ID A0A3Q9BME9_9LACT Unreviewed; 525 AA.
AC A0A3Q9BME9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=CCA-adding enzyme {ECO:0000256|HAMAP-Rule:MF_01263};
DE EC=2.7.7.72 {ECO:0000256|HAMAP-Rule:MF_01263};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000256|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA-NT {ECO:0000256|HAMAP-Rule:MF_01263};
GN Name=cca {ECO:0000256|HAMAP-Rule:MF_01263};
GN ORFNames=EJN90_12060 {ECO:0000313|EMBL:AZP05314.1};
OS Jeotgalibaca ciconiae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Jeotgalibaca.
OX NCBI_TaxID=2496265 {ECO:0000313|EMBL:AZP05314.1, ECO:0000313|Proteomes:UP000273326};
RN [1] {ECO:0000313|Proteomes:UP000273326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H21T32 {ECO:0000313|Proteomes:UP000273326};
RA Bae J.-W., Lee S.-Y.;
RT "Complete genome sequencing of Jeotgalibaca sp. H21T32.";
RL Submitted (DEC-2018) 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_01263}.
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_01263};
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_01263};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01263};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01263}.
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_01263}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Bacterial CCA-adding enzyme type 3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01263}.
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DR EMBL; CP034465; AZP05314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9BME9; -.
DR KEGG; jeh:EJN90_12060; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000273326; 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; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 1.10.110.30; -; 1.
DR Gene3D; 1.10.246.80; -; 1.
DR Gene3D; 1.20.58.560; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR HAMAP; MF_01263; CCA_bact_type3; 1.
DR InterPro; IPR032810; CCA-adding_enz_C.
DR InterPro; IPR023068; CCA-adding_enz_firmicutes.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR46173; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR46173:SF1; CCA TRNA NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR Pfam; PF13735; tRNA_NucTran2_2; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01263};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01263};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01263};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01263};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01263}; RNA repair {ECO:0000256|HAMAP-Rule:MF_01263};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01263};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01263}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01263}.
FT DOMAIN 27..147
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 174..228
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT DOMAIN 248..395
FT /note="CCA-adding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13735"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 32
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 35
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 116
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 159
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 162
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 165
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
FT BINDING 168
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01263"
SQ SEQUENCE 525 AA; 60496 MW; 1111C6AAEB27C327 CRC64;
MINIKQIPEF NKAASLIEKI EKEGYEAYFV GGGVRDTLLH LPISDVDIAS SATPEEIKRF
FPVTFDVGIQ HGTVMVLHEK ETYEITTFRT ESKYEKFRRP EKVDYVRSLE EDLKRRDFTI
NAIALNRNGQ LVDPFDGQID IKNKLIRAVG NPSERFREDA LRMMRAARFM SQLGFDIEEK
TKEAVEYYHP LLSKIAVERI REEWTKLLIG RNRKGGVKFF IETRLFQMCP GFQNRSEDLV
DLALFPHQFQ TPLIAWTVLL YFLKIDEEEV SSFLRAWKLS NKEISNVRTA LYALRVRMER
FWDNHLLFAT GIKIALEIED IMAGFGVVND INRLLALDKT LPIHSTHDIQ INGNEVIHLL
GFNRGGPYLG TILEDVKDRI LSGSLPNNKK QIETFILKRR FIYLDEVKKK EYIVEEGNSA
RSIELGDTGV LSSPSLLSFM EESCKEMIEG LVEEDETSVG TFVSMNHHYL TEIGSKIIIE
TRIKELSGKK YSFSIVARNG DDIVAIGEHT RKIINKNEFR NKLTK
//
