(data stored in ACNUC7421 zone)

SWISSPROT: RNH_ECODH

ID   RNH_ECODH               Reviewed;         155 AA.
AC   B1XD78;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 53.
DE   RecName: Full=Ribonuclease H {ECO:0000255|HAMAP-Rule:MF_00042};
DE            Short=RNase H {ECO:0000255|HAMAP-Rule:MF_00042};
DE            EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00042};
GN   Name=rnhA {ECO:0000255|HAMAP-Rule:MF_00042};
GN   OrderedLocusNames=ECDH10B_0195;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00042};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00042}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000255|HAMAP-
CC       Rule:MF_00042}.
DR   EMBL; CP000948; ACB01387.1; -; Genomic_DNA.
DR   RefSeq; WP_000917883.1; NC_010473.1.
DR   ProteinModelPortal; B1XD78; -.
DR   SMR; B1XD78; -.
DR   EnsemblBacteria; ACB01387; ACB01387; ECDH10B_0195.
DR   KEGG; ecd:ECDH10B_0195; -.
DR   eggNOG; ENOG4108UMW; Bacteria.
DR   eggNOG; COG0328; LUCA.
DR   HOGENOM; HOG000040465; -.
DR   KO; K03469; -.
DR   OMA; MQEIEIF; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
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_dom.
DR   InterPro; IPR002156; RNaseH_domain.
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; B1XD78.
DR   SWISS-2DPAGE; B1XD78.
KW   Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease.
FT   CHAIN         1    155       Ribonuclease H.
FT                                /FTId=PRO_1000090899.
FT   DOMAIN        1    142       RNase H. {ECO:0000255|HAMAP-
FT                                Rule:MF_00042}.
FT   METAL        10     10       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00042}.
FT   METAL        10     10       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00042}.
FT   METAL        48     48       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00042}.
FT   METAL        70     70       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00042}.
FT   METAL       134    134       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00042}.
SQ   SEQUENCE   155 AA;  17597 MW;  B8EF81EEB2F94CBE CRC64;
     MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM AAIVALEALK
     EHCEVILSTD SQYVRQGITQ WIHNWKKRGW KTADKKPVKN VDLWQRLDAA LGQHQIKWEW
     VKGHAGHPEN ERCDELARAA AMNPTLEDTG YQVEV
//

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