KPTA_AERPE
ID KPTA_AERPE Reviewed; 220 AA.
AC Q9YFP5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable RNA 2'-phosphotransferase;
DE EC=2.7.1.-;
GN Name=kptA; OrderedLocusNames=APE_0204.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000002; BAA79116.2; -; Genomic_DNA.
DR PIR; B72777; B72777.
DR PDB; 1WFX; X-ray; 2.80 A; A=35-220.
DR PDBsum; 1WFX; -.
DR AlphaFoldDB; Q9YFP5; -.
DR SMR; Q9YFP5; -.
DR STRING; 272557.APE_0204.1; -.
DR EnsemblBacteria; BAA79116; BAA79116; APE_0204.1.
DR KEGG; ape:APE_0204.1; -.
DR PATRIC; fig|272557.25.peg.146; -.
DR eggNOG; arCOG04063; Archaea.
DR OMA; TEEPVHC; -.
DR BRENDA; 2.7.1.160; 171.
DR EvolutionaryTrace; Q9YFP5; -.
DR Proteomes; UP000002518; 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 1: Evidence at protein level;
KW 3D-structure; NAD; Reference proteome; Transferase.
FT CHAIN 1..220
FT /note="Probable RNA 2'-phosphotransferase"
FT /id="PRO_0000157484"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1WFX"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1WFX"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1WFX"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:1WFX"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:1WFX"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:1WFX"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:1WFX"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1WFX"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1WFX"
SQ SEQUENCE 220 AA; 24703 MW; 57DA42C6A4159156 CRC64;
MAEELPELAL CCDGTVVEGR SNCRCKARAV LPGGMRVRLS KTLAGILRHH PGRYGVRLTR
EGWARVSEVV EGLRKAGWSW VEEWHIVGVA LHDPKGRYEL RNGEIRARYG HSIPVNVEPL
PGEPPPILYH GTTEEALPLI MERGIMRGRR LKVHLTSSLE DAVSTGRRHG NLVAVLLVDV
ECLRRRGLKV ERMSKTVYTV DWVPPECIAE VRRESLGRSL