ID A0A1G6SXR1_9BURK Unreviewed; 418 AA.
AC A0A1G6SXR1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Multifunctional CCA protein {ECO:0000256|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=CCA-adding enzyme {ECO:0000256|HAMAP-Rule:MF_01261};
DE EC=2.7.7.72 {ECO:0000256|HAMAP-Rule:MF_01261};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000256|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01261};
DE AltName: Full=tRNA-NT {ECO:0000256|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=2'-nucleotidase {ECO:0000256|HAMAP-Rule:MF_01261};
DE EC=3.1.3.- {ECO:0000256|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_01261};
DE EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_01261};
DE Includes:
DE RecName: Full=Phosphatase {ECO:0000256|HAMAP-Rule:MF_01261};
GN Name=cca {ECO:0000256|HAMAP-Rule:MF_01261};
GN ORFNames=SAMN05421548_11635 {ECO:0000313|EMBL:SDD21531.1};
OS Paraburkholderia lycopersici.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416944 {ECO:0000313|EMBL:SDD21531.1, ECO:0000313|Proteomes:UP000198908};
RN [1] {ECO:0000313|Proteomes:UP000198908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNe-862 {ECO:0000313|Proteomes:UP000198908};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2016) 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_01261}.
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_01261};
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_01261};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01261};
CC Note=Magnesium is required for nucleotidyltransferase activity.
CC {ECO:0000256|HAMAP-Rule:MF_01261};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01261};
CC Note=Nickel for phosphatase activity. {ECO:0000256|HAMAP-
CC Rule:MF_01261};
CC -!- SUBUNIT: Monomer. Can also form homodimers and oligomers.
CC {ECO:0000256|HAMAP-Rule:MF_01261}.
CC -!- DOMAIN: Comprises two domains: an N-terminal domain containing the
CC nucleotidyltransferase activity and a C-terminal HD domain associated
CC with both phosphodiesterase and phosphatase activities.
CC {ECO:0000256|HAMAP-Rule:MF_01261}.
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_01261}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01261}.
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DR EMBL; FMYQ01000016; SDD21531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6SXR1; -.
DR STRING; 416944.SAMN05421548_11635; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000198908; 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:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016791; F:phosphatase activity; 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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR HAMAP; MF_01261; CCA_bact_type1; 1.
DR HAMAP; MF_01262; CCA_bact_type2; 1.
DR InterPro; IPR012006; CCA_bact.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR PANTHER; PTHR47545:SF1; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR PIRSF; PIRSF000813; CCA_bact; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01261};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01261};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01261};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01261};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01261};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01261};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01261};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01261};
KW RNA repair {ECO:0000256|ARBA:ARBA00022800, ECO:0000256|HAMAP-
KW Rule:MF_01261};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01261};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01261};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01261}.
FT DOMAIN 232..333
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT BINDING 8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 8
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 11
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 91
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 143
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 146
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
SQ SEQUENCE 418 AA; 45968 MW; 934291DBC39D62F1 CRC64;
MKIYVVGGAI RDEMLGLPVR DRDYVVVGAT PAQMVAQGYR PVGKDFPVFL HPDTHEEYAL
ARTERKTAAG YHGFQFYYSP DVTLEEDLAR RDLTINAMAR EVQPGGVLTG EVVDPFGGAR
DLRARVFRHV SEAFLEDPVR ILRIARFAAR FADFAVAPET LDLMREMVAS GEVDALVPER
VWQELSRGLM ESKPSRMFEV LRDCGALARV LPEVDALWGV PQRADYHPEV DTGVHVMMVI
DHAAAQGYTL PVRFAALTHD LGKGTTPEDV LPRHLGHEGR SVDLLKPLCD RLRVPNDCRE
LAVLVAREHG NVHRVTDMGA AALVRLLERC DALRKPARFA EALQACESDL RGRLNWENAP
YPQAERLRVA LVAARGVDAG AIAQAIAQAG EKKGDAGKIK EAVHQARIAA VEAALASS
//
