(data stored in ACNUC7421 zone)

SWISSPROT: Q47TD6_THEFY

ID   Q47TD6_THEFY            Unreviewed;       182 AA.
AC   Q47TD6;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=RNA 2',3'-cyclic phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_01940};
DE            Short=RNA 2',3'-CPDase {ECO:0000256|HAMAP-Rule:MF_01940};
DE            EC=3.1.4.58 {ECO:0000256|HAMAP-Rule:MF_01940};
GN   OrderedLocusNames=Tfu_0243 {ECO:0000313|EMBL:AAZ54281.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54281.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-
CC       phosphomonoester. {ECO:0000256|HAMAP-Rule:MF_01940}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + RNA(n)-2',3'-cyclic phosphate = H(+) + RNA(n)-
CC         2'- phosphate; Xref=Rhea:RHEA:11828, Rhea:RHEA-COMP:13350,
CC         Rhea:RHEA-COMP:13351, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:136820, ChEBI:CHEBI:136821; EC=3.1.4.58;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01940};
CC   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. ThpR
CC       family. {ECO:0000256|HAMAP-Rule:MF_01940}.
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DR   EMBL; CP000088; AAZ54281.1; -; Genomic_DNA.
DR   RefSeq; WP_011290690.1; NC_007333.1.
DR   STRING; 269800.Tfu_0243; -.
DR   EnsemblBacteria; AAZ54281; AAZ54281; Tfu_0243.
DR   KEGG; tfu:Tfu_0243; -.
DR   eggNOG; ENOG4105UKC; Bacteria.
DR   eggNOG; COG1514; LUCA.
DR   HOGENOM; HOG000226389; -.
DR   OMA; PLDYHIT; -.
DR   OrthoDB; 1696971at2; -.
DR   BioCyc; TFUS269800:G1G4Q-248-MONOMER; -.
DR   Proteomes; UP000000434; 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; cNuc_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;
DR   PRODOM; Q47TD6.
DR   SWISS-2DPAGE; Q47TD6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01940};
KW   Ligase {ECO:0000313|EMBL:AAZ54281.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN        8     92       LigT_PEase. {ECO:0000259|Pfam:PF02834}.
FT   DOMAIN      100    170       LigT_PEase. {ECO:0000259|Pfam:PF02834}.
FT   MOTIF        40     43       HXTX 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
FT   MOTIF       128    131       HXTX 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
FT   ACT_SITE     40     40       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
FT   ACT_SITE    128    128       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
SQ   SEQUENCE   182 AA;  19553 MW;  54A3AEDF698216FB CRC64;
     MRLFTAVTPP AAALDALDAA VASARPTARG LRWVAREQWH MTLVFLGDVP DDQVDTVAGE
     LGRVAARHPA MSLSLRGSGT FPPQPVRSRV LWAGVDGDTA ALTALATDLR EAAVALGIPV
     ENRRYVPHVT VARARITTNL TAPCARLETL ATEPWQAAEV HLVHSRLGAV PRYQTIATWK
     LA
//

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