ID   SYC_BDEBA               Reviewed;         482 AA.
AC   Q6MKR7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Bd2317;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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; BX842652; CAE80140.1; -; Genomic_DNA.
DR   RefSeq; WP_011164742.1; NC_005363.1.
DR   AlphaFoldDB; Q6MKR7; -.
DR   SMR; Q6MKR7; -.
DR   STRING; 264462.Bd2317; -.
DR   EnsemblBacteria; CAE80140; CAE80140; Bd2317.
DR   KEGG; bba:Bd2317; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_1_7; -.
DR   OMA; HAWPASE; -.
DR   OrthoDB; 952207at2; -.
DR   Proteomes; UP000008080; 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; Reference proteome; Zinc.
FT   CHAIN           1..482
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159356"
FT   MOTIF           30..40
FT                   /note="'HIGH' region"
FT   MOTIF           265..269
FT                   /note="'KMSKS' region"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         233
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         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   482 AA;  54367 MW;  5B7F9C2D0433ECFE CRC64;
     MLKIHNSQSK QLEDFTPLTP GQVKMYVCGP TVYNFLHVGN FRGPVVFNMV RNWLEHLGYK
     VTYALNFTDV DDKIINRANE LGMSPTELSE KYIAEYKKDF ASLGLRPHDM NPKVTEHMDD
     IRSMVESLVS QKKAYEAQGD VLYSIESFKD YGKLSGRNTD DLLAGARVEV DEKKRNPMDF
     ALWKAAKPGE VSWPSPWGPG RPGWHIECSA MIKNLFGDQI DIHGGGMDLI FPHHENEIAQ
     SEGCTGKAFV KYWMHNNMLN FGGQKMSKSL GNIVTMREFL EMYNAEIYKW MILSAHYRTL
     SDFGDEAVER AVGGLSRVYS ALSMAESYLT PEVTQEDAAF AKITQDAWKK VEEAMNHDFG
     TPDAFAAMFE VVRQFNAQVR RGMKANPAIQ GKALAFHNFV RKMGSMMSLF QEPAHAFLIK
     LDDMLLKKMN LERSAVDALV AERGEARAAK DFAKSDELRA KITALGISVS DTPEGSFWEV
     TK