ID   KPTA_DEIRA              Reviewed;         283 AA.
AC   Q9RRR1;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Probable RNA 2'-phosphotransferase;
DE            EC=2.7.1.-;
GN   Name=kptA; OrderedLocusNames=DR_2427;
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).
CC   -!- FUNCTION: Removes the 2'-phosphate from RNA via an intermediate in
CC       which the phosphate is ADP-ribosylated by NAD followed by a presumed
CC       transesterification to release the RNA and generate ADP-ribose 1''-2''-
CC       cyclic phosphate (APPR>P). May function as an ADP-ribosylase (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
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DR   EMBL; AE000513; AAF11978.1; -; Genomic_DNA.
DR   PIR; A75274; A75274.
DR   RefSeq; NP_296147.1; NC_001263.1.
DR   AlphaFoldDB; Q9RRR1; -.
DR   SMR; Q9RRR1; -.
DR   STRING; 243230.DR_2427; -.
DR   EnsemblBacteria; AAF11978; AAF11978; DR_2427.
DR   KEGG; dra:DR_2427; -.
DR   eggNOG; COG1859; Bacteria.
DR   HOGENOM; CLU_982540_0_0_0; -.
DR   OrthoDB; 1893705at2; -.
DR   BRENDA; 2.7.1.160; 1856.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.170.30; -; 1.
DR   HAMAP; MF_00299; KptA; 1.
DR   InterPro; IPR002745; Ptrans_KptA/Tpt1.
DR   InterPro; IPR042081; RNA_2'-PTrans_C.
DR   InterPro; IPR022928; RNA_2'-PTrans_KptA.
DR   Pfam; PF01885; PTS_2-RNA; 1.
PE   3: Inferred from homology;
KW   NAD; Reference proteome; Transferase.
FT   CHAIN           1..283
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157479"
SQ   SEQUENCE   283 AA;  30191 MW;  7ABADB02576F624B CRC64;
     MLRRAQTCRS ATGNGGLKAT VTLQAGFPGV HGVYRHAEVL SNLSVSMRPT FNPFKRGQAA
     LLKLSAGILG RLPSGHTASL PIHTYTVINS AARGHCSFSL PQNRRRRLGL PAEGVPLDPA
     LKNGACASLS VRRWRLFSAA PRAGEGWRHA GTRRVGAAGA AARLPAGQPG APDAIRREGL
     RPVHRHHVSL SADTGAAQQV GARRGRAVAL VVATGALREA GYDFFRSDNG VWLTDTVPPE
     YLIRFQIESR TYPGAILRGA HGKNTVLRRW TGIRRLSGCS GIG