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Multifunctional CCA protein [Includes: CCA-adding enzyme (EC 2.7.7.72) (tRNA CCA-pyrophosphorylase) (tRNA nucleotidyltransferase) (tRNA-NT) (tRNA adenylyl-/cytidylyl-transferase) (CCA tRNA nucleotidyltransferase); Phosphatase (EC 3.1.3.-); 2',3'-cyclic phosphodiesterase (EC 3.1.4.-); 2'-nucleotidase]

 A0A1D2QR37_9GAMM        Unreviewed;       420 AA.
A0A1D2QR37;
30-NOV-2016, integrated into UniProtKB/TrEMBL.
30-NOV-2016, sequence version 1.
22-NOV-2017, entry version 12.
RecName: Full=Multifunctional CCA protein {ECO:0000256|HAMAP-Rule:MF_01261};
Includes:
RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_01261};
EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_01261};
Includes:
RecName: Full=2'-nucleotidase {ECO:0000256|HAMAP-Rule:MF_01261};
EC=3.1.3.- {ECO:0000256|HAMAP-Rule:MF_01261};
Includes:
RecName: Full=Phosphatase {ECO:0000256|HAMAP-Rule:MF_01261};
Includes:
RecName: Full=CCA-adding enzyme {ECO:0000256|HAMAP-Rule:MF_01261};
EC=2.7.7.72 {ECO:0000256|HAMAP-Rule:MF_01261};
AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261};
AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01261};
AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261};
AltName: Full=tRNA-NT {ECO:0000256|HAMAP-Rule:MF_01261};
AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000256|HAMAP-Rule:MF_01261};
Name=cca {ECO:0000256|HAMAP-Rule:MF_01261};
ORFNames=AB835_05840 {ECO:0000313|EMBL:ODS24042.1};
Candidatus Endobugula sertula (Bugula neritina bacterial symbiont).
Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
Cellvibrionaceae; Candidatus Endobugula.
NCBI_TaxID=62101 {ECO:0000313|EMBL:ODS24042.1};
[1] {ECO:0000313|EMBL:ODS24042.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AB1-4 {ECO:0000313|EMBL:ODS24042.1};
PubMed=27590822;
Miller I.J., Vanee N., Fong S.S., Lim-Fong G.E., Kwan J.C.;
"Lack of overt genome reduction in the bryostatin-producing bryozoan
symbiont, 'Candidatus Endobugula sertula'.";
Appl. Environ. Microbiol. 0:0-0(2016).
-!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
terminal CCA sequence in tRNAs without using a nucleic acid
template. Adds these three nucleotides in the order of C, C, and A
to the tRNA nucleotide-73, using CTP and ATP as substrates and
producing inorganic pyrophosphate. Also shows phosphatase, 2'-
nucleotidase and 2',3'-cyclic phosphodiesterase activities. These
phosphohydrolase activities are probably involved in the repair of
the tRNA 3'-CCA terminus degraded by intracellular RNases.
{ECO:0000256|SAAS:SAAS00858833}.
-!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a
3' CCA end + 3 diphosphate. {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00415332}.
-!- SUBUNIT: Monomer. Can also form homodimers and oligomers.
{ECO:0000256|HAMAP-Rule:MF_01261, ECO:0000256|SAAS:SAAS00534155}.
-!- DOMAIN: Comprises two domains: an N-terminal domain containing the
nucleotidyltransferase activity and a C-terminal HD domain
associated with both phosphodiesterase and phosphatase activities.
{ECO:0000256|HAMAP-Rule:MF_01261}.
-!- MISCELLANEOUS: A single active site specifically recognizes both
ATP and CTP and is responsible for their addition.
{ECO:0000256|HAMAP-Rule:MF_01261}.
-!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
{ECO:0000256|SAAS:SAAS00534164}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ODS24042.1}.
-----------------------------------------------------------------------
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EMBL; MDLC01000015; ODS24042.1; -; Genomic_DNA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-UniRule.
CDD; cd00077; HDc; 1.
CDD; cd05398; NT_ClassII-CCAase; 1.
HAMAP; MF_01261; CCA_bact_type1; 1.
HAMAP; MF_01262; CCA_bact_type2; 1.
InterPro; IPR012006; CCA_bact.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR006674; HD_domain.
InterPro; IPR002646; PolA_pol_head_dom.
InterPro; IPR032828; PolyA_RNA-bd.
Pfam; PF01966; HD; 1.
Pfam; PF01743; PolyA_pol; 1.
Pfam; PF12627; PolyA_pol_RNAbd; 1.
PIRSF; PIRSF000813; CCA_bact; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00415369};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00534220};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00820053};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00820061};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00534173};
Nickel {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00534156};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00415369};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00415426};
RNA repair {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00820060};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00415356};
Transferase {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00415426};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_01261,
ECO:0000256|SAAS:SAAS00820063}.
DOMAIN 11 130 PolyA_pol. {ECO:0000259|Pfam:PF01743}.
DOMAIN 157 219 PolyA_pol_RNAbd.
{ECO:0000259|Pfam:PF12627}.
DOMAIN 237 335 HD_domain. {ECO:0000259|Pfam:PF01966}.
METAL 29 29 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01261}.
METAL 31 31 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01261}.
BINDING 16 16 ATP or CTP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01261}.
BINDING 19 19 ATP or CTP. {ECO:0000256|HAMAP-
Rule:MF_01261}.
BINDING 99 99 ATP or CTP. {ECO:0000256|HAMAP-
Rule:MF_01261}.
BINDING 145 145 ATP or CTP. {ECO:0000256|HAMAP-
Rule:MF_01261}.
BINDING 148 148 ATP or CTP. {ECO:0000256|HAMAP-
Rule:MF_01261}.
SEQUENCE 420 AA; 48075 MW; 4851FA439DA792FC CRC64;
MENIQNTGVQ AYLVGGAVRD KLLGRPVADH DWVVIGATPE MLIEQGYQQI GNDFPCFLHP
ETKDEYALAR TERKSGKGHT GFVCDFSPEV TLEEDLSRRD LTINAIALTL EGKYVDPFNG
RADLNNKVLR HVSESFSDDP LRVLRVARFA ARYATLDFQV HPNTLELMKH LVNNGELAEL
TPERVWKEMS RALTEPRPSE FFRVLRACGA LEVLMPELDC LFGVPQPPQH HPEVDTGDHV
MMVVDIARER FDDLIVTWAA LMHDLGKGLT PEEEWPRHIR HEIKGVPLVE KVCECYKVPK
DFRTLAKLVS EHHLRCHKLL EMRPKSVLKL LEALDGFRRP ERVRYFAQAC EADARGRLGL
EQRDYPQSQL LIEYNQVAID TNIKPLLSEG YEGLKLAEKI RRLRLGSIKR YMAQYKIAPQ


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