ID   SYCM_BOVIN              Reviewed;         555 AA.
AC   Q2KIF8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Cysteinyl-tRNA synthetase, mitochondrial;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteine--tRNA ligase;
DE            Short=CysRS;
DE   Flags: Precursor;
GN   Name=CARS2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; BC112654; AAI12655.1; -; mRNA.
DR   IPI; IPI00713506; -.
DR   RefSeq; NP_001039409.1; -.
DR   UniGene; Bt.21918; -.
DR   Ensembl; ENSBTAG00000011471; Bos taurus.
DR   GeneID; 506598; -.
DR   KEGG; bta:506598; -.
DR   HOVERGEN; Q2KIF8; -.
DR   BRENDA; 6.1.1.16; 251.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
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; Ligase; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Transit peptide; Zinc.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    555       Cysteinyl-tRNA synthetase, mitochondrial.
FT                                /FTId=PRO_0000250740.
FT   MOTIF        72     82       "HIGH" region.
FT   MOTIF       309    313       "KMSKS" region.
FT   METAL        70     70       Zinc (By similarity).
FT   METAL       249    249       Zinc (By similarity).
FT   METAL       274    274       Zinc (By similarity).
FT   METAL       278    278       Zinc (By similarity).
FT   BINDING     312    312       ATP (By similarity).
SQ   SEQUENCE   555 AA;  61199 MW;  A55CD4CABBCCF9F7 CRC64;
     MLWTRRACGG AWLLRAARGP EPGRSASGAR GQGWLQPTGY DTGVKVYNSL TRRKDPLIVS
     RADAASWYSC GPTVYDHAHL GHACSYVRFD IIRRILSRVF GCTVVMVMGI TDVDDKIIRR
     ANEMSVSPAS LARLYEEDFK QDMAALKVLP PTAYLRVTEH VPQIVAFIER LIANGHAYCT
     AKGNVYFDLQ SRGDRYGKLV GVAPGPVGEP VDSDKRHTSD FALWKAAKPQ EPFWGSPWGD
     GRPGWHIECS TIASLVFGSQ LDIHSGGVDL AFPHHENEIA QCEAFHQCPQ WGNYFLHSGH
     LHVKGGGEKM SKSLKNYVTI KDFLRSTSPD VFRLFCLRSS YRSAIDYSEG ALLEARSLLR
     ATAAFVEDAR AYLRGQLAGG PIQEDVLWER LGRTKAAVQA ALADDFDTVR AVDAVMDLVH
     HGNRQLKAAS EEPRGPRSPA VLGAVVASVE HFFETVGVSL AERQCVPGAG SPAALYSLVE
     ELVRFRLKVR QFALASGEAP GEARRQRLLE RQPLLEACDA LRRDLAVHGI SIKDRSGSST
     WELLDPRTED PKPRS
//