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Database: UniProt
Entry: A0A191ZJB1_9GAMM
LinkDB: A0A191ZJB1_9GAMM
Original site: A0A191ZJB1_9GAMM 
ID   A0A191ZJB1_9GAMM        Unreviewed;       427 AA.
AC   A0A191ZJB1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=A9404_11840 {ECO:0000313|EMBL:ANJ67974.1};
OS   Halothiobacillus sp. LS2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=1860122 {ECO:0000313|EMBL:ANJ67974.1, ECO:0000313|Proteomes:UP000078596};
RN   [1] {ECO:0000313|EMBL:ANJ67974.1, ECO:0000313|Proteomes:UP000078596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS2 {ECO:0000313|EMBL:ANJ67974.1,
RC   ECO:0000313|Proteomes:UP000078596};
RA   Luo J., Tan X., Lin W.;
RT   "Insight into the functional genes involving in sulfur oxidation in Pearl
RT   River water.";
RL   Submitted (JUN-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; CP016027; ANJ67974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A191ZJB1; -.
DR   STRING; 1860122.A9404_11840; -.
DR   KEGG; haz:A9404_11840; -.
DR   Proteomes; UP000078596; 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: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   HAMAP; MF_01262; CCA_bact_type2; 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   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:UP000078596};
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          236..341
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         16
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         19
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         29
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         31
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01261"
FT   BINDING         99
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   427 AA;  46776 MW;  7AC8C5F9C2709CE8 CRC64;
     MSPAIEQDLN CYVVGGAVRD RLLGRPASDR DWVVVGSSPE DMRRRGFRPV GQDFPVFLHP
     ETGEEYALAR TERKQGRGHQ GFVFHAAPDV TLEDDLQRRD LTINALAQKQ DGTLVDPFGF
     KADLDARILR HVSPAFAEDP LRVLRVARFA AQLAAEGFEL AGETRDLMTA MTASGELDDL
     TAERVWQETR KALASPNPAR YFEILRTVGA LKVLFPEVDA LFGVPQPAHY HPEIDSGIHT
     LLALTAAVGL NNDVGQDVAV RFAVLCHDLG KALTPPEEWP RHIGHEQRGV APTRALCARL
     KVPRAVKELA VLTTAQHGRV HAAMEMRPAT LLDLIESLDG LRRPERMADV LTACHADARG
     RLGSETCDYP QADRVRAAAD IARGISPAPF LERGLTGVQL GEALRRARIQ AIKQALAESQ
     PNAQTAE
//
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