ID   KPTA_HYPBU              Reviewed;         233 AA.
AC   A2BMI7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=Hbut_1373;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM81198.1; -; Genomic_DNA.
DR   RefSeq; WP_011822516.1; NC_008818.1.
DR   AlphaFoldDB; A2BMI7; -.
DR   SMR; A2BMI7; -.
DR   STRING; 415426.Hbut_1373; -.
DR   EnsemblBacteria; ABM81198; ABM81198; Hbut_1373.
DR   GeneID; 4782171; -.
DR   KEGG; hbu:Hbut_1373; -.
DR   eggNOG; arCOG04063; Archaea.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   OMA; TEEPVHC; -.
DR   OrthoDB; 74155at2157; -.
DR   Proteomes; UP000002593; 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..233
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_1000022016"
SQ   SEQUENCE   233 AA;  26480 MW;  3148D9D1FD2171DB CRC64;
     MKPVYRCRVC SAYTEEPVHC GRPAEPLMTG EQRLRLSKLM TTLLRHLPHE AGLRLDPQGW
     VGIDELVRGI RERWRNRHLY QWVTRDHVIA VALLDPKGRF QLDLARGRIR AAYGHTVRVE
     LGYRPLSMDE LPDKLYHGTV AENLASILSE GLKPMRRLMV HMTTDYSSAV ETGRRHGPNV
     VVLVIDPRCL AKHGIPVYRA SDTIYLAPSV PPNCITGKIA RNPQSARKTY LHA