ID   CCA_BORBR               Reviewed;         364 AA.
AC   Q7U391;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=BB0207;
OS   Bordetella bronchiseptica (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB50 / ATCC BAA-588 / NCTC 13252;
RX   MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640437; CAE30705.1; -; Genomic_DNA.
DR   RefSeq; NP_886756.1; -.
DR   GeneID; 2662352; -.
DR   GenomeReviews; BX470250_GR; BB0207.
DR   KEGG; bbr:BB0207; -.
DR   NMPDR; fig|257310.1.peg.203; -.
DR   HOGENOM; Q7U391; -.
DR   OMA; Q7U391; ARQCAGD.
DR   BioCyc; BBRO257310:BB0207-MON; -.
DR   BRENDA; 2.7.7.21; 413.
DR   BRENDA; 2.7.7.25; 413.
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    364       CCA-adding enzyme.
FT                                /FTId=PRO_0000139014.
FT   METAL        32     32       Magnesium (By similarity).
FT   METAL        34     34       Magnesium (By similarity).
FT   BINDING      19     19       ATP or CTP; via amide nitrogen (By
FT                                similarity).
FT   BINDING      22     22       ATP or CTP (By similarity).
FT   BINDING     102    102       ATP or CTP (By similarity).
FT   BINDING     148    148       ATP or CTP (By similarity).
FT   BINDING     151    151       ATP or CTP (By similarity).
SQ   SEQUENCE   364 AA;  39281 MW;  FEF8DF92C5A9C4F3 CRC64;
     MSRADDPGVA GLQVYIVGGA VRDGLLGLPA GDRDWVVVGA TPEDMARRGF IPVGGDFPVF
     LHPRTKEEYA LARTERKSGR GYKGFTFYTG ADVTLEQDLQ RRDLTVNAIA RTPQGELVDP
     LDGVADVRAR VLRHVGEAFA EDPVRILRLG RFAARFGDFS IAPETMQLCR RMVEAGEADA
     LVPERVWKEV SRGLMAQAPS RMLDVLARAG ALARVMPELH DDAAVRAEID RAAAAGLPLA
     GRYALLCRHT PERDALGRRL RAPVECMDQA RLLPLAVDAL AASATPAAQL DLIERCDALR
     KPERFDALLQ AAAIVAPVDL SAWRARVQAV RAIDAGAIAR QCAGDPARIK PALRQARLQA
     LGGA
//