ID   SYC2_MYCLE              Reviewed;         412 AA.
AC   Q49784;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Putative cysteinyl-tRNA synthetase 2;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteine--tRNA ligase 2;
DE            Short=CysRS 2;
GN   Name=cysS2; OrderedLocusNames=ML1302; ORFNames=B2126_C2_193;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP +
CC       diphosphate + L-cysteinyl-tRNA(Cys).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17194.1; Type=Frameshift; Positions=Several;
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DR   EMBL; U00017; AAA17194.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL583921; CAC31683.1; ALT_INIT; Genomic_DNA.
DR   PIR; H87071; H87071.
DR   RefSeq; NP_301936.1; -.
DR   HSSP; P21888; 1LI5.
DR   GeneID; 910422; -.
DR   GenomeReviews; AL450380_GR; ML1302.
DR   KEGG; mle:ML1302; -.
DR   NMPDR; fig|272631.1.peg.808; -.
DR   Leproma; ML1302; -.
DR   HOGENOM; Q49784; -.
DR   BioCyc; MLEP272631:ML1302-MON; -.
DR   BRENDA; 6.1.1.16; 808.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00041; atypical; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR015804; Cys-tRNA-synt_Ia_C.
DR   InterPro; IPR015803; Cys-tRNA-synt_Ia_N.
DR   InterPro; IPR017812; Mycothiol_biosynthesis_MshC.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR10890; Cys_tRNA-synt_1a; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   TIGRFAMs; TIGR03447; mycothiol_MshC; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    412       Putative cysteinyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000159438.
FT   MOTIF        46     56       "HIGH" region.
FT   MOTIF       289    293       "KMSKS" region.
FT   BINDING     292    292       ATP (By similarity).
FT   CONFLICT    274    274       A -> AGTTCTLG (in Ref. 1).
FT   CONFLICT    305    305       A -> P (in Ref. 1).
FT   CONFLICT    309    309       P -> R (in Ref. 1).
SQ   SEQUENCE   412 AA;  45293 MW;  48165EF99409A25B CRC64;
     MVFRTGSGVA GRGPELRLYD TSDRQVRPVS AAVAPTCKAT MYVCGITPYD ATHLGHAATY
     LAFDLIHRLW LDLGHEVHYV QNVTDVDDPL FERADRNGVD WRDLAEREVA LFRDDMASLR
     ILPPHDYVAA TETIVEIVEL VDKMLVSGAA YVIDDEYPDI YFRADATLQF GYESGYDRDT
     MLRLYEQSGG DPRRPGKNGE LDALLWRAAR PGEPSWSSPF GPGRPGWHVE CAAIALSRIG
     IGLDIQGGGS DLIFPHHEFT AAHAECVRGE RRFARHYVHA GMIGWDEHKM SKSRGNLVLV
     STLRAQGAPP SAIRLGLLAG HYRADRFWSS QLLDDAIARL HRWRTAASMP AGPDVADVIA
     RVRGYLADDL DTPKAIAALD GWVTDALEYG GHDAAAPKLL ATAIDALLGV DL
//