(data stored in SCRATCH zone)

SWISSPROT: C0ZPR9_RHOE4

ID   C0ZPR9_RHOE4            Unreviewed;       464 AA.
AC   C0ZPR9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE            Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN   Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041,
GN   ECO:0000313|EMBL:BAH31397.1};
GN   OrderedLocusNames=RER_06890 {ECO:0000313|EMBL:BAH31397.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31397.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31397.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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:0000256|HAMAP-
CC         Rule:MF_00041, ECO:0000256|SAAS:SAAS01120893};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00041};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00041};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00041}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041,
CC       ECO:0000256|SAAS:SAAS00043683}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00041,
CC       ECO:0000256|SAAS:SAAS01085510}.
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DR   EMBL; AP008957; BAH31397.1; -; Genomic_DNA.
DR   RefSeq; WP_003945830.1; NC_012490.1.
DR   STRING; 234621.RER_06890; -.
DR   EnsemblBacteria; BAH31397; BAH31397; RER_06890.
DR   GeneID; 31540533; -.
DR   KEGG; rer:RER_06890; -.
DR   PATRIC; fig|234621.6.peg.1137; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   Proteomes; UP000002204; 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;
DR   PRODOM; C0ZPR9.
DR   SWISS-2DPAGE; C0ZPR9.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043709, ECO:0000313|EMBL:BAH31397.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043696};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043701};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043689, ECO:0000313|EMBL:BAH31397.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043657};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043715};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00041,
KW   ECO:0000256|SAAS:SAAS00043668};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00041, ECO:0000256|SAAS:SAAS00043692}.
FT   DOMAIN      338    399       DALR_2. {ECO:0000259|SMART:SM00840}.
FT   MOTIF        31     41       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   MOTIF       263    267       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00041}.
FT   METAL        29     29       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       207    207       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       232    232       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   METAL       236    236       Zinc. {ECO:0000256|HAMAP-Rule:MF_00041}.
FT   BINDING     266    266       ATP. {ECO:0000256|HAMAP-Rule:MF_00041}.
SQ   SEQUENCE   464 AA;  50959 MW;  9AA065838ED85F37 CRC64;
     MTLRLYDTGT RALRDFVPLA PGHASVYLCG ATVQGDPHIG HVRSGVAFDV LRRWLLAHGN
     DVAFVRNVTD IDDKILNKAA GAGRPWWEWA ATFERSFTWA YDQLGVLPPS IEPRATGHVT
     QMVEMMERLI ENGHAYAAGG DVYFDVQSYP EYGALSGHKL DDVHQGESAA EGKRDPRDFT
     LWKAVKPGEP SWPTPWGPGR PGWHLECSAM AEFYLGAAFD IHCGGRDLVF PHHENEIAQA
     KCAGDDFAQY WLHNGWVTMS GEKMSKSLGN VLSVPNVLKK VRPQELRYYL GSAHYRSNLE
     YSDEALDESA KSYQGLESFV LRTHKRAGGV ELGTWTEGFA AALDNDLSVP IALAEIHGKA
     SEGNSALAAG DLDAARVAAG QVRAMLAILG VDPLDEHWTQ SGGDTETAME ALDVLVRADL
     DRRQQARTEK NWAVADEVRD RLIKAGIEVT DTPDGPEWSL KAGQ
//

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