ID   KPTA_HALMA              Reviewed;         222 AA.
AC   Q5UXB8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=rrnAC3404;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV48085.1; -; Genomic_DNA.
DR   RefSeq; WP_011224785.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UXB8; -.
DR   SMR; Q5UXB8; -.
DR   STRING; 272569.rrnAC3404; -.
DR   EnsemblBacteria; AAV48085; AAV48085; rrnAC3404.
DR   GeneID; 40154190; -.
DR   KEGG; hma:rrnAC3404; -.
DR   PATRIC; fig|272569.17.peg.3922; -.
DR   eggNOG; arCOG04063; Archaea.
DR   HOGENOM; CLU_052998_4_1_2; -.
DR   OMA; TEEPVHC; -.
DR   Proteomes; UP000001169; Chromosome I.
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..222
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000231957"
SQ   SEQUENCE   222 AA;  23867 MW;  B9A470C8F9103A6B CRC64;
     MPDAVRRCPE DGFFEGDTCP VCDGAGTHIL DGARRRQLSK FVSGALRHFP EDAGIEVDKA
     GWTGFDALRV AVERQYDWAD AAALAGVIAT DPKGRFERTG VGNEAGITTA GGRVRAAYGH
     SVDVTLDGTD DPVPATLYHG TAPRNVDSIR EAGLKPMSRQ TVHLSESAAA AREVGRRHAA
     DPVVFVVDAT AMQSDDRRIV KRGTETYTTD RVSPVYLSLL EK