ID A0A291JNA4_9STAP Unreviewed; 466 AA.
AC A0A291JNA4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041,
GN ECO:0000313|EMBL:SUM56086.1};
GN ORFNames=BJD96_12385 {ECO:0000313|EMBL:ATH61050.1}, BUZ61_06810
GN {ECO:0000313|EMBL:PTK59129.1}, CD130_04145
GN {ECO:0000313|EMBL:PNZ99350.1}, NCTC13834_02464
GN {ECO:0000313|EMBL:SUM56086.1};
OS Staphylococcus nepalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=214473 {ECO:0000313|EMBL:ATH61050.1, ECO:0000313|Proteomes:UP000217956};
RN [1] {ECO:0000313|EMBL:PTK59129.1, ECO:0000313|Proteomes:UP000240400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 4337 {ECO:0000313|EMBL:PTK59129.1,
RC ECO:0000313|Proteomes:UP000240400};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:ATH61050.1, ECO:0000313|Proteomes:UP000217956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1 {ECO:0000313|EMBL:ATH61050.1,
RC ECO:0000313|Proteomes:UP000217956};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Staphylococcus nepalensis JS1.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PNZ99350.1, ECO:0000313|Proteomes:UP000236280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15150 {ECO:0000313|EMBL:PNZ99350.1,
RC ECO:0000313|Proteomes:UP000236280};
RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D.,
RA Crook D., Paul J.;
RT "Draft genome sequences of 64 type strains of genus Staph aureus.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PTK59129.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4337 {ECO:0000313|EMBL:PTK59129.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:SUM56086.1, ECO:0000313|Proteomes:UP000254412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13834 {ECO:0000313|EMBL:SUM56086.1,
RC ECO:0000313|Proteomes:UP000254412};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00041};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00041}.
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DR EMBL; CP017460; ATH61050.1; -; Genomic_DNA.
DR EMBL; PPRR01000049; PNZ99350.1; -; Genomic_DNA.
DR EMBL; PZHR01000028; PTK59129.1; -; Genomic_DNA.
DR EMBL; UHDS01000001; SUM56086.1; -; Genomic_DNA.
DR KEGG; snl:BJD96_12385; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000217956; Chromosome.
DR Proteomes; UP000236280; Unassembled WGS sequence.
DR Proteomes; UP000240400; Unassembled WGS sequence.
DR Proteomes; UP000254412; 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:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00840; DALR_2; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00041};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00041}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT DOMAIN 351..417
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|SMART:SM00840"
FT MOTIF 30..40
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT MOTIF 265..269
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ SEQUENCE 466 AA; 53794 MW; AB73A33797B802D6 CRC64;
MITLYNTLTR QKETFKSIEP GKVKMYVCGP TVYNYIHIGN ARPAINYDVV RRYLEYQGYE
VNYVSNFTDV DDKLIKRSKE LNEPVNTIAN RYIDAFYEDV GALNVKKATS NPRVMNHMDD
IIKFIGELVE EGYAYQSGGD VYFRTRKFED YGKLSHQSLN DLKVGARIEQ GEQKEDALDF
TLWKQAKPDE ISWDSPFGKG RPGWHIECSV MAYHELGATI DIHAGGTDLQ FPHHENEIAQ
SEAHNHAPFA NYWMHNGFIN IDNEKMSKSL GNFVLVHEII KEIDPDVLRF FMISVHYRSP
INYNMELVSA ARSGLERIRN SYQAIEEREA IATNIEAQDN YIEEINQILE QFETVMNDDF
NTANAITAWY DLTKLANKYV LENTTSTEVI ERFKTVYQIF SDVLGVPLKP ETSDELLDED
VEALIEERNT ARKNKDFARA DEIRDQLKAQ NIILEDTPQG VRFKRG
//
