(data stored in SCRATCH3701 zone)

SWISSPROT: SYC_RICTY

ID   SYC_RICTY               Reviewed;         457 AA.
AC   Q68XV4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 91.
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=RT0051;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(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}.
DR   EMBL; AE017197; AAU03538.1; -; Genomic_DNA.
DR   RefSeq; WP_011190525.1; NC_006142.1.
DR   SMR; Q68XV4; -.
DR   STRING; 257363.RT0051; -.
DR   PRIDE; Q68XV4; -.
DR   EnsemblBacteria; AAU03538; AAU03538; RT0051.
DR   KEGG; rty:RT0051; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   OrthoDB; 952207at2; -.
DR   BioCyc; RTYP257363:G1G0L-52-MONOMER; -.
DR   Proteomes; UP000000604; 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; 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;
DR   PRODOM; Q68XV4.
DR   SWISS-2DPAGE; Q68XV4.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN           1..457
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159470"
FT   MOTIF           31..41
FT                   /note="'HIGH' region"
FT   MOTIF           272..276
FT                   /note="'KMSKS' region"
FT   METAL           29
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   METAL           214
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   METAL           239
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   METAL           243
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
FT   BINDING         275
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00041"
SQ   SEQUENCE   457 AA;  53143 MW;  22BBA46DE77D5384 CRC64;
     MQLHLYNTLT RTKEVFNPQD HANVKMYVCG PTVYDNPHIG NSRSVVVYDL LYRIIIKIFG
     KKAVKYVRNI TDIDDKIIDR AESLGININD LTNKVTREFH INMAYLGCML PSIEPKATEH
     IDVMIEIIER LIAQDHAYIT DNHVYFDVLS APNYTELSNR NLEEMFEGVR IENSKTKKNP
     QDFVLWKPAK QNEPKNVNFS SPWGLGRPGW HIECSAMSYK YLGENFDIHG GGADLIFPHH
     TNEIAQSRCA FPSSTYAKYW IHNGFLTVNG EKMSKSLGNF ITVRDLMDKQ IQGEVVRLFL
     LSSHYRRPLD YNDKAIDDAK KTLDYWYRAI KEINVQKVDL PSDFMQSLFD DMNTPLAIKI
     INDYAKGVFI SKTEAERKFN ASAIITCANF IGLMRKTQYE WFNNDIDKLY INELINKRLK
     AKKQKNWLLA DKIRNQLLEK KIILEDKSDC TTIWRKE
//

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