ID   M7TAX3_9EURY            Unreviewed;       225 AA.
AC   M7TAX3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   13-APR-2016, entry version 13.
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; Thermoplasmata; 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
CC       presumed transesterification to release the RNA and generate ADP-
CC       ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-
CC       ribosylase. {ECO:0000256|HAMAP-Rule:MF_00299}.
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00299}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {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:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00299; KptA; 1.
DR   InterPro; IPR002745; Ptrans_KptA/Tpt1.
DR   InterPro; IPR022928; RNA_2'-PTrans_KptA.
DR   Pfam; PF01885; PTS_2-RNA; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053781};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00299};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00299,
KW   ECO:0000313|EMBL:EMR74008.1}.
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
//