CATNT_DEIRA
ID CATNT_DEIRA Reviewed; 374 AA.
AC Q9RVP2;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=CC-adding tRNA nucleotidyltransferase {ECO:0000305};
DE Short=C-adding TNT {ECO:0000305};
DE EC=2.7.7.- {ECO:0000269|PubMed:12370185};
DE AltName: Full=CC-adding enzyme {ECO:0000303|PubMed:12370185};
GN OrderedLocusNames=DR_0983 {ECO:0000312|EMBL:AAF10560.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12370185; DOI=10.1074/jbc.m207527200;
RA Tomita K., Weiner A.M.;
RT "Closely related CC- and A-adding enzymes collaborate to construct and
RT repair the 3'-terminal CCA of tRNA in Synechocystis sp. and Deinococcus
RT radiodurans.";
RL J. Biol. Chem. 277:48192-48198(2002).
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:12370185}.
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:12370185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60009;
CC Evidence={ECO:0000269|PubMed:12370185};
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; AE000513; AAF10560.1; -; Genomic_DNA.
DR PIR; B75453; B75453.
DR RefSeq; NP_294707.1; NC_001263.1.
DR RefSeq; WP_010887626.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RVP2; -.
DR SMR; Q9RVP2; -.
DR STRING; 243230.DR_0983; -.
DR EnsemblBacteria; AAF10560; AAF10560; DR_0983.
DR KEGG; dra:DR_0983; -.
DR PATRIC; fig|243230.17.peg.1170; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_5_1_0; -.
DR InParanoid; Q9RVP2; -.
DR OMA; FTFHPAF; -.
DR OrthoDB; 2018439at2; -.
DR Proteomes; UP000002524; Chromosome I.
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: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 Pfam; PF01743; PolyA_pol; 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..374
FT /note="CC-adding tRNA nucleotidyltransferase"
FT /id="PRO_0000447569"
FT BINDING 39..42
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 126..127
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 131
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 171..180
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
FT BINDING 209
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000250|UniProtKB:O67911"
SQ SEQUENCE 374 AA; 39755 MW; C5E5B9CB05728633 CRC64;
MATPDGEQVW AQLQPQDRAW LNDLSRRAGP DTELALVGGA VRDALLGQTP LDLDIVVAGQ
DGQGVEALAL ASGLPFVFHP AFENATLTLP DGRGADLVRA RREHYPQPGR NPEPLPGTLH
DDLRRRDFGL NALALRLRED GAPELLDVVG GLRDLERREL RPLHDRSLHE DASRLVRAAR
LAARLELHPA PELLAQVPDA LALADDTPRL WAELKLLLAE PRPGQAARVL DGWGAGTLLP
GLPLLEALDV QQNAGTPVQP GTYAAAVLSA APDAAALAER MALGERPAAL LARALSDSYF
APGTPELQLR GLLRPESYLP LTGREVVALG VAPGPAVGRA LAHLAGLRQS GAVRSADEER
TALRAYLGAN PKAT
