ID   KPTA_METAC              Reviewed;         207 AA.
AC   Q8TH84;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=MA_4638;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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; AE010299; AAM07972.1; -; Genomic_DNA.
DR   RefSeq; WP_011024506.1; NC_003552.1.
DR   AlphaFoldDB; Q8TH84; -.
DR   SMR; Q8TH84; -.
DR   STRING; 188937.MA_4638; -.
DR   EnsemblBacteria; AAM07972; AAM07972; MA_4638.
DR   GeneID; 1476532; -.
DR   KEGG; mac:MA_4638; -.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   InParanoid; Q8TH84; -.
DR   OMA; EHGYFRG; -.
DR   OrthoDB; 74155at2157; -.
DR   PhylomeDB; Q8TH84; -.
DR   Proteomes; UP000002487; Chromosome.
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; IBA:GO_Central.
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_0000157487"
SQ   SEQUENCE   207 AA;  24023 MW;  5ACF31D742BA6341 CRC64;
     MIRKCTEHGY FRGGSCQQCK RPGRYVLDDS REEKLGRFVS GTLRHFPASA GVKMDEYGWV
     DLNAFCDVMK KRYNWMRKEY LYALVESDEK GRYQIRGFMI RARYGHSVNI ELDYEESDAP
     YVYYGASPEE VDVLLENGIF PIKQRYVHLS TSYEKAAEVA LIHTESPVIL QVDAFRAQED
     GISLKLATDY IVLAEKIPPE YLYVIEE