AATNT_ALKHC
ID AATNT_ALKHC Reviewed; 427 AA.
AC Q9K8X1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=A-adding tRNA nucleotidyltransferase {ECO:0000303|PubMed:16109934};
DE Short=A-adding TNT {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:16109934};
DE AltName: Full=A-adding enzyme {ECO:0000303|PubMed:16109934};
DE AltName: Full=NTSFII {ECO:0000303|PubMed:16109934};
GN OrderedLocusNames=BH2881 {ECO:0000312|EMBL:BAB06600.1};
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 terminal adenosine residue to tRNA.
CC {ECO:0000269|PubMed:16109934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end +
CC diphosphate; Xref=Rhea:RHEA:60012, Rhea:RHEA-COMP:10468, Rhea:RHEA-
CC COMP:15488, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83069,
CC ChEBI:CHEBI:83071; Evidence={ECO:0000269|PubMed:16109934};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60013;
CC Evidence={ECO:0000269|PubMed:16109934};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O66728};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {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; BAB06600.1; -; Genomic_DNA.
DR PIR; A84010; A84010.
DR RefSeq; WP_010899028.1; NC_002570.2.
DR AlphaFoldDB; Q9K8X1; -.
DR SMR; Q9K8X1; -.
DR STRING; 272558.10175503; -.
DR EnsemblBacteria; BAB06600; BAB06600; BAB06600.
DR KEGG; bha:BH2881; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_5_1_9; -.
DR OMA; SADRIMN; -.
DR OrthoDB; 2018439at2; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; 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; 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 SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..427
FT /note="A-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447564"
FT BINDING 49..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 136..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 181..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O66728"
SQ SEQUENCE 427 AA; 48501 MW; 67CE211B31B6D7A9 CRC64;
MSEEHQESYH SDNLIDLMNH TLTNDHLQLL KKLGEMAAKL RMNLFLVGGT VRDMLRGVPG
GDLDLVIEGD ALAFSQNVAN VLGGKVKHHE PFATATWVGA ENLKLDIVSA RAESYAKPGA
LPTIRHSHIT DDLARRDFSI NAMAIHLHPA SYGQLVDPFH GRHDLTNGLI RILHSQSFID
DPTRLLRGVR FVSRFNYRFE QKTANLALAT QPALTNALAN VSPERIVHEL KLLCHETDPV
SSFSKLEDLH VWQALLGLTF SSSSATHLSR LQEEQNGEPL HWFQAIATVG FLEDNWKASL
VPFAITAMEQ RFLQNIEDIQ KRLTNMTRFS TDYLHKQLYQ VPEEPLRFYA LSSGEEMQKV
LDLYLHQRKQ LQPLLTGHDL MELGMKPSPL FKECLLLHEC EQLKGTIENK QDALQFAREF
FNHKQPL
