ID   D1CIB0_THET1            Unreviewed;       785 AA.
AC   D1CIB0;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   01-MAY-2013, entry version 23.
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
GN   Name=cysS; OrderedLocusNames=Tter_2592;
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1;
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP +
CC       diphosphate + L-cysteinyl-tRNA(Cys).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP001826; ACZ43481.1; -; Genomic_DNA.
DR   RefSeq; YP_003324303.1; NC_013526.1.
DR   ProteinModelPortal; D1CIB0; -.
DR   EnsemblBacteria; ACZ43481; ACZ43481; Tter_2592.
DR   GeneID; 8640621; -.
DR   KEGG; ttr:Tter_2592; -.
DR   PATRIC; 32505611; VBITheTer68767_2765.
DR   KO; K01883; -.
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:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:HAMAP.
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; IPR001173; Glyco_trans_2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; tRNAsyn_1a_bind; 1.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   MOTIF        29     39       "HIGH" region (By similarity).
FT   MOTIF       275    279       "KMSKS" region (By similarity).
FT   METAL        27     27       Zinc (By similarity).
FT   METAL       218    218       Zinc (By similarity).
FT   METAL       243    243       Zinc (By similarity).
FT   METAL       247    247       Zinc (By similarity).
FT   BINDING     278    278       ATP (By similarity).
SQ   SEQUENCE   785 AA;  90295 MW;  A317A2BF0D277457 CRC64;
     MRLYNTLTRR VEEVVPVEPG RIRMYTCGPT VYRYIHIGNL RSFCTADWIR RALLREGYEV
     IHVKNITDVG HMRQELLDQG EDKLEAEARR VGRTPGEIAE FYTRAFMRDE ARMNILPASV
     FPRATQHVGE MIEIVRELER QGYAYRAGGN VYFDVARLPQ YGQLSGNSLP ELTSSQEDAT
     ADKRSPLDFA LWKEAEPGRL MAWDSPWGRG FPGWHIECTA MAIKYLGTEI DIHTGGVDNI
     FPHHENERAQ SEAYVGHRWV RHWVHTQHLL TDGLKMSKSM SNDYTLDDIV ARGFEPLALR
     YLFTTAHYRT RLNFTFRALA GAQTSLRRLR MAALAARDEA VAPPDEEAMR PWREAFDRSL
     RDDLNLPAAM AVVWDVVRRS GLGPAERAAL LAEFDEVLGL DVFAEPDSGL LLEPRQDVRE
     LLALRAEVRA RGDYALADAL RSDLEARGVE LRDTRQGTRA YRLRINRLPH VFTSSAEVPS
     RVGEPDRYEW SVNLIARNNR EDLERCLRSL ARHLHGRSLE VVVVDSGSTD DTLGLMLELY
     HRGYWEEEGV RVPLKVLFAD HNIGFAASRN ATMRASEGWY VVWLDTSVEL AGDVWTPLEE
     ALADRSVGVA GPFGLVTEDL REFERTPGPD ADAMEGYLFA FRRALLEEVG LLDNEKFRFY
     RLADVYYSFF FKAAGLRVVV VPEVERRIIL HPHREWYSLL PEERQTKSKH NYDLFRARWH
     HGESLLVARD GQVERWLEHD HPRHVDADHF HPPEELPPPG VPHVHPHRHL PDHQHNHPHY
     HFQGD
//