ID   KPTA_THEAC              Reviewed;         235 AA.
AC   P57718; Q9HLV7;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Probable RNA 2'-phosphotransferase;
DE            EC=2.7.1.-;
GN   Name=kptA; OrderedLocusNames=Ta0118;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC11265.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL445063; CAC11265.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010900545.1; NC_002578.1.
DR   AlphaFoldDB; P57718; -.
DR   SMR; P57718; -.
DR   STRING; 273075.Ta0118m; -.
DR   PRIDE; P57718; -.
DR   EnsemblBacteria; CAC11265; CAC11265; CAC11265.
DR   GeneID; 1456972; -.
DR   KEGG; tac:Ta0118; -.
DR   eggNOG; arCOG04063; Archaea.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   OMA; EHGYFRG; -.
DR   OrthoDB; 74155at2157; -.
DR   Proteomes; UP000001024; 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..235
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157495"
FT   REGION          208..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   235 AA;  27050 MW;  70A4062661D63253 CRC64;
     MPELRTCHGP YRGRECPVCG KPGKILMNER EVDEVSRTLA AILRHDPERY HIRLDSHGYA
     RIAGIVTVLR KYKGMKWITF DHILSLAETD PKGRYQVSGV LIRAMYGHTI PVDLSDLPED
     NIPDVLYYQS SAAEAPLVKE AGIYPSDKTW VHLSGTYRRS YVSGLYHIDD PFILRIDARS
     MIDSGHDIYR SSDDIYLTRE IPPEYIQDAE PEEVTLTEEE KMDIDRVRNK NKKDQ