THPR_THEMA
ID THPR_THEMA Reviewed; 187 AA.
AC Q9X2H4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=TM_1860;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(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}.
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DR EMBL; AE000512; AAD36922.1; -; Genomic_DNA.
DR PIR; E72201; E72201.
DR RefSeq; NP_229656.1; NC_000853.1.
DR RefSeq; WP_004082411.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X2H4; -.
DR SMR; Q9X2H4; -.
DR STRING; 243274.THEMA_04870; -.
DR EnsemblBacteria; AAD36922; AAD36922; TM_1860.
DR KEGG; tma:TM1860; -.
DR eggNOG; COG1514; Bacteria.
DR InParanoid; Q9X2H4; -.
DR OMA; HITLRFL; -.
DR OrthoDB; 1696971at2; -.
DR Proteomes; UP000008183; 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; IPR004175; RNA_CPDase.
DR PANTHER; PTHR35561; PTHR35561; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
DR TIGRFAMs; TIGR02258; 2_5_ligase; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..187
FT /note="RNA 2',3'-cyclic phosphodiesterase"
FT /id="PRO_0000138969"
FT MOTIF 40..43
FT /note="HXTX 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT MOTIF 125..128
FT /note="HXTX 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
SQ SEQUENCE 187 AA; 22065 MW; 912D041454F0C921 CRC64;
MRTFIAIDVN EEVKKQASEI IEKLMKRGFG ATWVSEENMH LTLFFLGEVD EQKISEIAEH
LCRRVRGFPS FSFTVKGFGY FKRKMSPRVF WLGVENTDRL MKLYEELRNE LSHHGFSFEE
KFVPHITIGR VKYYPDKWEK LIEDIDFPPI EVAVDRFKIY SSTLTPTGPI YKVLYECQFE
GGLIRYA