ID   KPTA_PYRAB              Reviewed;         183 AA.
AC   Q9V2B7; G8ZFZ2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Probable RNA 2'-phosphotransferase;
DE            EC=2.7.1.-;
GN   Name=kptA; OrderedLocusNames=PYRAB01570; ORFNames=PAB2247;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB49081.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69533.1; -; Genomic_DNA.
DR   PIR; B75204; B75204.
DR   AlphaFoldDB; Q9V2B7; -.
DR   SMR; Q9V2B7; -.
DR   STRING; 272844.PAB2247; -.
DR   EnsemblBacteria; CAB49081; CAB49081; PAB2247.
DR   KEGG; pab:PAB2247; -.
DR   PATRIC; fig|272844.11.peg.170; -.
DR   eggNOG; arCOG04063; Archaea.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   OMA; TEEPVHC; -.
DR   PhylomeDB; Q9V2B7; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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..183
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157490"
SQ   SEQUENCE   183 AA;  21501 MW;  DEC04CDF6FA4FBED CRC64;
     MGKAQSVRFK VSKLMAYILR HDPWSFNLQP DEEGFVDLEE FVNAIRRVYP WVTKEFILDI
     VERDEKERYE VKEGKIRARY GHSYPVILDH KEDKESKTLY HGTIRENLEG IMREGIKPMK
     RQFVHLSLNY EDAYNTGRRH GSNVVVLMID ADCLRKKGFK ILKAGKKVRI VKYVPVDCIV
     GEL