(data stored in SCRATCH zone)

SWISSPROT: C8U1S6_ECO10

ID   C8U1S6_ECO10            Unreviewed;       155 AA.
AC   C8U1S6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Ribonuclease H {ECO:0000256|HAMAP-Rule:MF_00042, ECO:0000256|SAAS:SAAS01082054};
DE            Short=RNase H {ECO:0000256|HAMAP-Rule:MF_00042};
DE            EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00042, ECO:0000256|SAAS:SAAS01082054};
GN   Name=rnhA {ECO:0000256|HAMAP-Rule:MF_00042,
GN   ECO:0000313|EMBL:BAI29084.1};
GN   OrderedLocusNames=ECO103_0208 {ECO:0000313|EMBL:BAI29084.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29084.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29084.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS01082064}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         EC=3.1.26.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00042,
CC         ECO:0000256|SAAS:SAAS01118375};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00042};
CC       Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion
CC       at a regulatory site, or after substrate binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00042};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS01082108}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042,
CC       ECO:0000256|SAAS:SAAS01082116}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000256|HAMAP-
CC       Rule:MF_00042, ECO:0000256|SAAS:SAAS01082081}.
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DR   EMBL; AP010958; BAI29084.1; -; Genomic_DNA.
DR   RefSeq; WP_000917888.1; NC_013353.1.
DR   SMR; C8U1S6; -.
DR   EnsemblBacteria; BAI29084; BAI29084; ECO103_0208.
DR   KEGG; eoh:ECO103_0208; -.
DR   HOGENOM; HOG000040465; -.
DR   KO; K03469; -.
DR   OMA; MQEIEIF; -.
DR   BioCyc; ECOL585395:ECO103_RS01090-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd09278; RNase_HI_prokaryote_like; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00042; RNase_H; 1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR022892; RNaseHI.
DR   Pfam; PF00075; RNase_H; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50879; RNASE_H; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1S6.
DR   SWISS-2DPAGE; C8U1S6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS01082089};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS01082063};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS01082115};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS01082062};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS01082080};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00042,
KW   ECO:0000256|SAAS:SAAS01082100}.
FT   DOMAIN        1    142       RNase H. {ECO:0000259|PROSITE:PS50879}.
FT   METAL        10     10       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        10     10       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        48     48       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL        70     70       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
FT   METAL       134    134       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00042}.
SQ   SEQUENCE   155 AA;  17570 MW;  3BC69BDD9BF94CAF CRC64;
     MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM AAIVALEALK
     EHCEVILSTD SQYVRQGITQ WIHSWKKRGW KTADKKPVKN VDLWQRLDAA LGQHQIKWEW
     VKGHAGHPEN ERCDELARAA AMNPTLEDTG YQVEV
//

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