ID   CCA_BLOPB               Reviewed;         408 AA.
AC   Q493X4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=BPEN_064;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40710.1; -; Genomic_DNA.
DR   RefSeq; YP_277582.1; -.
DR   GeneID; 3563148; -.
DR   GenomeReviews; CP000016_GR; BPEN_064.
DR   KEGG; bpn:BPEN_064; -.
DR   HOGENOM; Q493X4; -.
DR   OMA; Q493X4; KHHGHGQ.
DR   BioCyc; CBLO291272:BPEN_064-MON; -.
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    408       CCA-adding enzyme.
FT                                /FTId=PRO_1000054314.
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      91     91       ATP or CTP (By similarity).
FT   BINDING     137    137       ATP or CTP (By similarity).
FT   BINDING     140    140       ATP or CTP (By similarity).
SQ   SEQUENCE   408 AA;  47442 MW;  54C5EDA653982A08 CRC64;
     MEKYLVGGAV RDALLKLPVQ EKDWVVVGSS PQEMLNIGYE QVGKDFPVFL HPESHEEYAL
     ARTERKSGQG YTGFICHTAP SITIEEDLYR RDLTINAMAY DSHGNLIDPY HGQRDIKLRL
     LRHVSHTFHE DPLRVLRVAR FAARFAHMNF AIAPETLILM KQMIHELLSL SPERIWTETK
     KALITDNPQV YFTVLRHCGA LKILFPELDA LFDIPTPTQY CTKINTGYYT MTTLSKAAYL
     TDDISVRFSV LCRDLGKGIP LNKINKNTKH HDHRKLGITL IHNLCNRFKI PHEIRNFSKI
     TSEYHDYLYN VKILKPEMLM TLFHVFDCWR RPNRIDQIIL VSQSDPIRWK NYNNYSLNQE
     NLLRTAFTVT KKISTVDIIK DGFTGSNISR ELYARRLHAL NSWKNKQI
//