ID   KPTA_METMA              Reviewed;         207 AA.
AC   Q8PXC3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=MM_1298;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(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; AE008384; AAM30994.1; -; Genomic_DNA.
DR   RefSeq; WP_011033245.1; NC_003901.1.
DR   AlphaFoldDB; Q8PXC3; -.
DR   SMR; Q8PXC3; -.
DR   STRING; 192952.MM_1298; -.
DR   EnsemblBacteria; AAM30994; AAM30994; MM_1298.
DR   GeneID; 44089087; -.
DR   GeneID; 66137270; -.
DR   KEGG; mma:MM_1298; -.
DR   PATRIC; fig|192952.21.peg.1509; -.
DR   eggNOG; arCOG04063; Archaea.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   OMA; EHGYFRG; -.
DR   Proteomes; UP000000595; 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..207
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157489"
SQ   SEQUENCE   207 AA;  23845 MW;  54D6E6E807794DA6 CRC64;
     MIRKCTDHGY FRGGSCQQCK RPGRYVLDDG REEKLGRFVS GTLRHFPASA GVKMDKYGWI
     DLNAFCEVMK KRYNWMRKEY LYALVESDEK GRYQISGPMI RARYGHSVNV DLDYDESDTP
     YVYYGASPEE VDVLLENGIF PIKQRYVHLS TTYEKAAEVA LIHTESPVIL QVDAFRAQED
     GISLKLATDY IVLAEKIPPD YLFVLED