ID   THPR_ARCFU              Reviewed;         176 AA.
AC   O28125;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=AF_2157;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB89083.1; -; Genomic_DNA.
DR   PIR; E69519; E69519.
DR   RefSeq; WP_010879646.1; NC_000917.1.
DR   AlphaFoldDB; O28125; -.
DR   SMR; O28125; -.
DR   STRING; 224325.AF_2157; -.
DR   EnsemblBacteria; AAB89083; AAB89083; AF_2157.
DR   GeneID; 24795904; -.
DR   KEGG; afu:AF_2157; -.
DR   eggNOG; arCOG01736; Archaea.
DR   HOGENOM; CLU_081251_3_4_2; -.
DR   OMA; HITLRFL; -.
DR   OrthoDB; 102399at2157; -.
DR   PhylomeDB; O28125; -.
DR   Proteomes; UP000002199; 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_0000138962"
FT   MOTIF           39..42
FT                   /note="HXTX 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT   MOTIF           122..125
FT                   /note="HXTX 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT   ACT_SITE        39
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT   ACT_SITE        122
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
SQ   SEQUENCE   176 AA;  20060 MW;  B0680DE85A3F9E71 CRC64;
     MRLFVAVDVD DSIREKVKPI LKELSGVSGV KAVEPENLHI TLLFLGEVGE EKLARIEERL
     SEVTFQPFKI SFEGVGAFPN PGSPRVVWIG VKEEGELTRL ANSVYEKLKK LGFRRDKDFK
     AHLTVGRVKR KNPEVADIVR KYSSESFGEM EVRDFRLKQS ILTPKGPIYK DLRVFE