THPR_METTH
ID THPR_METTH Reviewed; 184 AA.
AC O26683;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=MTH_583;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(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; AE000666; AAB85089.1; -; Genomic_DNA.
DR PIR; C69177; C69177.
DR RefSeq; WP_010876222.1; NC_000916.1.
DR AlphaFoldDB; O26683; -.
DR SMR; O26683; -.
DR STRING; 187420.MTH_583; -.
DR EnsemblBacteria; AAB85089; AAB85089; MTH_583.
DR GeneID; 24853719; -.
DR KEGG; mth:MTH_583; -.
DR PATRIC; fig|187420.15.peg.562; -.
DR HOGENOM; CLU_081251_3_4_2; -.
DR OMA; HNEEMAS; -.
DR Proteomes; UP000005223; 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; 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..184
FT /note="RNA 2',3'-cyclic phosphodiesterase"
FT /id="PRO_0000138964"
FT MOTIF 42..45
FT /note="HXTX 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
FT MOTIF 127..130
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 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940"
SQ SEQUENCE 184 AA; 21107 MW; 9F96678D65CC07D1 CRC64;
MKVRAFLAVD LDEGLRDHVS RIQDTLKSAD AQVKFVEPEN LHFTLKFFGD VGEGKLRRIE
NVVRDTLRGY EPFEISIRGA GVFPNPRYIR VVWLGVENPE TFSDLQRSLD MEFVKMGFRP
ERDYVPHLTV GRVKGPRNRD KLAELIGELQ NVEVGSMRVS EVSLKRSELT PAGPIYTDME
VFRL
