THPR_PYRHO
ID THPR_PYRHO Reviewed; 184 AA.
AC O57823;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=PH0099;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=16131753; DOI=10.1107/s0907444905017841;
RA Rehse P.H., Tahirov T.H.;
RT "Structure of a putative 2'-5' RNA ligase from Pyrococcus horikoshii.";
RL Acta Crystallogr. D 61:1207-1212(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=17142895; DOI=10.1107/s1744309106046616;
RA Gao Y.G., Yao M., Okada A., Tanaka I.;
RT "The structure of Pyrococcus horikoshii 2'-5' RNA ligase at 1.94 A
RT resolution reveals a possible open form with a wider active-site cleft.";
RL Acta Crystallogr. F 62:1196-1200(2006).
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; BA000001; BAA29168.1; -; Genomic_DNA.
DR PIR; A71230; A71230.
DR RefSeq; WP_010884220.1; NC_000961.1.
DR PDB; 1VDX; X-ray; 2.40 A; A=1-184.
DR PDB; 1VGJ; X-ray; 1.94 A; A=1-184.
DR PDBsum; 1VDX; -.
DR PDBsum; 1VGJ; -.
DR AlphaFoldDB; O57823; -.
DR SMR; O57823; -.
DR STRING; 70601.3256485; -.
DR EnsemblBacteria; BAA29168; BAA29168; BAA29168.
DR GeneID; 1444002; -.
DR KEGG; pho:PH0099; -.
DR eggNOG; arCOG01736; Archaea.
DR OMA; HITLRFL; -.
DR OrthoDB; 102399at2157; -.
DR BRENDA; 6.5.1.B3; 5244.
DR EvolutionaryTrace; O57823; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..184
FT /note="RNA 2',3'-cyclic phosphodiesterase"
FT /id="PRO_0000138965"
FT MOTIF 40..43
FT /note="HXTX 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT ECO:0000305|PubMed:17142895"
FT MOTIF 125..128
FT /note="HXTX 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT ECO:0000305|PubMed:17142895"
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..8
FT /evidence="ECO:0007829|PDB:1VGJ"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1VGJ"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1VGJ"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:1VGJ"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:1VGJ"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:1VGJ"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:1VGJ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:1VGJ"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:1VGJ"
SQ SEQUENCE 184 AA; 21096 MW; F9C5C5D6BA897CE3 CRC64;
MRAFIAIDVN ESVRDSLVRA QDYIGSKEAK IKFVERENLH ITLKFLGEIT EEQAEEIKNI
LKKIAEKYKK HEVKVKGIGV FPNPNYIRVI WAGIENDEII REMAREIEDE LAKLGFKKEG
NFVAHITLGR VKFVKDKLGL TMKLKELANE DFGSFVVDAI ELKKSTLTPK GPIYETLARF
ELSE
