ID   CCA_HAHCH               Reviewed;         422 AA.
AC   Q2SM94;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=HCH_01366;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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. 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; CP000155; ABC28230.1; -; Genomic_DNA.
DR   RefSeq; YP_432655.1; -.
DR   GeneID; 3838951; -.
DR   GenomeReviews; CP000155_GR; HCH_01366.
DR   KEGG; hch:HCH_01366; -.
DR   NMPDR; fig|349521.5.peg.1235; -.
DR   HOGENOM; Q2SM94; -.
DR   OMA; Q2SM94; KHHGHGQ.
DR   BioCyc; HCHE349521:HCH_01366-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    422       Multifunctional CCA protein.
FT                                /FTId=PRO_1000054268.
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   422 AA;  47649 MW;  6099690A60677542 CRC64;
     MQRYLVGGAV RDALLGLPVK DRDWVVVGAT PEQMLDQGYQ QVGADFPVFL HPESKEEHAL
     ARTERKSGKG YTGFICDFSP DISLEDDLLR RDLTINAMAM DDDGNLVDPF NGRQDLEARI
     LRHVSPAFTE DPLRVLRVAR FASRYADLGF TVAPETLQLM QDIQASGELK ALTAERVWQE
     TVRALGQKQP RVYFQVLKDA HALQDIFPEL NALFGVPQTP QYHPEVDTGL HSLMALEQAC
     LLSEREEVRF AALIHDLGKG VTPQEEWPKH HNHEAVGVDL VKALTERVKA PKLFKELALM
     ACQYHTHCHR ALELRANTLV KLLQSCDAWR RPDRFELFLL ACEADARGRT GWEQKPYPQA
     DFLRGVLETC QQIQPQELVA QGYTGARLGE EIQRRRISAV KRFKQDNAPE AQEKGGEDVG
     LT
//