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Database: UniProt
Entry: A3MWY7_PYRCJ
LinkDB: A3MWY7_PYRCJ
Original site: A3MWY7_PYRCJ 
ID   A3MWY7_PYRCJ            Unreviewed;       418 AA.
AC   A3MWY7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 83.
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=Pcal_1737 {ECO:0000313|EMBL:ABO09154.1};
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359 {ECO:0000313|EMBL:ABO09154.1, ECO:0000313|Proteomes:UP000001431};
RN   [1] {ECO:0000313|EMBL:ABO09154.1, ECO:0000313|Proteomes:UP000001431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1
RC   {ECO:0000313|Proteomes:UP000001431};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000561; ABO09154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MWY7; -.
DR   STRING; 410359.Pcal_1737; -.
DR   KEGG; pcl:Pcal_1737; -.
DR   eggNOG; arCOG04249; Archaea.
DR   HOGENOM; CLU_044679_1_0_2; -.
DR   OMA; YAEHPYI; -.
DR   OrthoDB; 7378at2157; -.
DR   Proteomes; UP000001431; 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.
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};
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          39..138
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          155..263
FT                   /note="tRNA nucleotidyltransferase substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF09249"
FT   DOMAIN          276..393
FT                   /note="CCA-adding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21133"
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         56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         56
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         65
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         140
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         160
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         160
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT   BINDING         169
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
SQ   SEQUENCE   418 AA;  47473 MW;  91F1DEA37C5867DA CRC64;
     MSLEEVLEEA YKLVTPTPEE EKKVAEVASN VKGLVARWVE ERGVRAEVQV LGSSARGTWL
     PGQRDIDIFI VLEDRSIKPE EVVESLSKFL DVVGVSWGLR FAQHPYLTVF IDGYEVDVVP
     CYKISPGERP ITAADRSPLH HQFLMQRMTQ QQRQDVRLLK LFLKAIGVYG AEIKVEGFSG
     YLAELLVVYY GSFLDVLKAA SKWRPYRTFI SFQEVKTKFR APLVVVDPVD SSRNAAAAVS
     LTSMSTFILA ARRFLKRPSM SYFRPTVGKL VQPLHVVEVV FPYPAEPPDI VWGKYKRLGR
     ALFNWIRECG FRVYRWGVES DEKSYVSLVY VLETAVLPPY VLHKGPPVYD DAVDKFVEKY
     VGEDVVGPFV QGSRVYVIKR RKYTQIADCI KAKLGGGEYV VKLGEYSGEL VRKNPWIT
//
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