KPTA_PYRFU
ID KPTA_PYRFU Reviewed; 183 AA.
AC Q8U4K2;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 25-MAY-2022, entry version 87.
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=PF0083;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL80207.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009950; AAL80207.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011011195.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U4K2; -.
DR SMR; Q8U4K2; -.
DR STRING; 186497.PF0083; -.
DR EnsemblBacteria; AAL80207; AAL80207; PF0083.
DR GeneID; 41711871; -.
DR KEGG; pfu:PF0083; -.
DR PATRIC; fig|186497.12.peg.87; -.
DR eggNOG; arCOG04063; Archaea.
DR HOGENOM; CLU_052998_4_1_2; -.
DR OMA; EHGYFRG; -.
DR OrthoDB; 74155at2157; -.
DR PhylomeDB; Q8U4K2; -.
DR Proteomes; UP000001013; 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..183
FT /note="Probable RNA 2'-phosphotransferase"
FT /id="PRO_0000157492"
SQ SEQUENCE 183 AA; 21361 MW; CD2AE3B79F764CDE CRC64;
MVGGDRRFKV SKLMAYILRH SPWEFGLEPD EEGFVELADL IRAIKTVYPW VTEEFIKEIV
EKDSKGRYEI RGSKIRARYG HSYPVVLKHE EDTESKVLYH GTIRENLKGI LKEGIKPMKR
QYVHLSLSYE DAYYTGRRHG KDVVVLLIDA ECLRRKGYKI LKAGKRVRIV KHVPVECISE
ILD