ID   CCA_ALCBS               Reviewed;         410 AA.
AC   Q0VMU8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=ABO_2052;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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. 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM286690; CAL17500.1; -; Genomic_DNA.
DR   RefSeq; YP_693772.1; -.
DR   GeneID; 4212963; -.
DR   GenomeReviews; AM286690_GR; ABO_2052.
DR   KEGG; abo:ABO_2052; -.
DR   NMPDR; fig|393595.12.peg.2054; -.
DR   HOGENOM; Q0VMU8; -.
DR   OMA; Q0VMU8; KHHGHGQ.
DR   BioCyc; ABOR393595:ABO_2052-MON; -.
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    410       Multifunctional CCA protein.
FT                                /FTId=PRO_1000054246.
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   410 AA;  45874 MW;  6C154B4C7E43D51A CRC64;
     MNVYLVGGAV RDSLLGLPVT EKDWVVVGAT PKEMEANGFR PVGKDFPVFL HPKTQEEYAL
     ARTERKSGHG YGGFTFHAAS TVSLEEDLIR RDLTINAMAQ ARGGEIIDPF NGRVDLKARL
     LRHVSPAFAE DPLRVLRVAR FAARYHWLGF QVADDTLMLM KQLSDSGELG YLVAERVWKE
     TSRALMERDP QVFFQVLHRC GALHALFPEL AALDGVPQPE QHHPEVDTLL HQFLCLKQAA
     RLGLSLNARY ALLCHDLGKG KTPKEEWPRH IAHEIRSARL SKKVSKRLKV PKEAATLATL
     VAEFHTHSHR ALELKPATVW KLFKSLDILR RPERLTDFLG ACEADARGRT SFENREYPQA
     SYLQGAADAA RQVDIQALQA QGHEGPALGE AIEQARIDAI ATFKQQELNP
//