THPR_AERPE
ID THPR_AERPE Reviewed; 176 AA.
AC Q9YB03;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=RNA 2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01940};
DE Short=RNA 2',3'-CPDase {ECO:0000255|HAMAP-Rule:MF_01940};
DE EC=3.1.4.58 {ECO:0000255|HAMAP-Rule:MF_01940};
GN OrderedLocusNames=APE_1792;
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: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-
CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_01940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-
CC end 2'-phospho-ribonucleotide-RNA + H(+); Xref=Rhea:RHEA:11828,
CC Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:17353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83064, ChEBI:CHEBI:173113;
CC EC=3.1.4.58; Evidence={ECO:0000255|HAMAP-Rule:MF_01940};
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. ThpR family.
CC {ECO:0000255|HAMAP-Rule:MF_01940}.
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; BAA80795.1; -; Genomic_DNA.
DR PIR; F72563; F72563.
DR AlphaFoldDB; Q9YB03; -.
DR SMR; Q9YB03; -.
DR STRING; 272557.APE_1792; -.
DR EnsemblBacteria; BAA80795; BAA80795; APE_1792.
DR KEGG; ape:APE_1792; -.
DR PATRIC; fig|272557.25.peg.1201; -.
DR eggNOG; arCOG01736; Archaea.
DR OMA; HITLRFL; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0008664; F:2'-5'-RNA ligase activity; IEA:InterPro.
DR HAMAP; MF_01940; RNA_CPDase; 1.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR014051; Phosphoesterase_HXTX.
DR InterPro; IPR004175; RNA_CPDase.
DR PANTHER; PTHR35561; PTHR35561; 1.
DR Pfam; PF02834; LigT_PEase; 2.
DR SUPFAM; SSF55144; SSF55144; 1.
DR TIGRFAMs; TIGR02258; 2_5_ligase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..176
FT /note="RNA 2',3'-cyclic phosphodiesterase"
FT /id="PRO_0000138961"
FT MOTIF 28..31
FT /note="HXTX 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT MOTIF 113..116
FT /note="HXTX 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT ACT_SITE 28
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT ACT_SITE 113
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
SQ SEQUENCE 176 AA; 19666 MW; C8BD5FC929F7E56D CRC64;
MVGRLARLRD SIAHTGVPMK TVEDENFHIT LRFIGEVSEP VAAEIGERLA SIRFERFRIE
LRGLGAFPRP DRPRVVWVGV GGGAGELRRI RDEVERILTS MGFSPEKQEF HPHVTLARIK
GARNLPALVK LLREMGDVEV GSVEVSSIRL KQSILTRQGP IYKTLYEVKA ASSGRV