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Database: UniProt
Entry: A0RYQ4_CENSY
LinkDB: A0RYQ4_CENSY
Original site: A0RYQ4_CENSY 
ID   A0RYQ4_CENSY            Unreviewed;       442 AA.
AC   A0RYQ4;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=CCA-adding enzyme {ECO:0000256|HAMAP-Rule:MF_01264};
DE            EC=2.7.7.72 {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
DE   AltName: Full=tRNA-NT {ECO:0000256|HAMAP-Rule:MF_01264};
GN   Name=cca {ECO:0000256|HAMAP-Rule:MF_01264};
GN   OrderedLocusNames=CENSYa_1862 {ECO:0000313|EMBL:ABK78471.1};
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Nitrososphaerota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK78471.1, ECO:0000313|Proteomes:UP000000758};
RN   [1] {ECO:0000313|EMBL:ABK78471.1, ECO:0000313|Proteomes:UP000000758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A {ECO:0000313|Proteomes:UP000000758};
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01264};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01264};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01264}.
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC       and CTP and is responsible for their addition. {ECO:0000256|HAMAP-
CC       Rule:MF_01264}.
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Archaeal CCA-adding enzyme subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01264}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01264}.
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DR   EMBL; DP000238; ABK78471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RYQ4; -.
DR   STRING; 414004.CENSYa_1862; -.
DR   EnsemblBacteria; ABK78471; ABK78471; CENSYa_1862.
DR   KEGG; csy:CENSYa_1862; -.
DR   HOGENOM; CLU_044679_1_0_2; -.
DR   OMA; YAEHPYI; -.
DR   Proteomes; UP000000758; 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; 3.30.70.1550; Archaeal tRNA CCA-adding enzyme catalytic domain; 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.
DR   PROSITE; PS50152; 25A_SYNTH_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01264};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01264}; Reference proteome {ECO:0000313|Proteomes:UP000000758};
KW   RNA repair {ECO:0000256|ARBA:ARBA00022800, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01264};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01264}.
FT   DOMAIN          44..133
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          151..257
FT                   /note="tRNA nucleotidyltransferase substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF09249"
FT   DOMAIN          272..389
FT                   /note="CCA-adding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21133"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         50
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         53
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         137
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         157
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         166
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
SQ   SEQUENCE   442 AA;  48408 MW;  07F0863D8DF3B6E9 CRC64;
     MTVLDRARKL AVPSARAARE KDRTAARALA LVESEIAGRP RITGAEFGGS YPKGTWLPGR
     SDIDIFVRFD VSAPRGEFED VSKEVGFAAL KGHGPYTRFS EHPYVEAEME GTRINVIPCY
     EVEKGKWKSA ADRSRFHTAF MKENLTSTMR DEVRLLKLFL KNNGVYGAEI SRQGFSGYAT
     EVLVWNFGGF EGVVRGMAGI RRGQVIGTAG KEFDTPVSIM DPVDPLRNLA AAVSVESLGR
     LVLLCRGFEK KQSASYFVRR KLRTSEALLR NCITVSFRHE ERSPDTIWGQ VKRAASAVGQ
     QLMMAGFTVA RSGAWTDGRS RACLFFLLES RSIPEYTVRE GPDFFGGDDA ERFAASGRKA
     LAVWVGGSGR VMSMERRAES DAQGFLRTLL GRGLDGSGVP RGIKPDVKRG FAVAAGGSRL
     PESVKAELLE LVSTDAAVFP SR
//
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