CATNT_ALKHC
ID CATNT_ALKHC Reviewed; 375 AA.
AC Q9KC89;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=CC-adding tRNA nucleotidyltransferase {ECO:0000303|PubMed:16109934};
DE Short=C-adding TNT {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:16109934};
DE AltName: Full=CC-adding enzyme {ECO:0000303|PubMed:16109934};
DE AltName: Full=NTSFI {ECO:0000303|PubMed:16109934};
GN OrderedLocusNames=BH1684 {ECO:0000312|EMBL:BAB05403.1};
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16109934; DOI=10.1128/jb.187.17.5927-5936.2005;
RA Bralley P., Chang S.A., Jones G.H.;
RT "A phylogeny of bacterial RNA nucleotidyltransferases: Bacillus halodurans
RT contains two tRNA nucleotidyltransferases.";
RL J. Bacteriol. 187:5927-5936(2005).
CC -!- FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the
CC tRNA CCA terminus. Adds the two cytidine residues to tRNA.
CC {ECO:0000269|PubMed:16109934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA precursor + 2 CTP = a tRNA with a 3' CC end + 2
CC diphosphate; Xref=Rhea:RHEA:60008, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC COMP:15488, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896,
CC ChEBI:CHEBI:83069; Evidence={ECO:0000269|PubMed:16109934};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60009;
CC Evidence={ECO:0000269|PubMed:16109934};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O67911};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:16109934};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; BA000004; BAB05403.1; -; Genomic_DNA.
DR PIR; D83860; D83860.
DR RefSeq; WP_010897846.1; NC_002570.2.
DR AlphaFoldDB; Q9KC89; -.
DR SMR; Q9KC89; -.
DR STRING; 272558.10174301; -.
DR EnsemblBacteria; BAB05403; BAB05403; BAB05403.
DR KEGG; bha:BH1684; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_3_0_9; -.
DR OMA; MRAVRFM; -.
DR OrthoDB; 2018439at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR032810; CCA-adding_enz_C.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR Pfam; PF13735; tRNA_NucTran2_2; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..375
FT /note="CC-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000139029"
FT BINDING 27..30
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 95..96
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 100
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 137..146
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 177
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
SQ SEQUENCE 375 AA; 42113 MW; 7133A060EEFD3D93 CRC64;
MDDVIKKGLS IVSELRDHGF EAYIVGGAVR DYHIGRKPKD VDVVTSASPE EIRTLYPHAF
QINRQFQTLT VHLQKVAIEV STLRGGSIED DLCSRDFTIN AMALAMNGDI IDPTGGKTDL
ENGVIRSFHP EARFKEDPLR MLRAPRFASE LGFTVAKGTA EAIKGSCSLL ADVAVERVEK
ELTQLMIGTH RSSGWCLLHE TGLYPFIPGV SLSKETVLRM KEISRSPGLL PADGFWAILY
LLENCSMKLP LAKEKKKRIR TIVHYVGERQ NHSWNETMLY QASLSVATVV EQIRALFGQA
SVHEEELRQL WSSLPIQTRT ELAVTGRDVM AHFQKKGGPW LADTLADIEE AVLLKHIENE
KKSIIQWLEE RRVES
