CCA_HAMD5
ID CCA_HAMD5 Reviewed; 405 AA.
AC C4K6G4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01262};
DE EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01262};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01262};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01262};
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000255|HAMAP-Rule:MF_01262};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01262};
DE AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01262};
GN Name=cca {ECO:0000255|HAMAP-Rule:MF_01262}; OrderedLocusNames=HDEF_1538;
OS Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX NCBI_TaxID=572265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5AT;
RX PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT "Hamiltonella defensa, genome evolution of protective bacterial
RT endosymbiont from pathogenic ancestors.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(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. {ECO:0000255|HAMAP-Rule:MF_01262}.
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_01262};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01262};
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_01262}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Bacterial CCA-adding enzyme type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01262}.
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DR EMBL; CP001277; ACQ68157.1; -; Genomic_DNA.
DR RefSeq; WP_015873925.1; NC_012751.1.
DR AlphaFoldDB; C4K6G4; -.
DR SMR; C4K6G4; -.
DR STRING; 572265.HDEF_1538; -.
DR EnsemblBacteria; ACQ68157; ACQ68157; HDEF_1538.
DR GeneID; 66261182; -.
DR KEGG; hde:HDEF_1538; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_1_1_6; -.
DR OMA; GWTFHGH; -.
DR Proteomes; UP000002334; 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:0000287; F:magnesium ion binding; 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; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_01262; CCA_bact_type2; 1.
DR InterPro; IPR012006; CCA_bact.
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; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding;
KW Transferase; tRNA processing.
FT CHAIN 1..405
FT /note="CCA-adding enzyme"
FT /id="PRO_1000214137"
FT DOMAIN 220..326
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_01262"
FT BINDING 8
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 11
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 91
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 137
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT BINDING 140
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
SQ SEQUENCE 405 AA; 46272 MW; 19D362123FFBDD6D CRC64;
MNVYLVGGAV RNRLLKLPVT ERDWVVVGAT PEEMLLLGYK KVGKNFPVFL HPETKEEYAL
ARTERKMAEG HTGFACYASP DVTLEEDLLR RDLTINAIAC NDKGDLIDPY QGEKDLNQLI
LRHVSEAFIE DPLRVLRVAR FAAQFAHLGF SIDSVTLDLM TKISQSGELL TLSPERVWKE
TEKALLSPSP HIYFQVLKHC SAILVLFPEI DTLCSPLRCP LSHGLSTLSI AAKLTDQKEV
RFAALCHILG KKLTEYDVLG THDRAVLKRV PLCDLNKIEQ LCERLKLPNL FRELLKHTLK
YRGLVTIINR LSFPLLLNFF DELDLWRKPY RLEQLILISK ADESTEGGVE GKHDYQAQYV
REAFNIARAV SVKKILEGGF RKEAIQKELT RRRNQALDQW QKQKT
