ID   CCA_BURCM               Reviewed;         413 AA.
AC   Q0BB41;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Multifunctional CCA protein;
DE   Includes:
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;
DE   Includes:
DE     RecName: Full=2'-nucleotidase;
DE              EC=3.1.3.-;
DE   Includes:
DE     RecName: Full=2',3'-cyclic phosphodiesterase;
DE              EC=3.1.4.-;
DE   Includes:
DE     RecName: Full=Phosphatase;
DE              EC=3.1.3.-;
GN   Name=cca; OrderedLocusNames=Bamb_3076;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. Also shows phosphatase, 2'-
CC       nucleotidase and 2',3'-cyclic phosphodiesterase activities. These
CC       phosphohydrolase activities are probably involved in the repair of
CC       the tRNA 3'-CCA terminus degraded by intracellular RNases (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + tRNA(n) = diphosphate + tRNA(n+1).
CC   -!- CATALYTIC ACTIVITY: CTP + tRNA(n) = diphosphate + tRNA(n+1).
CC   -!- COFACTOR: Magnesium for nucleotidyltransferase activity (By
CC       similarity).
CC   -!- COFACTOR: Nickel for phosphatase activity (By similarity).
CC   -!- SUBUNIT: Monomer. Can also form homodimers and oligomers (By
CC       similarity).
CC   -!- DOMAIN: Comprises two domains: an N-terminal domain containing the
CC       nucleotidyltransferase activity and a C-terminal HD domain
CC       associated with both phosphodiesterase and phosphatase activities
CC       (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 1 subfamily.
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DR   EMBL; CP000440; ABI88632.1; -; Genomic_DNA.
DR   RefSeq; YP_774966.1; -.
DR   GeneID; 4310768; -.
DR   GenomeReviews; CP000440_GR; Bamb_3076.
DR   KEGG; bam:Bamb_3076; -.
DR   NMPDR; fig|339670.3.peg.88; -.
DR   OMA; Q0BB41; KHHGHGQ.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0016151; F:nickel ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; 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_01261; -; 1.
DR   InterPro; IPR012006; CCA_bact.
DR   InterPro; IPR003607; Met-dep_phosphohydro_HD.
DR   InterPro; IPR006674; Met-dep_phosphohydro_HD_sub.
DR   InterPro; IPR002646; PolyA_pol_reg.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   PIRSF; PIRSF000813; CCA_bact; 1.
DR   SMART; SM00471; HDc; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nickel; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA repair; RNA-binding; Transferase;
KW   tRNA processing.
FT   CHAIN         1    413       Multifunctional CCA protein.
FT                                /FTId=PRO_1000054252.
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     143    143       ATP or CTP (By similarity).
FT   BINDING     146    146       ATP or CTP (By similarity).
SQ   SEQUENCE   413 AA;  45516 MW;  CE17C8357BF2506E CRC64;
     MNIYAVGGAI RDDLLGVPVQ DRDYVVVGAT PEQMVAQGFR PVGKDFPVFL HPDTQEEYAL
     ARTERKTAAG YHGFQFYFAP DVTLDEDLAR RDLTINAMAR EVSPEGALVG PVIDPFDGQA
     DLHARVFRHV GDAFVEDPVR ILRIARFAAR FADFTVADDT LALMRRMVDA GEADALVAER
     VWQEIARGLM EAKPSRMFAV LRECGALARV LPEVDALWGV PQRADYHPEV DTGVHVMMVV
     DYAAKQGYSL PVRFAALTHD LGKATTPADV LPRHVGHEGR SVELIKPLCE RLRVPNECRD
     LALVVAREHG NLHRVMEMGA AALVRFFERS DALRKPARFA EMLQACESDA RGRLGLDTQP
     YPQAERLRVA LVAARSVDAG AIARGVGDDV MQIKDAVHRA RVEAVKQALA IGE
//