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Database: UniProt
Entry: CCA_PYRAE
LinkDB: CCA_PYRAE
Original site: CCA_PYRAE 
ID   CCA_PYRAE               Reviewed;         419 AA.
AC   Q8ZTC3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 104.
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};
GN   Name=cca {ECO:0000255|HAMAP-Rule:MF_01264}; OrderedLocusNames=PAE3325;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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. tRNA 3'-terminal CCA addition is required both for tRNA
CC       processing and repair. Also involved in tRNA surveillance by mediating
CC       tandem CCA addition to generate a CCACCA at the 3' terminus of unstable
CC       tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs
CC       are marked with CCACCA and rapidly degraded. {ECO:0000255|HAMAP-
CC       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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a tRNA with a 3' CCA end + ATP + 2 CTP = a tRNA with a 3'
CC         CCACCA end + 3 diphosphate; Xref=Rhea:RHEA:76235, Rhea:RHEA-
CC         COMP:10468, Rhea:RHEA-COMP:18655, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:83071,
CC         ChEBI:CHEBI:195187; Evidence={ECO:0000255|HAMAP-Rule:MF_01264};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76236;
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; AE009441; AAL64839.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZTC3; -.
DR   SMR; Q8ZTC3; -.
DR   STRING; 178306.PAE3325; -.
DR   EnsemblBacteria; AAL64839; AAL64839; PAE3325.
DR   KEGG; pai:PAE3325; -.
DR   PATRIC; fig|178306.9.peg.2503; -.
DR   eggNOG; arCOG04249; Archaea.
DR   HOGENOM; CLU_044679_1_0_2; -.
DR   InParanoid; Q8ZTC3; -.
DR   OMA; YAEHPYI; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; 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; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.1410.30; CCA tRNA nucleotidyltransferase, domain 2; 1.
DR   Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR   HAMAP; MF_01264; CCA_arch; 1.
DR   InterPro; IPR048833; CAA_C.
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; IPR011068; NuclTrfase_I-like_C.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   InterPro; IPR015329; tRNA_NucTransf2.
DR   NCBIfam; TIGR03671; cca_archaeal; 1.
DR   PANTHER; PTHR39643; CCA-ADDING ENZYME; 1.
DR   PANTHER; PTHR39643:SF1; CCA-ADDING ENZYME; 1.
DR   Pfam; PF21133; CAA_C_arc; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF09249; tRNA_NucTransf2; 1.
DR   PIRSF; PIRSF005335; CCA_arch; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 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..419
FT                   /note="CCA-adding enzyme"
FT                   /id="PRO_0000139077"
FT   BINDING         54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         54
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         57
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         68
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         141
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         161
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
FT   BINDING         170
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01264"
SQ   SEQUENCE   419 AA;  48046 MW;  DE0613CC00C8FDE9 CRC64;
     MSTLEEVLSE AYKLVIPSEE EEKRIREVTQ KVKRLVSQII EEGGIDALVD VYGSGARGTW
     LPGQRDIDIF VVLNDRRIKP EDVVKILTSR FTTLGLNWAL RYAQHPYVSL QVDDYEVDIV
     PCYKIQPGER PITAADRSPL HHKFLSERLK KDQILDVRLL KLFLKTIGVY GAEIKTEGFS
     GYLTELLVVY YGSFIEVLRA ASRWRPYKTY ITFVETSAKF KSPLVVVDPV DPNRNAAAAV
     SLTSMSTLIL AARRFLKKPS LSYFQPSRGY AIRQVETVEV VYPYPGEPPD IVWGKYKRIG
     RNLFKWLREC GFKVFRWGVE SDEKTYVKLV YVVEQTKLAP YTLHKGPPVY DDAVDAFIEK
     YVNEEVIGPF VVGARAYVIK KRKWTDISHC INAKLGKGNY DIRVNLYDGD LVRKTPWLT
//
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