(data stored in ACNUC7421 zone)

SWISSPROT: B7UIJ1_ECO27

ID   B7UIJ1_ECO27            Unreviewed;       176 AA.
AC   B7UIJ1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JAN-2019, entry version 50.
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   Name=ligT {ECO:0000313|EMBL:CAS07698.1};
GN   Synonyms=thpR {ECO:0000256|HAMAP-Rule:MF_01940};
GN   OrderedLocusNames=E2348C_0150 {ECO:0000313|EMBL:CAS07698.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07698.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07698.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS07698.1; -; Genomic_DNA.
DR   RefSeq; WP_001294702.1; NC_011601.1.
DR   EnsemblBacteria; CAS07698; CAS07698; E2348C_0150.
DR   KEGG; ecg:E2348C_0150; -.
DR   HOGENOM; HOG000226389; -.
DR   KO; K01975; -.
DR   OMA; GVVWLGC; -.
DR   BioCyc; ECOL574521:E2348C_RS00775-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UIJ1.
DR   SWISS-2DPAGE; B7UIJ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01940};
KW   Ligase {ECO:0000313|EMBL:CAS07698.1}.
FT   DOMAIN       11     89       LigT_PEase. {ECO:0000259|Pfam:PF02834}.
FT   DOMAIN       92    166       LigT_PEase. {ECO:0000259|Pfam:PF02834}.
FT   MOTIF        43     46       HXTX 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
FT   MOTIF       125    128       HXTX 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
FT   ACT_SITE     43     43       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
FT   ACT_SITE    125    125       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01940}.
SQ   SEQUENCE   176 AA;  19964 MW;  9DAA9FB3DA1E327E CRC64;
     MSEPQRLFFA IDLPAEIREQ IIHWRATHFP PEAGRPVAAD NLHLTLAFLG EVSAEKEKAL
     SLLAGRIRQP GFTLTLDDAG QWLRSRVVWL GMRQPPRGLI QLANMLRSQA ARSGCFQSNR
     PFHPHITLLR DASEAVTIPP PGFNWSYTVT EFTLYASSFA RGRTRYTPLK RWALTQ
//

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