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Database: UniProt
Entry: A0A1G6NJJ5_9BURK
LinkDB: A0A1G6NJJ5_9BURK
Original site: A0A1G6NJJ5_9BURK 
ID   A0A1G6NJJ5_9BURK        Unreviewed;       418 AA.
AC   A0A1G6NJJ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=SAMN05444679_104279 {ECO:0000313|EMBL:SDC67476.1};
OS   Variovorax sp. CF079.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882774 {ECO:0000313|EMBL:SDC67476.1, ECO:0000313|Proteomes:UP000198763};
RN   [1] {ECO:0000313|EMBL:SDC67476.1, ECO:0000313|Proteomes:UP000198763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF079 {ECO:0000313|EMBL:SDC67476.1,
RC   ECO:0000313|Proteomes:UP000198763};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FMZU01000004; SDC67476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6NJJ5; -.
DR   STRING; 1882774.SAMN05444679_104279; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000198763; 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; cd00077; HDc; 1.
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   InterPro; IPR012006; CCA_bact.
DR   InterPro; IPR003607; HD/PDEase_dom.
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   SMART; SM00471; HDc; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01261}; Hydrolase {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}; Multifunctional enzyme {ECO:0000256|HAMAP-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}; Reference proteome {ECO:0000313|Proteomes:UP000198763};
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          234..335
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         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         145
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         148
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
SQ   SEQUENCE   418 AA;  45938 MW;  8107682E77AB1591 CRC64;
     MQTYLVGGAI RDALLGRPGS DRDWVVVGAT PEEMVAKGFL PVGRDFPVFL HPKTREEYAL
     ARTERKSAPG YRGFTIHAAP DVTLEQDLAR RDLTVNAIAL PANKAASAID TAHLIDPFHG
     RHDLAQKLLR HVTDAFREDP VRILRVARFA ARFTDFEVAP ETMALMREMV AAGEVDALVP
     ERVWQELARG LMEARPSRMF ELLRDCGALA VLLPELDRLW GVPQPEAHHP EVDTGLHLMM
     VLDMAARLEA PLAVRFACLV HDLGKGSTPP EVLPRHIGHE QRSAELLQAV CERWRVPVEL
     RELAEVVARE HGNIHRSGEL NATALVRLLD RCDAFRKPER FEQALLACEC DARGRLGLED
     SAYPQRECLL AALGAAQSVE TEPIARDAQL AGAAGPKIGE AIARARVAAV AAALPPRA
//
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