ID A0A150WQL7_BDEBC Unreviewed; 430 AA.
AC A0A150WQL7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=AZI86_06995 {ECO:0000313|EMBL:KYG66782.1};
OS Bdellovibrio bacteriovorus.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG66782.1, ECO:0000313|Proteomes:UP000075320};
RN [1] {ECO:0000313|EMBL:KYG66782.1, ECO:0000313|Proteomes:UP000075320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R0 {ECO:0000313|EMBL:KYG66782.1,
RC ECO:0000313|Proteomes:UP000075320};
RA Ploux O.;
RL Submitted (MAR-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG66782.1}.
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; LUKE01000001; KYG66782.1; -; Genomic_DNA.
DR RefSeq; WP_061834360.1; NZ_LUKE01000001.1.
DR AlphaFoldDB; A0A150WQL7; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000075320; 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|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:UP000075320}.
FT DOMAIN 146..416
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 52..110
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 269..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 292
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 356..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
FT BINDING 391
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00176"
SQ SEQUENCE 430 AA; 47737 MW; 377268E7EFE718B6 CRC64;
MIDIKLLEKK AETGTSYYDE YKQSLINRGA SADILDTVMG LSKKRREMIT EAETAKANQN
KLSGEIGKLK REGKDASAIL AEVDKLKSTV KDLEAKAAEA DLEVTNLLLT MPNKPHSSVP
VGSDEKGNKI LKTVGTPTSF SFKAKEHFEL GEKLNIIDFE RAGKTTGTRF AFLKGAAAAM
ERGLIQFMMD LHSQKHGYTE MIPPFMVNSN SLLGTGQFPK FKEDVFNLSG TDLYLIPTAE
VPVTNYYNNE ILDEKDLPQS FCAYSPCFRS EAGSAGRDTR GLIRQHQFDK VELMTFCHPD
KSYEVHEALT THAEQVLLDL ELPFRRMLLC TGDMGFGAAK THDLEVWLPG QGAYREISSC
SNFEDFQARR ANIRFRSAGG KPQFVHTLNG SGLAVGRTLV AILENNQRED GSIAIPKALQ
KYMAGKTEIR
//