ID F3YAJ4_MELPT Unreviewed; 410 AA.
AC F3YAJ4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=MPTP_1068 {ECO:0000313|EMBL:BAK21522.1};
OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS 702443).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Melissococcus.
OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK21522.1, ECO:0000313|Proteomes:UP000008456};
RN [1] {ECO:0000313|EMBL:BAK21522.1, ECO:0000313|Proteomes:UP000008456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC {ECO:0000313|Proteomes:UP000008456};
RX PubMed=21622755; DOI=10.1128/JB.05151-11;
RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL J. Bacteriol. 193:4029-4030(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 35311;
RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA Akiyama T.;
RT "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL Submitted (APR-2011) 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; AP012200; BAK21522.1; -; Genomic_DNA.
DR RefSeq; WP_013773960.1; NC_015516.1.
DR AlphaFoldDB; F3YAJ4; -.
DR STRING; 940190.MPTP_1068; -.
DR KEGG; mps:MPTP_1068; -.
DR HOGENOM; CLU_015961_3_0_9; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000008456; 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 HAMAP; MF_01263; CCA_bact_type3; 1.
DR InterPro; IPR032810; CCA-adding_enz_C.
DR InterPro; IPR023068; CCA-adding_enz_firmicutes.
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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000008456};
KW 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 249..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 410 AA; 46907 MW; 3B07CF30CB3BF003 CRC64;
MKLTKLPIEF TEATPIIKKI QKGGYEAYFV GGSVRDVLLN KPIHDVDIAS SAYPEEIKQL
FRRTIDVGIE HGTVLVLHGS KQYEITTFRT ESTYQDFRRP DTVTFVRSLS EDLKRRDFTI
NALALDRSGQ VIDQFDGISD IENKVIRAVG DPKARFHEDA LRMMRALRFA SQLDFQIEEK
TLAGISAFHF LLEKVSVERI TIEFVKMLLG KNRKAGLYPF IQTECYQYCP CLKQAGEALL
NFSELPNQQI AEESEAWTLL LHSLNLTKEA ALVFLKSWKL SNHLIQEVCQ LSKGLNFRLK
KAFSIEMLYE LGLEKALIVE KLLIYYHKES QPELVKQQFA QLPIHNRKQL AITGKDLLNI
TNGKSGKWVG ELLSLIESQV LHGDLINTTE ELISYAKSKL EMEDKKGDFF
//
