ID   KPTA_PYRAE              Reviewed;         213 AA.
AC   Q8ZSP2;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=PAE3647;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(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; AE009441; AAL65071.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZSP2; -.
DR   SMR; Q8ZSP2; -.
DR   STRING; 178306.PAE3647; -.
DR   PRIDE; Q8ZSP2; -.
DR   EnsemblBacteria; AAL65071; AAL65071; PAE3647.
DR   KEGG; pai:PAE3647; -.
DR   PATRIC; fig|178306.9.peg.2752; -.
DR   eggNOG; arCOG04063; Archaea.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   InParanoid; Q8ZSP2; -.
DR   OMA; TEEPVHC; -.
DR   Proteomes; UP000002439; 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..213
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157491"
SQ   SEQUENCE   213 AA;  23452 MW;  12DF2AD12CE69636 CRC64;
     MNDVYKCPVC GQLTESPTHC GVSAVKILDG AMRLKISKLL SLALRHSPSV LGLSLDKGGW
     ADVKTALEGL RKAGIRADYE ALYAVVALDE KGRFELKDGK IRARYGHTID VEVEYEADSE
     SKVLYHGTSR HLLPSIMAQG LLPMRRRYVH LSPDFATACQ NARRRPLPVV IEIDAECLRA
     RGYVVYAASG KVRLAKHVPP ECLKKVVDCP TPS