ID   M7TAX3_9EURY            Unreviewed;       225 AA.
AC   M7TAX3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   07-APR-2021, entry version 21.
DE   RecName: Full=Probable RNA 2'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00299};
DE            EC=2.7.1.- {ECO:0000256|HAMAP-Rule:MF_00299};
GN   Name=kptA {ECO:0000256|HAMAP-Rule:MF_00299};
GN   ORFNames=MBGDN05_00382 {ECO:0000313|EMBL:EMR74008.1};
OS   Thermoplasmatales archaeon SCGC AB-539-N05.
OC   Archaea; Euryarchaeota; Diaforarchaea group; Thermoplasmata;
OC   Thermoplasmatales.
OX   NCBI_TaxID=1198116 {ECO:0000313|EMBL:EMR74008.1, ECO:0000313|Proteomes:UP000053781};
RN   [1] {ECO:0000313|EMBL:EMR74008.1, ECO:0000313|Proteomes:UP000053781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AB-539-N05 {ECO:0000313|EMBL:EMR74008.1};
RX   PubMed=23535597; DOI=10.1038/nature12033;
RA   Lloyd K.G., Schreiber L., Petersen D.G., Kjeldsen K.U., Lever M.A.,
RA   Steen A.D., Stepanauskas R., Richter M., Kleindienst S., Lenk S.,
RA   Schramm A., Jorgensen B.B.;
RT   "Predominant archaea in marine sediments degrade detrital proteins.";
RL   Nature 496:215-218(2013).
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:0000256|ARBA:ARBA00002203, ECO:0000256|HAMAP-Rule:MF_00299}.
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family.
CC       {ECO:0000256|ARBA:ARBA00009836, ECO:0000256|HAMAP-Rule:MF_00299}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMR74008.1}.
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DR   EMBL; ALXL01000032; EMR74008.1; -; Genomic_DNA.
DR   EnsemblBacteria; EMR74008; EMR74008; MBGDN05_00382.
DR   Proteomes; UP000053781; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00299};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053781};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00299}.
SQ   SEQUENCE   225 AA;  25191 MW;  2849492C2F0F8ECA CRC64;
     MFVMLAECSN HGYYRGEVCP VCDKKGKFLM NDNELGSLGR IMAGVLRHFP DKIGLMMDGK
     GWVDVSALVD ALCTSRSGFH WLRNQHIEAI AATDPKGRYQ IDGGMIRATY GHTIDLNLDD
     LPVTSKDKFY YPVTEEEAEI VLEGGLHPID RKKVHLSGTI EKAIEAGKVR TEDPFILSID
     GAKAKEDGIR IYHAGKEVYI TDSIDAKYIS KVDESEIKKL FEEKH
//