ID   SYC1_PHOPR              Reviewed;         464 AA.
AC   Q6LT67;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   09-APR-2025, entry version 111.
DE   RecName: Full=Cysteine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00041};
DE            Short=CysRS 1 {ECO:0000255|HAMAP-Rule:MF_00041};
GN   Name=cysS1 {ECO:0000255|HAMAP-Rule:MF_00041};
GN   OrderedLocusNames=PBPRA1098;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Cys) + L-cysteine + ATP = L-cysteinyl-tRNA(Cys) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661, Rhea:RHEA-
CC         COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78517, ChEBI:CHEBI:456215;
CC         EC=6.1.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00041};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         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; CR378666; CAG19509.1; -; Genomic_DNA.
DR   RefSeq; WP_011217842.1; NC_006370.1.
DR   AlphaFoldDB; Q6LT67; -.
DR   SMR; Q6LT67; -.
DR   STRING; 298386.PBPRA1098; -.
DR   KEGG; ppr:PBPRA1098; -.
DR   eggNOG; COG0215; Bacteria.
DR   HOGENOM; CLU_013528_0_1_6; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 1.20.120.1910:FF:000001; Cysteine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000009; Cysteine--tRNA ligase; 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; IPR056411; CysS_C.
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; PF23493; CysS_C; 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; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..464
FT                   /note="Cysteine--tRNA ligase 1"
FT                   /id="PRO_0000159453"
FT   MOTIF           30..40
FT                   /note="'HIGH' region"
FT   MOTIF           266..270
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         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   464 AA;  52294 MW;  5853E76518677407 CRC64;
     MLKIYNSLTK QKEEFKPIQP GKIGMYVCGV TIYDLCHIGH GRTFVSFDVV SRYLRYSGYD
     LTFVRNITDI DDKIIKRAAE NGESCESLTE RLIGEMHKDF DALGMKRPDI EPRATEFIAE
     IIILCERLIE RGFAYVASNG DVMFEVSKFE EYGRLSRQDL DQLQAGARVD IDMAKRSPLD
     FVLWKMSKPG EPTWESPWGA GRPGWHIECS AMNSAILGDH FDIHGGGSDL QFPHHENEIA
     QSCCATGSQY VNTWMHSGMV MVDREKMSKS LGNFFTIRDV LAHYDAESVR YFLMSGHYRS
     QLNYSEDNLK QARSALERLY TSLRGLDLTA QAEGGEEFVT RFTASMNDDF NTPEAYSVLF
     DMAREINRLK ADETIANNIV QASALGARLR ELADILGLLS QDPEAFLQGG AGQDDVAEIE
     TLVQQRLDAR AAKDWAAADA ARDKLLAMKI ILEDGPQGTT WRRK
//