ID   KPTA_METKA              Reviewed;         234 AA.
AC   Q8X261;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=MK1434;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Belova G.I., Malykh A.G., Kozyavkin S.A., Slesarev A.I.;
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AF311944; AAL61957.1; -; Genomic_DNA.
DR   EMBL; AE009439; AAM02647.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X261; -.
DR   SMR; Q8X261; -.
DR   STRING; 190192.MK1434; -.
DR   EnsemblBacteria; AAM02647; AAM02647; MK1434.
DR   KEGG; mka:MK1434; -.
DR   PATRIC; fig|190192.8.peg.1590; -.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   OMA; TEEPVHC; -.
DR   Proteomes; UP000001826; 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; Reference proteome; Transferase.
FT   CHAIN           1..234
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157488"
SQ   SEQUENCE   234 AA;  27356 MW;  FEB9DDC384EEF521 CRC64;
     MKPIRVCPEC GKYTEKHTCE RCGRRTEEFL DGRRRLALSK LLSGILRHFP EEVKVKLDDE
     GFTDCDVHEL AERIKKYWKN REYYRWLTGE HIIAVVETCP KGRFEIDEHG RIRARYGHSR
     RLSVRPTLPE AENVKELYHG TARENLESIL QHGIKPMGRR AVHLTDDERE ALITALRHTR
     NPVILVVDAE RLRRHGLVPR KAGKNVYVVE GTVPPDCITR VIRNPRRSVE SEKR