CCA_TERTT
ID CCA_TERTT Reviewed; 411 AA.
AC C5BPQ5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Multifunctional CCA protein {ECO:0000255|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01261};
DE EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01261};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=2'-nucleotidase {ECO:0000255|HAMAP-Rule:MF_01261};
DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01261};
DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=Phosphatase {ECO:0000255|HAMAP-Rule:MF_01261};
DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261};
GN Name=cca {ECO:0000255|HAMAP-Rule:MF_01261}; OrderedLocusNames=TERTU_3154;
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901;
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC terminal CCA sequence in tRNAs without using a nucleic acid template.
CC Adds these three nucleotides in the order of C, C, and A to the tRNA
CC nucleotide-73, using CTP and ATP as substrates and producing inorganic
CC pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic
CC phosphodiesterase activities. These phosphohydrolase activities are
CC probably involved in the repair of the tRNA 3'-CCA terminus degraded by
CC intracellular RNases. {ECO:0000255|HAMAP-Rule:MF_01261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3
CC diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC Note=Magnesium is required for nucleotidyltransferase activity.
CC {ECO:0000255|HAMAP-Rule:MF_01261};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC Note=Nickel for phosphatase activity. {ECO:0000255|HAMAP-
CC Rule:MF_01261};
CC -!- SUBUNIT: Monomer. Can also form homodimers and oligomers.
CC {ECO:0000255|HAMAP-Rule:MF_01261}.
CC -!- DOMAIN: Comprises two domains: an N-terminal domain containing the
CC nucleotidyltransferase activity and a C-terminal HD domain associated
CC with both phosphodiesterase and phosphatase activities.
CC {ECO:0000255|HAMAP-Rule:MF_01261}.
CC -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC and CTP and is responsible for their addition. {ECO:0000255|HAMAP-
CC Rule:MF_01261}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01261}.
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DR EMBL; CP001614; ACR14324.1; -; Genomic_DNA.
DR RefSeq; WP_015820440.1; NC_012997.1.
DR AlphaFoldDB; C5BPQ5; -.
DR SMR; C5BPQ5; -.
DR STRING; 377629.TERTU_3154; -.
DR EnsemblBacteria; ACR14324; ACR14324; TERTU_3154.
DR KEGG; ttu:TERTU_3154; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_1_1_6; -.
DR OMA; GWTFHGH; -.
DR OrthoDB; 2018439at2; -.
DR Proteomes; UP000009080; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_01261; CCA_bact_type1; 1.
DR HAMAP; MF_01262; CCA_bact_type2; 1.
DR InterPro; IPR012006; CCA_bact.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR PIRSF; PIRSF000813; CCA_bact; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nickel; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW RNA repair; RNA-binding; Transferase; tRNA processing.
FT CHAIN 1..411
FT /note="Multifunctional CCA protein"
FT /id="PRO_1000214134"
FT DOMAIN 228..329
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 8
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 11
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 91
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 137
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 140
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
SQ SEQUENCE 411 AA; 46409 MW; DD336A21ACACBF97 CRC64;
MKIYLVGGAV RDQLLGYPHH EQDWVVVGAT PQQMLDAGFK PVGKDFPVFL HPETQEEYAL
ARQERKTAPG YTGFAFHADE TVTLEQDLLR RDLTINAIAM DEEGTIIDPY NGKRDIETRT
LRHVSQAFCE DPVRILRIAR FAARYHHLGF RIAPETLALM RDMVQAGEVD HLVAERVWKE
LSRALEEQHP AIFIQTLREC GALHRLMPEL NALFGIPQPE AHHPEVDTGV HALLALERAC
ELSSTPEVRF AALIHDLGKG VTPKHLWPSH HGHEQDGVAL VEQLCNRLST PNQFRELAVA
VCAYHTHCHR AFELNAKTLL KTLLALDGLR RPERFQQFCL CCQADAQGRT GLENRPYPQA
AYFLQALEEI QKVDAKMFVA QGKKGAEIGE AMYSARLQKI KLLKTAQTPH E
