CATNT_THET2
ID CATNT_THET2 Reviewed; 434 AA.
AC Q72K91;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=TT_C0556 {ECO:0000312|EMBL:AAS80904.1};
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
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}.
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DR EMBL; AE017221; AAS80904.1; -; Genomic_DNA.
DR AlphaFoldDB; Q72K91; -.
DR SMR; Q72K91; -.
DR STRING; 262724.TT_C0556; -.
DR EnsemblBacteria; AAS80904; AAS80904; TT_C0556.
DR KEGG; tth:TT_C0556; -.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG1353; Bacteria.
DR HOGENOM; CLU_015961_6_2_0; -.
DR OMA; GWTFHGH; -.
DR BRENDA; 2.7.7.72; 2305.
DR Proteomes; UP000000592; 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; cd00077; HDc; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00277; HDIG; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW RNA-binding; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..434
FT /note="CC-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447572"
FT BINDING 19..22
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 90..91
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 95
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 130..139
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 175
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
SQ SEQUENCE 434 AA; 49369 MW; 7D235BFA0E5A1430 CRC64;
MAHMDFPFYT PKDAFPVGGA VRDLLLGRRP TDLDYAALDP EKAAEEAKRR LGGSLFPLDP
KRGHYRLVVG ERTLDFTPLE GRLEEDLLRR DYRVNALLWK GGAVFGLKGV EEDLRRRLLV
PVREENLYQD HLRSLRGVRL AATLGFGLPR RTREALGRHA RFLQAHPEAL PARERVKEEL
ARLLLSPRAA FGLRLLERVG LLGVYLPELA LLVGLHQGGV HHLPAWEHTL SAVFHLLWLW
PEAPLEARLA ALFHDVGKPL TRRFDPEVGR FRFLGHAEVG AEIARASLFW LRFPKEVVER
VAGLVRRHMD RLPEERKALR RFFLRRQDLL PDLVYLMAAD RLATRGVERE AWEVLGRYEE
VLKDPLPQRP LLSGEEVMAL LGLQEGPEVG RALKALLEAQ AEGRVGTKEE ARAFLLYWRG
GREAQASGTP DHPH
