ID A0A0V8RUL9_PYROC Unreviewed; 476 AA.
AC A0A0V8RUL9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=CF15_02800 {ECO:0000313|EMBL:KSW11756.1};
OS Pyrodictium occultum.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=2309 {ECO:0000313|EMBL:KSW11756.1, ECO:0000313|Proteomes:UP000053352};
RN [1] {ECO:0000313|EMBL:KSW11756.1, ECO:0000313|Proteomes:UP000053352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL-19 {ECO:0000313|EMBL:KSW11756.1,
RC ECO:0000313|Proteomes:UP000053352};
RA Utturkar S., Huber H., Leptihn S., Brown S., Stetter K.O., Podar M.;
RT "Genome sequence of Pyrodictium occultum PL-19, a marine hyperthermophilic
RT archaeon isolated from Volcano, Italy.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KSW11756.1}.
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DR EMBL; LNTB01000001; KSW11756.1; -; Genomic_DNA.
DR RefSeq; WP_058370433.1; NZ_LNTB01000001.1.
DR AlphaFoldDB; A0A0V8RUL9; -.
DR STRING; 2309.CF15_02800; -.
DR OrthoDB; 7378at2157; -.
DR Proteomes; UP000053352; Unassembled WGS sequence.
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 {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}; Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01264};
KW Reference proteome {ECO:0000313|Proteomes:UP000053352};
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 42..82
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 161..276
FT /note="tRNA nucleotidyltransferase substrate binding"
FT /evidence="ECO:0000259|Pfam:PF09249"
FT DOMAIN 317..426
FT /note="CCA-adding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21133"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 57
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 60
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 147
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 167
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
FT BINDING 176
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01264"
SQ SEQUENCE 476 AA; 53093 MW; BC2645AA0EE41789 CRC64;
MGAACILGSV EEDVLREIRP SPEERDRLRE VAGRAVNLVQ HALRQLGVEA RVTIEGSYAK
DTWLRGDVDL DVFLLLPEET CLETIESGLV EKLAALLSST GVKVELRYAQ HPYLRFMVDG
VWVEAVPGCS VSDPSRPLTA VDRTPFHRIY VIEHTTPEMR DEIRLLKSFM KGVGVYGAEL
AVRGFSGYLT ELLVIHYQCF RRVLEAALTW RPPVIIDVEG RHGRRELLKK FRGAAMIVPD
PVDPGRNAAA AVSRRSIALF ITAARLYLRE PSKRFFRVPG EARVSPPLLP GSVVAAYGPR
ASNTVIIAME PGRTLPPDNM WGIALRALRQ ARGLLERWGF RVLAASAHAG GEGRIALAIE
LESRLLPRYE LHLGPHAWNG ENAERFLEKY RRDTEALGPW VEEDGRLAVA RPRRYRDAVE
LLRGRLAEWL PGSARGYRVE IAPLPAAASE LRGEELEWLA REAARAPSWL KPGLSS
//
