ID   CCA_BUCCC               Reviewed;         414 AA.
AC   Q058D0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   05-MAY-2009, entry version 16.
DE   RecName: Full=CCA-adding enzyme;
DE            EC=2.7.7.25;
DE            EC=2.7.7.21;
DE   AltName: Full=tRNA nucleotidyltransferase;
DE   AltName: Full=tRNA adenylyl-/cytidylyl- transferase;
DE   AltName: Full=tRNA CCA-pyrophosphorylase;
DE   AltName: Full=tRNA-NT;
GN   Name=cca; OrderedLocusNames=BCc_038;
OS   Buchnera aphidicola subsp. Cinara cedri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=372461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17038625; DOI=10.1126/science.1130441;
RA   Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M.,
RA   Michelena J.M., Silva F.J., Moya A., Latorre A.;
RT   "A small microbial genome: the end of a long symbiotic relationship?";
RL   Science 314:312-313(2006).
CC   -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC       terminal CCA sequence in tRNAs without using a nucleic acid
CC       template. Adds these three nucleotides in the order of C, C, and A
CC       to the tRNA nucleotide-73, using CTP and ATP as substrates and
CC       producing inorganic pyrophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + tRNA(n) = diphosphate + tRNA(n+1).
CC   -!- CATALYTIC ACTIVITY: CTP + tRNA(n) = diphosphate + tRNA(n+1).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both
CC       ATP and CTP and is responsible for their addition (By similarity).
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Bacterial CCA-adding enzyme type 2 subfamily.
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DR   EMBL; CP000263; ABJ90519.1; -; Genomic_DNA.
DR   RefSeq; YP_802612.1; -.
DR   GeneID; 4440713; -.
DR   GenomeReviews; CP000263_GR; BCc_038.
DR   KEGG; bcc:BCc_038; -.
DR   OMA; Q058D0; NPHVYFQ.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR   GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:HAMAP.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:HAMAP.
DR   HAMAP; MF_01262; -; 1.
DR   InterPro; IPR012006; CCA_bact.
DR   InterPro; IPR002646; PolyA_pol_reg.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   PIRSF; PIRSF000813; CCA_bact; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA repair; RNA-binding;
KW   Transferase; tRNA processing.
FT   CHAIN         1    414       CCA-adding enzyme.
FT                                /FTId=PRO_1000054315.
FT   METAL        21     21       Magnesium (By similarity).
FT   METAL        23     23       Magnesium (By similarity).
FT   BINDING       8      8       ATP or CTP; via amide nitrogen (By
FT                                similarity).
FT   BINDING      11     11       ATP or CTP (By similarity).
FT   BINDING      92     92       ATP or CTP (By similarity).
FT   BINDING     138    138       ATP or CTP (By similarity).
FT   BINDING     141    141       ATP or CTP (By similarity).
SQ   SEQUENCE   414 AA;  49356 MW;  9627D5C5071E5858 CRC64;
     MKIYLVGGAI RDRLLNIPVR DRDWVVVGIR DPKEMLKKNY QQVGKGFPVF IHPKTHEEYS
     LARTEKKNGV GHTGFLFDFS SRITLKEDLK RRDLTINAIA QDSSGKIIDF FNGKKDIQKK
     ILRHVSYSFQ EDPLRVLRIA RFAALLSHLG FYIAKKTLSL MKLICSRKEL LYLTPERIWK
     ETQKGLSTQN PHVYFQVLYS CNALFFLFPE INYFYKKTYF LNSFIKHINL VQYSLIELSK
     ISKVTKDINI RFSYFLQFFY YVYPIPNIGT KDYFFYKKPA FLLKKMLIRL KIPKETSEII
     FFLCGFHNFL QNINIQSSKL IIKFFNIIDV WRKPNRLNQL IYLDFYNFNS LKNKKNDFFL
     GKLLKYMFSL IKDISVCSFI KEKKFKGIEI KNDLNRLRIQ SFKEMKEKII LNIF
//