CCA_CUPMC
ID CCA_CUPMC Reviewed; 414 AA.
AC Q1LS11;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Rmet_0179;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF07065.1; -; Genomic_DNA.
DR RefSeq; WP_011515088.1; NC_007973.1.
DR AlphaFoldDB; Q1LS11; -.
DR SMR; Q1LS11; -.
DR STRING; 266264.Rmet_0179; -.
DR EnsemblBacteria; ABF07065; ABF07065; Rmet_0179.
DR KEGG; rme:Rmet_0179; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_1_1_4; -.
DR OMA; GWTFHGH; -.
DR OrthoDB; 2018439at2; -.
DR Proteomes; UP000002429; 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 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..414
FT /note="Multifunctional CCA protein"
FT /id="PRO_1000054290"
FT DOMAIN 232..333
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 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 143
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT BINDING 146
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
SQ SEQUENCE 414 AA; 45494 MW; 3386A3BF95AC6D36 CRC64;
MQVYAVGGAV RDQLLGKPSQ DRDYVVVGAT PADMEAAGFK PVGKDFPVFL HPHTKAEYAL
ARTERKTAVG YKGFAFYTGA DVTLEEDLVR RDLTINAMAQ AVDEHDNLVG PVIDPYGGQK
DLAARKFRHV SDAFAEDPVR ILRVARFAAR FHEFTVAPET VALMRKIVDA GEVDALVPER
VWQELSRGLM EAKPSRMFDV LRECGALAHL LPELDRLWGV PQRPEYHPEV DTGVHVMMVI
DYAASVGASL PVRFAAMAHD LGKGTTPEDM LPRHIGHEQR GVKLLEAICQ RLRVPNDCRE
LALVVAREHG NIHRSTEFGA AALTRLVERC DALRKPERFA EALLACEADA RGRLGFADKD
YPQADRLLAA RDAAASVDAG AIAKACGDKV DQIKDRVHKA RVAAVAQRLG MAEE
