ID   THPR_AQUAE              Reviewed;         188 AA.
AC   O66967;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=aq_768;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}.
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DR   EMBL; AE000657; AAC06930.1; -; Genomic_DNA.
DR   PIR; D70367; D70367.
DR   RefSeq; NP_213528.1; NC_000918.1.
DR   AlphaFoldDB; O66967; -.
DR   SMR; O66967; -.
DR   STRING; 224324.aq_768; -.
DR   EnsemblBacteria; AAC06930; AAC06930; aq_768.
DR   KEGG; aae:aq_768; -.
DR   PATRIC; fig|224324.8.peg.611; -.
DR   eggNOG; COG1514; Bacteria.
DR   HOGENOM; CLU_081251_3_2_0; -.
DR   InParanoid; O66967; -.
DR   OMA; HITLRFL; -.
DR   OrthoDB; 1696971at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR   GO; GO:0010738; P:regulation of protein kinase A signaling; IBA:GO_Central.
DR   HAMAP; MF_01940; RNA_CPDase; 1.
DR   InterPro; IPR009097; Cyclic_Pdiesterase.
DR   InterPro; IPR014051; Phosphoesterase_HXTX.
DR   InterPro; IPR004175; RNA_CPDase.
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..188
FT                   /note="RNA 2',3'-cyclic phosphodiesterase"
FT                   /id="PRO_0000138966"
FT   MOTIF           42..45
FT                   /note="HXTX 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT   MOTIF           130..133
FT                   /note="HXTX 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT   ACT_SITE        42
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
SQ   SEQUENCE   188 AA;  21366 MW;  8452945D171DBDEA CRC64;
     MKVVRAFVGF FTSKSINEVA ERIKKEVDLK IMGKWVEPQN VHMTLQFLGD ITEAQAIEVI
     KNLQEISKKN IPFRIKYKGL GVFPDVKRPR VLWIGVSEGA NKLTNLAKEV ARLNAKKGII
     PKNSKNFVPH VTICRIKSYD RKTLNELLRK YRTVEFGEDE VNKIALISST LTSVGPIYTV
     VEEFYLGG