THPR_PYRFU
ID THPR_PYRFU Reviewed; 184 AA.
AC Q8U4Q3;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, 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, ECO:0000269|PubMed:19155324};
GN OrderedLocusNames=PF0027 {ECO:0000312|EMBL:AAL80151.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND STRUCTURE BY NMR.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=19155324; DOI=10.1261/rna.1122109;
RA Kanai A., Sato A., Fukuda Y., Okada K., Matsuda T., Sakamoto T., Muto Y.,
RA Yokoyama S., Kawai G., Tomita M.;
RT "Characterization of a heat-stable enzyme possessing GTP-dependent RNA
RT ligase activity from a hyperthermophilic archaeon, Pyrococcus furiosus.";
RL RNA 15:420-431(2009).
CC -!- FUNCTION: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-
CC phosphomonoester. In vitro, ligates 5' and 3' half-tRNA molecules with
CC 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the
CC product containing the 2'-5' phosphodiester linkage. Ligase activity
CC requires GTP, but GTP hydrolysis is not required for the reaction,
CC which is reversible. Ligase activity is weak compared to the
CC phosphodiesterase activity. {ECO:0000269|PubMed:19155324}.
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 ECO:0000269|PubMed:19155324};
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. ThpR family.
CC {ECO:0000255|HAMAP-Rule:MF_01940}.
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DR EMBL; AE009950; AAL80151.1; -; Genomic_DNA.
DR RefSeq; WP_011011139.1; NZ_CP023154.1.
DR PDB; 2FYH; NMR; -; A=1-184.
DR PDBsum; 2FYH; -.
DR AlphaFoldDB; Q8U4Q3; -.
DR BMRB; Q8U4Q3; -.
DR SMR; Q8U4Q3; -.
DR STRING; 186497.PF0027; -.
DR EnsemblBacteria; AAL80151; AAL80151; PF0027.
DR GeneID; 41711813; -.
DR KEGG; pfu:PF0027; -.
DR PATRIC; fig|186497.12.peg.29; -.
DR eggNOG; arCOG01736; Archaea.
DR HOGENOM; CLU_081251_3_4_2; -.
DR OMA; HITLRFL; -.
DR OrthoDB; 102399at2157; -.
DR PhylomeDB; Q8U4Q3; -.
DR BRENDA; 3.1.4.58; 5243.
DR BRENDA; 6.5.1.B3; 5243.
DR EvolutionaryTrace; Q8U4Q3; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..184
FT /note="RNA 2',3'-cyclic phosphodiesterase"
FT /id="PRO_0000431803"
FT MOTIF 40..43
FT /note="HXTX 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT ECO:0000305|PubMed:19155324"
FT MOTIF 125..128
FT /note="HXTX 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT ECO:0000305|PubMed:19155324"
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"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2FYH"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2FYH"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2FYH"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:2FYH"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:2FYH"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:2FYH"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:2FYH"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:2FYH"
SQ SEQUENCE 184 AA; 20995 MW; 99B45A0210A31E33 CRC64;
MRAFIAIDVS ESVRDALVRA QDYIGSKEAK IKFVERENFH ITLKFLGEIT EEQAEEIKKI
LEKIAKKYKK HEVNVRGIGV FPNPNYVRVI WAGVENDEII KKIAKEIDDE LAKLGFKKEG
NFVAHITLGR VKFVKDKLGL AMKLKELANE DFGSFIVEAI ELKKSTLTPK GPIYETLARF
ELSE
