KPTA_PYRHO
ID KPTA_PYRHO Reviewed; 177 AA.
AC O57899;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable RNA 2'-phosphotransferase;
DE EC=2.7.1.-;
GN Name=kptA; OrderedLocusNames=PH0160;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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}.
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DR EMBL; BA000001; BAA29229.1; -; Genomic_DNA.
DR PIR; F71237; F71237.
DR AlphaFoldDB; O57899; -.
DR SMR; O57899; -.
DR STRING; 70601.3256546; -.
DR EnsemblBacteria; BAA29229; BAA29229; BAA29229.
DR KEGG; pho:PH0160; -.
DR eggNOG; arCOG04063; Archaea.
DR OMA; EHGYFRG; -.
DR BRENDA; 2.7.1.160; 5244.
DR Proteomes; UP000000752; 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; Transferase.
FT CHAIN 1..177
FT /note="Probable RNA 2'-phosphotransferase"
FT /id="PRO_0000157493"
SQ SEQUENCE 177 AA; 20868 MW; B69926274B3E04B8 CRC64;
MRFKVSKLMA YILRHSPWEF GLEPDEEGFV SIEELVNAVR KVYPWVTEEY IREIVERDEK
GRYEIRGNKI RARYGHSYPV ILRHEEDKES KVLYHGTVRR NLKGIMREGI KPMKRQYVHL
SINYEDAYNT GRRHGEDVVV LIIDAECLRN KGYKILKAGK KVRIVKHVPV DCISGIL