CCA_AERHY
ID CCA_AERHY Reviewed; 192 AA.
AC P45749;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=CCA-adding enzyme;
DE EC=2.7.7.72;
DE AltName: Full=CCA tRNA nucleotidyltransferase;
DE AltName: Full=tRNA CCA-pyrophosphorylase;
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase;
DE AltName: Full=tRNA nucleotidyltransferase;
DE AltName: Full=tRNA-NT;
DE Flags: Fragment;
GN Name=cca;
OS Aeromonas hydrophila.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=644;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ah65;
RX PubMed=7961440; DOI=10.1128/jb.176.22.6819-6826.1994;
RA Jahagirdar R., Howard S.P.;
RT "Isolation and characterization of a second exe operon required for
RT extracellular protein secretion in Aeromonas hydrophila.";
RL J. Bacteriol. 176:6819-6826(1994).
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC and CTP and is responsible for their addition. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Bacterial CCA-adding enzyme type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; X81473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P45749; -.
DR SMR; P45749; -.
DR STRING; 1448139.AI20_00285; -.
DR eggNOG; COG0617; Bacteria.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; RNA repair; RNA-binding; Transferase;
KW tRNA processing.
FT CHAIN 1..>192
FT /note="CCA-adding enzyme"
FT /id="PRO_0000139013"
FT BINDING 8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 8
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 11
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 91
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 137
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT BINDING 140
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT NON_TER 192
SQ SEQUENCE 192 AA; 21633 MW; C0A885DF0B6835DD CRC64;
MQTYLVGGAV RDRLLGLPQG DRDHLVVGAT VEQMLALGFT QVGRDFPVFL HPKTQQEYAL
ARTERKQGRG YTGFVCHASP EVTLEQDLLR RDLTVNAIAE DEEGRLHDPY GGIQDLERRV
LRHVSPAFAE DPLRILRVAR FAARFHAQGF VVAPETLALM REMTDAGELA HLTPERVWKE
LERVLLGETP QI
