTFIPF VKPAPIDEDA
KKATGKK
