CATNT_ALKCK
ID CATNT_ALKCK Reviewed; 376 AA.
AC Q5WGA1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=CC-adding tRNA nucleotidyltransferase {ECO:0000305};
DE Short=C-adding TNT {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:18523015};
DE AltName: Full=CC-adding enzyme {ECO:0000303|PubMed:18523015};
GN OrderedLocusNames=ABC2069;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 8716;
RX PubMed=18523015; DOI=10.1073/pnas.0801971105;
RA Neuenfeldt A., Just A., Betat H., Moerl M.;
RT "Evolution of tRNA nucleotidyltransferases: a small deletion generated CC-
RT adding enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7953-7958(2008).
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:18523015}.
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:18523015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60009;
CC Evidence={ECO:0000269|PubMed:18523015};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O67911};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP006627; BAD64604.1; -; Genomic_DNA.
DR RefSeq; WP_011246912.1; NC_006582.1.
DR AlphaFoldDB; Q5WGA1; -.
DR SMR; Q5WGA1; -.
DR STRING; 66692.ABC2069; -.
DR EnsemblBacteria; BAD64604; BAD64604; ABC2069.
DR KEGG; bcl:ABC2069; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_3_0_9; -.
DR OMA; MRAVRFM; -.
DR OrthoDB; 2018439at2; -.
DR BRENDA; 2.7.7.72; 7525.
DR Proteomes; UP000001168; 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..376
FT /note="CC-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000139032"
FT BINDING 26..29
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 94..95
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 99
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 136..145
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 176
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
SQ SEQUENCE 376 AA; 41958 MW; B94ED19681B023CC CRC64;
MSIWMEGFKA VRTLNAAGFE AYIVGGAVRD YLLGKDVDDV DIATQASPHQ VADIFTKGVH
INQEHKTVLI PGEKGPIEIT TYKGETLAED LQKRDFTINA LAMTETREVI DPYGGRQDLQ
KRLLRSYDAQ KRLSEDPLRM LRAARFISSL GFEADRQLVK ETTVQKAALQ RCARERVVVE
LEKLLKGMET EAAFAFLQET GAIHSLPGIQ ITDSQLAELM RLPKQQWDSG DRAWLEFAIC
TGGPSSMAAL PLPKKRKQLV AAGLKAFEYR QTQQRWSDWQ LYISGLAIAM QIEEIRAGRQ
LPSIQKEELA EQWSALPIKA KSDLAITGRD LLHAKAAPGP WMKEALQAAE KAVVTKKCPN
EKAAILAFLT MREDGK
