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Database: UniProt/TrEMBL
Entry: E4TEJ4_CALNY
LinkDB: E4TEJ4_CALNY
Original site: E4TEJ4_CALNY 
ID   E4TEJ4_CALNY            Unreviewed;       479 AA.
AC   E4TEJ4;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   01-MAY-2013, entry version 19.
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
GN   Name=cysS; OrderedLocusNames=Calni_0407;
OS   Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 /
OS   Yu37-1).
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae.
OX   NCBI_TaxID=768670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19672;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA   Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Calditerrivibrio nitroreducens
RT   DSM 19672.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19672 / NBRC 101217 / Yu37-1;
RX   PubMed=21475587; DOI=10.4056/sigs.1523807;
RA   Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Land M.;
RT   "Complete genome sequence of Calditerrivibrio nitroreducens type
RT   strain (Yu37-1).";
RL   Stand. Genomic Sci. 4:54-62(2011).
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; CP002347; ADR18320.1; -; Genomic_DNA.
DR   RefSeq; YP_004050483.1; NC_014758.1.
DR   ProteinModelPortal; E4TEJ4; -.
DR   EnsemblBacteria; ADR18320; ADR18320; Calni_0407.
DR   GeneID; 10008414; -.
DR   KEGG; cni:Calni_0407; -.
DR   PATRIC; 45188508; VBICalNit163602_0473.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; DFDALNM; -.
DR   BioCyc; CNIT768670:GHD1-416-MONOMER; -.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_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; 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        30     40       "HIGH" region (By similarity).
FT   MOTIF       265    269       "KMSKS" region (By similarity).
FT   METAL        28     28       Zinc (By similarity).
FT   METAL       208    208       Zinc (By similarity).
FT   METAL       233    233       Zinc (By similarity).
FT   METAL       237    237       Zinc (By similarity).
FT   BINDING     268    268       ATP (By similarity).
SQ   SEQUENCE   479 AA;  55363 MW;  1984E8F34C796789 CRC64;
     MLKIFNTLSG EKEVFTPLED NKVKIYVCGV TVYDYCHIGH ARSSIVFDTI RRYLKYKGFD
     VTFVKNFTDV DDKIIKRANE ENKSINEITD FFIKAHDEDM DKLNILRPDY TPRATEYIDG
     MIKLCEKLIE KGFAYESNGD VYFKVRAFKD YGKLSKRDLD DLLAGARVDV NEIKEDPLDF
     ALWKRSKEGE PGWDSPWGRG RPGWHIECSV MSAEILGIPF DIHGGGKDLI FPHHENEIAQ
     SEAAEGKEFA RYWIHNGFVN INKEKMSKSL GNFFTIRDVL KEVDPEVLRF FLLTTHYRSP
     LDFSFENLLE AENALDRIYT AIDELESAVF NNKKPAQKGK IDEIVDRFKR DFEESMDDDF
     NTASAISNIF ELIKGVNLLL SERLNSEDLN YLKVRFEEVK AIIRDVLGIL TKTASEWFKM
     NLSIDESELQ KLIEEREIAR RNKDFSKADA IRNELKTKGV ELLDTPTGTK FRAKRLRGG
//
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