ID A0A1R4B328_9VIBR Unreviewed; 435 AA.
AC A0A1R4B328;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:SJL83319.1};
GN ORFNames=VPAL9027_01285 {ECO:0000313|EMBL:SJL83319.1};
OS Vibrio palustris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1918946 {ECO:0000313|EMBL:SJL83319.1, ECO:0000313|Proteomes:UP000189475};
RN [1] {ECO:0000313|EMBL:SJL83319.1, ECO:0000313|Proteomes:UP000189475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 9027 {ECO:0000313|EMBL:SJL83319.1,
RC ECO:0000313|Proteomes:UP000189475};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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=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|HAMAP-Rule:MF_00176};
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|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 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|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|HAMAP-
CC Rule:MF_00176}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00176}.
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DR EMBL; FUFT01000002; SJL83319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4B328; -.
DR STRING; 1918946.VPAL9027_01285; -.
DR OrthoDB; 9804647at2; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000189475; Unassembled WGS sequence.
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: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; 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:UP000189475}.
FT DOMAIN 173..421
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 30..64
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 242..244
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 273..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 296
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 360..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 396
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
SQ SEQUENCE 435 AA; 48852 MW; 5AB421CE99E64369 CRC64;
MLDSKLLRAE LDETAAKLAR RGYQLDVDTI RSLEEKRKSI QVEVENLQSK RNSISKQIGQ
LMSKGDKEGA EEIKQQIGSL GNDLDAKKVE LVSLQEELDA IALGIPNIPA DEVPDGKDED
DNVEVSRWGT PKTYDFEVKD HVDLGEMGDG LDFASATKLT GARFVVMKGQ FARLHRAIAQ
FMLDLHTEQH GYTELYVPYL VNADSLYGTG QLPKFGADLY HTEPLTEKVD DEELRRLSLI
PTAEVPVTNL VRDEIVDEEQ LPLKMTAHTP CFRSEAGSYG RDTRGLIRMH QFDKVELVQV
TKPEDSMDAL EELTGHAEKV LQLLELPYRK VILCTGDMGF GAKKTYDLEV WVPAQNTYRE
ISSCSNTGDF QARRMQARFR RQGQKKPELV HTLNGSGLAV GRTMVAILEN NQQADGRIEI
PQVLQKYMNG HTHIG
//
