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Database: UniProt
Entry: N4WI76_9BACI
LinkDB: N4WI76_9BACI
Original site: N4WI76_9BACI 
ID   N4WI76_9BACI            Unreviewed;       467 AA.
AC   N4WI76;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
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:ENH95877.1};
GN   ORFNames=J416_13821 {ECO:0000313|EMBL:ENH95877.1};
OS   Gracilibacillus halophilus YIM-C55.5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH95877.1, ECO:0000313|Proteomes:UP000012283};
RN   [1] {ECO:0000313|EMBL:ENH95877.1, ECO:0000313|Proteomes:UP000012283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH95877.1,
RC   ECO:0000313|Proteomes:UP000012283};
RA   Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT   "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a moderately
RT   halophilic and thermophilic organism from the Xiaochaidamu salt lake.";
RL   Submitted (MAR-2013) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001080, 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|ARBA:ARBA00004496,
CC       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}.
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:ENH95877.1}.
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DR   EMBL; APML01000071; ENH95877.1; -; Genomic_DNA.
DR   RefSeq; WP_003473436.1; NZ_APML01000071.1.
DR   AlphaFoldDB; N4WI76; -.
DR   STRING; 1308866.J416_13821; -.
DR   PATRIC; fig|1308866.3.peg.2787; -.
DR   eggNOG; COG0215; Bacteria.
DR   OrthoDB; 9815130at2; -.
DR   Proteomes; UP000012283; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00041};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00041}; Reference proteome {ECO:0000313|Proteomes:UP000012283};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT   DOMAIN          353..417
FT                   /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT                   /evidence="ECO:0000259|SMART:SM00840"
FT   COILED          414..441
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           31..41
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOTIF           266..270
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   467 AA;  53820 MW;  23354D9256351A3B CRC64;
     MAIRIFNTLT REKETFTPIE PNRVKMYVCG PTVYNYIHIG NARPAIVFDT VRRYFEYRGY
     NVDYVLNFTD VDDKLIQAAN ELGEEVPTIA ERFIQAYKED VGALGVKEAV YHPRVTETMD
     DIIMFIQTLI DKGHAYEANG DVYFKTRSFD EYGKLSHQSI DELRSGARIQ VGEKKQDPLD
     FALWKQAKEG EIAWSSPWGQ GRPGWHIECS AMAKKYLGDT IDIHAGGQDL AFPHHENEIA
     QSEAQNEQTF ANYWMHNGYI NIDNEKMSKS LGNVVLAHDL IQQHDPKVVR FFMLSVHYRH
     PINFSDELLE GAKSSFQRII NVYENLEHRK KASVDLTDDT DVWLTKVDAL QQKFEKEMDD
     DFNTANAIAV IFDLVKEANV YLQEKQTHTK VIDAFQQLLK ESMQVLGISI DADDELLDEE
     IEQLIAERKQ ARQEKNFALA DKIRDDLKDK GIILEDTPQG TRWKRGL
//
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