KPTA_METBF
ID KPTA_METBF Reviewed; 207 AA.
AC Q46DV8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Mbar_A0962;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ69934.1; -; Genomic_DNA.
DR RefSeq; WP_011305983.1; NC_007355.1.
DR AlphaFoldDB; Q46DV8; -.
DR SMR; Q46DV8; -.
DR STRING; 269797.Mbar_A0962; -.
DR EnsemblBacteria; AAZ69934; AAZ69934; Mbar_A0962.
DR GeneID; 3626458; -.
DR KEGG; mba:Mbar_A0962; -.
DR eggNOG; arCOG04063; Archaea.
DR HOGENOM; CLU_052998_4_1_2; -.
DR OMA; EHGYFRG; -.
DR OrthoDB; 74155at2157; -.
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..207
FT /note="Probable RNA 2'-phosphotransferase"
FT /id="PRO_0000231958"
SQ SEQUENCE 207 AA; 24164 MW; C65EA96118C680D5 CRC64;
MIRKCTEHGY FRGGSCLQCK RPGRYLLDDN KEEKLGRFVS GTLRHFPESA GVTMDRFGWV
NINDFCDVMR KRYSWMRKEY LYALVESDEK GRYEIRNSRI RARYGHSVNI DLDYRESDSP
YLYYGASPEE VDVLLENGIF PIKQRYVHLS TSYEKAVEVA LIHTENPVIL QIDAFKAQED
GISLKLATDD IVLAERIPPE YLFVVEE