ID   KPTA_THEON              Reviewed;         180 AA.
AC   B6YXF3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Probable RNA 2'-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00299};
DE            EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_00299};
GN   Name=kptA {ECO:0000255|HAMAP-Rule:MF_00299}; OrderedLocusNames=TON_1278;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00299}.
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00299}.
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DR   EMBL; CP000855; ACJ16766.1; -; Genomic_DNA.
DR   RefSeq; WP_012572238.1; NC_011529.1.
DR   AlphaFoldDB; B6YXF3; -.
DR   SMR; B6YXF3; -.
DR   STRING; 523850.TON_1278; -.
DR   EnsemblBacteria; ACJ16766; ACJ16766; TON_1278.
DR   GeneID; 7018304; -.
DR   KEGG; ton:TON_1278; -.
DR   PATRIC; fig|523850.10.peg.1286; -.
DR   eggNOG; arCOG04063; Archaea.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   OMA; TEEPVHC; -.
DR   OrthoDB; 74155at2157; -.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.970; -; 1.
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   InterPro; IPR042080; RNA_2'-PTrans_N.
DR   PANTHER; PTHR12684; PTHR12684; 1.
DR   Pfam; PF01885; PTS_2-RNA; 1.
PE   3: Inferred from homology;
KW   NAD; Transferase.
FT   CHAIN           1..180
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_1000115317"
SQ   SEQUENCE   180 AA;  20798 MW;  408F1C07FF92CA7C CRC64;
     MFPGRRKVSK LMAYILRHSP EEFGLRPDVE GFVPLSELVE ALKTIYPDVT EEFVREIVAR
     DAKGRYEIQG DRIRARYGHS FPVSLDHEED TESRFLYHGT PRRNLESILR EGLKPMRRQF
     VHLSTSKSEA IKTGRRHGRD VVLLVIDAEC LRKKGLKVYK AGKNVRIVEK VPPECITLEV