(data stored in ACNUC7421 zone)

SWISSPROT: RNH2_ECO57

ID   RNH2_ECO57              Reviewed;         198 AA.
AC   Q8X8X6;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 91.
DE   RecName: Full=Ribonuclease HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE            Short=RNase HII {ECO:0000255|HAMAP-Rule:MF_00052};
DE            EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00052};
GN   Name=rnhB {ECO:0000255|HAMAP-Rule:MF_00052};
GN   OrderedLocusNames=Z0195, ECs0185;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids. {ECO:0000255|HAMAP-Rule:MF_00052}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_00052}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00052};
CC       Note=Manganese or magnesium. Binds 1 divalent metal ion per
CC       monomer in the absence of substrate. May bind a second metal ion
CC       after substrate binding. {ECO:0000255|HAMAP-Rule:MF_00052};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00052}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000255|HAMAP-
CC       Rule:MF_00052}.
DR   EMBL; AE005174; AAG54485.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33608.1; -; Genomic_DNA.
DR   PIR; A85503; A85503.
DR   PIR; A90652; A90652.
DR   RefSeq; NP_308212.1; NC_002695.1.
DR   RefSeq; WP_000569419.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; Q8X8X6; -.
DR   SMR; Q8X8X6; -.
DR   STRING; 155864.Z0195; -.
DR   EnsemblBacteria; AAG54485; AAG54485; Z0195.
DR   EnsemblBacteria; BAB33608; BAB33608; BAB33608.
DR   GeneID; 913902; -.
DR   KEGG; ece:Z0195; -.
DR   KEGG; ecs:ECs0185; -.
DR   PATRIC; fig|386585.9.peg.288; -.
DR   eggNOG; ENOG4108UH2; Bacteria.
DR   eggNOG; COG0164; LUCA.
DR   HOGENOM; HOG000100288; -.
DR   KO; K03470; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00052_B; RNase_HII_B; 1.
DR   InterPro; IPR022898; RNase_HII.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR012337; RNaseH-like_dom.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   PANTHER; PTHR10954:SF15; PTHR10954:SF15; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X8X6.
DR   SWISS-2DPAGE; Q8X8X6.
KW   Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Manganese;
KW   Metal-binding; Nuclease.
FT   CHAIN         1    198       Ribonuclease HII.
FT                                /FTId=PRO_0000111573.
FT   METAL        16     16       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00052}.
FT   METAL        17     17       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00052}.
FT   METAL       108    108       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00052}.
SQ   SEQUENCE   198 AA;  21466 MW;  253517F887750496 CRC64;
     MIEFVYPHTQ LVAGVDEVGR GPLVGAVVTA AVILDPARPI AGLNDSKKLS EKRRLALCEE
     IKEKALSWSL GRAEPHEIDE LNILHATMLA MQRAVAGLHI APEYVLIDGN RCPKLPMPAM
     AVVKGDSRVP EISAASILAK VTRDAEMAAL DIVFPQYGFA QHKGYPTAFH LEKLAEHGAT
     EHHRRSFGPV KRALGLAS
//

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