ID SYC_GEOKA Reviewed; 466 AA.
AC Q5L429;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00041};
DE EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00041};
DE Short=CysRS {ECO:0000255|HAMAP-Rule:MF_00041};
GN Name=cysS {ECO:0000255|HAMAP-Rule:MF_00041}; OrderedLocusNames=GK0085;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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:0000255|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00041};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00041}.
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DR EMBL; BA000043; BAD74370.1; -; Genomic_DNA.
DR RefSeq; WP_011229600.1; NC_006510.1.
DR AlphaFoldDB; Q5L429; -.
DR SMR; Q5L429; -.
DR STRING; 235909.GK0085; -.
DR KEGG; gka:GK0085; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_9; -.
DR Proteomes; UP000001172; Chromosome.
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; cd07963; Anticodon_Ia_Cys; 1.
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; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..466
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159401"
FT MOTIF 32..42
FT /note="'HIGH' region"
FT MOTIF 267..271
FT /note="'KMSKS' region"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 466 AA; 53949 MW; CC0E69D401636B1D CRC64;
MSSIRLYNTL TRKKEPFEPL EPNKVKMYVC GPTVYNYIHI GNARAAIVFD TIRRYLEFRG
YDVTYVSNFT DVDDKLIKAA RELGESVPAI AERFIEAYFE DIQALGCKKA DIHPRVTENI
DTIIEFIQAL IDKGYAYEVD GDVYYRTRKF REYGKLSHQS IDELQAGARI EIGEKKDDPL
DFALWKAAKE GEICWDSPWG KGRPGWHIEC SAMARKYLGD TIDIHAGGQD LTFPHHENEI
AQSEALTGKP FAKYWLHNGY LNINNEKMSK SLGNFVLVHD IIREIDPQVL RFFMLSVHYR
HPINYSEELL ESARRGLERL KTAYSNLQHR LQASTNLTDN DEEWVSRIAD IRASFIREMD
DDFNTANGIA VLFELAKQAN LYLQEKTTSE KVIHAFLREF EQLADVLGLT LKQDELLDEE
IEALIQKRNE ARKNRDFALA DRIRDELRAK NIILEDTPQG TRWKRG
//
