ID   SYC_ANAPZ               Reviewed;         462 AA.
AC   Q2GKF4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Cysteinyl-tRNA synthetase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteine--tRNA ligase;
DE            Short=CysRS;
GN   Name=cysS; OrderedLocusNames=APH_0555;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000235; ABD43506.1; -; Genomic_DNA.
DR   RefSeq; YP_505147.1; -.
DR   GeneID; 3930041; -.
DR   GenomeReviews; CP000235_GR; APH_0555.
DR   KEGG; aph:APH_0555; -.
DR   NMPDR; fig|212042.5.peg.547; -.
DR   TIGR; APH_0555; -.
DR   HOGENOM; Q2GKF4; -.
DR   OMA; Q2GKF4; VLWKAAK.
DR   BioCyc; APHA212042:APH_0555-MON; -.
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:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00041; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR015804; Cys-tRNA-synt_Ia_C.
DR   InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR   InterPro; IPR015803; Cys-tRNA-synt_Ia_N.
DR   InterPro; IPR002308; Cys-tRNA-synth_1a.
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; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   TIGRFAMs; TIGR00435; cysS; 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; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    462       Cysteinyl-tRNA synthetase.
FT                                /FTId=PRO_0000240888.
FT   MOTIF        29     39       "HIGH" region.
FT   MOTIF       270    274       "KMSKS" region.
FT   METAL        27     27       Zinc (By similarity).
FT   METAL       211    211       Zinc (By similarity).
FT   METAL       236    236       Zinc (By similarity).
FT   METAL       240    240       Zinc (By similarity).
FT   BINDING     273    273       ATP (By similarity).
SQ   SEQUENCE   462 AA;  51808 MW;  E015BBC0EEA9D2DD CRC64;
     MKLYDTFSAA KRVFDPIDSA CVKIYACGPT VYDLAHIGNA RSAVVYDVLF RLLRELYPEV
     IYVRNITDVD DKIINAAAET GQNIGDFTER YIRYFHEDMD ALNCLSPTVE PRATAEIDTM
     LQLISRLVES GHAYVKGGSV YFSISSHRHY GRLSGRKIDE MISGNRVSID AEKLHPGDFV
     LWKPATEQDI KLGAAWESPW GGGRPGWHIE CSAMSYRYLG ESFDIHGGGA DLMFPHHENE
     LAQNMCAFSG SEYARYWVHN GFLTVNAGEK MSKSLGNVIT VRGLRNSGIE GAVIRYVFLC
     THYRKPLDWN EKAIFDAQSA LSKMRRSCEE FTSEELNSDI EAVGVHNMLL EALKDDMNTP
     MAIAALHALV GEINKTTDFK ERLKLARVLN RSAKLMGITD GFAGKSAEEA VDVDKIQELL
     ERRREARNGG NYSLADEIRD QLHSMGIVIK DDKDGVTRWS RA
//