ID A0A1S3LLW4_SALSA Unreviewed; 513 AA.
AC A0A1S3LLW4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=serine--tRNA ligase {ECO:0000256|ARBA:ARBA00012840};
DE EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
GN Name=LOC106567354 {ECO:0000313|RefSeq:XP_013991973.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013991973.1};
RN [1] {ECO:0000313|RefSeq:XP_013991973.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013991973.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001032};
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 Evidence={ECO:0000256|ARBA:ARBA00001706};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily.
CC {ECO:0000256|ARBA:ARBA00010728}.
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DR RefSeq; XP_013991973.1; XM_014136498.1.
DR AlphaFoldDB; A0A1S3LLW4; -.
DR STRING; 8030.ENSSSAP00000076617; -.
DR PaxDb; 8030-ENSSSAP00000076617; -.
DR Ensembl; ENSSSAT00000110091; ENSSSAP00000076617; ENSSSAG00000065653.
DR GeneID; 106567354; -.
DR KEGG; sasa:106567354; -.
DR OMA; GYTPCFR; -.
DR OrthoDB; 239638at2759; -.
DR Proteomes; UP000087266; Chromosome ssa13.
DR Bgee; ENSSSAG00000065653; Expressed in semen and 16 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 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; PTHR11778:SF7; SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11778; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|RefSeq:XP_013991973.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 203..453
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 479..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 58649 MW; 2BFBEBA1B0BF28CD CRC64;
MVLDLDQFRA DKGGDPEVIR ETQRKRFKDV SLVDKLVHAD TEWRKCRFTA DNLNKAKNLC
SKTVGEKMKK KEPIGEDDSL PDDAQNLEAL TADTLAPLTV TQIKKVRLLV DEAVQKSDSE
RVKLEEERFQ YLREIGNLLH PSVPISNDED ADNKVERTWG DCTVQKKYSH VDLVVMIDGY
DGEKGAIVAG SRGYFLKGPL VFLEQALINY ALRMLHSKNY QMLYTPFFMR KEVMQEVAQL
SQFDDELYKV IGKSSEKSED TAIDEKYLIA TSEQPIAAFL RDEWLKPEEL PIRYAGLSTC
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVFA SPHDNKSWEM MDEMIGTAEE FYQTLGIPYR
IVNIVSGALN HAASKKLDLE AWFPGSAAFR ELVSCSNCLD YQARRLRIRY GQTKKMMDKA
DYVHMLNATM CATTRVMCAI LETYQTEEGI IIPEVLRNFM PPGMTEMLKF VKPAPIDVEM
SKKQKKQQDG GKKKQGSGDQ LQNQVDNMSV HDS
//
