SYC_HELP2
ID SYC_HELP2 Reviewed; 465 AA.
AC B6JMA7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=HPP12_0883;
OS Helicobacter pylori (strain P12).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=570508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P12;
RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT "The complete genome sequence of Helicobacter pylori strain P12.";
RL Submitted (OCT-2008) 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: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; CP001217; ACJ08035.1; -; Genomic_DNA.
DR RefSeq; WP_000471404.1; NC_011498.1.
DR AlphaFoldDB; B6JMA7; -.
DR SMR; B6JMA7; -.
DR EnsemblBacteria; ACJ08035; ACJ08035; HPP12_0883.
DR KEGG; hpp:HPP12_0883; -.
DR HOGENOM; CLU_013528_0_1_7; -.
DR OMA; AKYWMHN; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000008198; 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; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR10890; PTHR10890; 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; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..465
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_1000090843"
FT MOTIF 29..39
FT /note="'HIGH' region"
FT MOTIF 269..273
FT /note="'KMSKS' region"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ SEQUENCE 465 AA; 53128 MW; DF0A65C3728C79B8 CRC64;
MFIYDTKSKQ KVPFEPLVQN KANIYVCGPT VYDDAHLGHA RSAIAFDLLR RTLELSGYEV
VLVRNFTDID DKIINKAFKE NKSIQELSSI YIESYTRDLN ALNVKKPSLE PKASEYLDAM
VRMIETLLEK NFAYQVSNGD IYLDTSKDKD YGSLSMHNSS VEFSRIGLVQ EKRLEQDFVL
WKSYKGDNDV GFDSPLGKGR PGWHIECSSM VFETLALANA PYQIDIHAGG ADLLFPHHEN
EACQTRCAFG VELAKYWMHN GFVNINNEKM SKSLGNSFFI KDALKNYDGE ILRNYLLGVH
YRSVLNFNEE DLLVSKKRLD KIYRLKQRVL GTLGGINPNF KKEILECMQD DLNVSKALSV
LESMLSSTNE KLDQNPKNKA LKGEILANLK FIEELLGIGV KDPSAYFQLG VSESEKQEIE
NKIEERKRAK EQKDFLKADS IREELLNHKI ALMDTPQGTI WEKLF
