ID   SYCC_MACFA              Reviewed;         748 AA.
AC   Q4R550;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Cysteinyl-tRNA synthetase, cytoplasmic;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteine--tRNA ligase;
DE            Short=CysRS;
GN   Name=CARS; ORFNames=QccE-19031;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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DR   EMBL; AB169694; BAE01775.1; -; mRNA.
DR   HOVERGEN; Q4R550; -.
DR   BRENDA; 6.1.1.16; 3438.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; ISS:UniProtKB.
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; 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; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   TIGRFAMs; TIGR00435; cysS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis; Zinc.
FT   CHAIN         1    748       Cysteinyl-tRNA synthetase, cytoplasmic.
FT                                /FTId=PRO_0000250744.
FT   MOTIF        57     67       "HIGH" region.
FT   MOTIF       406    410       "KMSKS" region.
FT   METAL        55     55       Zinc (By similarity).
FT   METAL       348    348       Zinc (By similarity).
FT   METAL       373    373       Zinc (By similarity).
FT   METAL       377    377       Zinc (By similarity).
FT   BINDING     409    409       ATP (By similarity).
FT   MOD_RES     260    260       Phosphotyrosine (By similarity).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
SQ   SEQUENCE   748 AA;  85452 MW;  8809DBB18338B7CF CRC64;
     MAGSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV TWYCCGPTVY
     DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD KIIKRARQNH LFEQYLEKRP
     EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ MLERIQHEVQ LATEPLEKAV QSRLTGEEVN
     SCVEVLLEEA KDLLSDWLDS TLGSDVTDNS IFSKLPKFWE GEFHRDMEAL NVLPPDVLTR
     VSEYVPEIVN FVQKIVDNGY GYVSDGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG
     EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA MAGTLLGASM
     DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL TITGCKMSKS LKNFITIKDA
     LKKHSARQLR LAFLMHSWKD TLDYSSNTME SALQYEKFLN EFFLNVKDIL RAPVDITGQF
     EKWGEEEAEL NKNFYDKKTA IHEALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAMRKRPN
     RALLENIALY LTHMLKIFGA IEEESSLGFP VGGSGTSLNL ESTVMPYLQV LSEFREGVRK
     IAREQKVPEV LQLSDALRDD ILPELGVRFE DPEGLPTVVK LVDRNTLLKE REEKRQVEEE
     KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK FDENGLPTHD AEGKELSKGQ
     AKKVKKLFEA QEKLYKEYLQ MPQNGSFQ
//