ID I4VRE6_9GAMM Unreviewed; 424 AA.
AC I4VRE6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 ECO:0000313|EMBL:EIL89787.1};
GN ORFNames=UU9_08690 {ECO:0000313|EMBL:EIL89787.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL89787.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL89787.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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}.
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:EIL89787.1}.
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DR EMBL; AJXU01000031; EIL89787.1; -; Genomic_DNA.
DR AlphaFoldDB; I4VRE6; -.
DR STRING; 1163408.UU9_08690; -.
DR PATRIC; fig|1163408.3.peg.1781; -.
DR eggNOG; COG0617; Bacteria.
DR Proteomes; UP000004210; 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 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 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|HAMAP-Rule:MF_01261, ECO:0000313|EMBL:EIL89787.1};
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}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01261};
KW Nickel {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}; Reference proteome {ECO:0000313|Proteomes:UP000004210};
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 241..343
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT BINDING 21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 21
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 24
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 104
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 150
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT BINDING 153
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
SQ SEQUENCE 424 AA; 46199 MW; CEDB7B616F32062A CRC64;
MTVRMPGAWQ DRGMRIYLVG GAVRDALLDR PVVDHDHVVV GAMPDDLLAL GYRPVGKDFP
VFLHPDTGEE YALARTERKT GRGYHGFVFQ ADATVTLEQD LARRDLTINA IARDEHGALT
DPFHGVRDIE ARVLRHVSPA FVEDPVRVLR VARFAARFAP LGFTVAAETM ALMQQMVRDG
EVDHLVPERV WAETRKALTE PQPSAFLRVL REAGALRVLF PEVDALYGVP QRAEFHPEID
TGVHVEMVLD AAAKLAPRND LVGFCALTHD LGKALTPADA LPRHIGHEHR GVAPLRQLAA
RLKVPTEHAA LAEAVCREHL NAHRAFELKP ATVAKLLASL DALRRPARLD VFLAACMADK
RGRLGHEGDA YPQADYLREA CAAAAAVNAS TFVAQGLAGP AIGAAMERAR IDAIATVKTK
LPAS
//
