CCA_THEAI
ID CCA_THEAI Reviewed; 222 AA.
AC Q9V302;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01264};
DE EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01264};
DE AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01264};
DE Flags: Fragment;
GN Name=cca {ECO:0000255|HAMAP-Rule:MF_01264};
OS Thermoplasma acidophilum.
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=2303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HO-62;
RX PubMed=10438486; DOI=10.1074/jbc.274.33.23160;
RA Cosper N.J., Stalhandske C.M.V., Iwasaki H., Oshima T., Scott R.A.,
RA Iwasaki T.;
RT "Structural conservation of the isolated zinc site in archaeal zinc-
RT containing ferredoxins as revealed by X-ray absorption spectroscopic
RT analysis and its evolutionary implications.";
RL J. Biol. Chem. 274:23160-23168(1999).
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_01264}.
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_01264};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01264};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01264}.
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_01264}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Archaeal CCA-adding enzyme subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01264}.
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DR EMBL; AB023294; BAA82799.1; -; Genomic_DNA.
DR PIR; T37335; T37335.
DR AlphaFoldDB; Q9V302; -.
DR SMR; Q9V302; -.
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:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:InterPro.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 1.10.1410.30; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_01264; CCA_arch; 1.
DR InterPro; IPR008229; CCA-adding_arc.
DR InterPro; IPR042090; CCA_tRNA_nucleotrans_2.
DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR015329; tRNA_NucTransf2.
DR PANTHER; PTHR39643; PTHR39643; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF09249; tRNA_NucTransf2; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR03671; cca_archaeal; 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..>222
FT /note="CCA-adding enzyme"
FT /id="PRO_0000139086"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 50
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 53
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 135
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 155
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT BINDING 164
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT NON_TER 222
SQ SEQUENCE 222 AA; 25546 MW; F2B46152F924EB9C CRC64;
MIDYQEVLSR YRPTQEEENR LRIISDDIIR KINSICRSRR LRAEAVIVGS YAKGTNLRDG
DLDIFIAFDR DYPEEIINTE GLHIGHAVIP NGREKYAEHP YVSGEIGGVK IDVVPCYKMS
FGDRKISAVD RTLLHTEYVN GHLDEKGRDE VRLLKIFTKS IGVYGAEART FGFSGYLCEL
LVIRFRSFEN VIRYFSKAKG RVLIDPDERF RDPMLLIDPV DP
