(data stored in ACNUC10821 zone)

SWISSPROT: C8U1Q1_ECO10

ID   C8U1Q1_ECO10            Unreviewed;       198 AA.
AC   C8U1Q1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Ribonuclease HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE            Short=RNase HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE            EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00052};
GN   Name=rnhB {ECO:0000256|HAMAP-Rule:MF_00052,
GN   ECO:0000313|EMBL:BAI29059.1};
GN   OrderedLocusNames=ECO103_0181 {ECO:0000313|EMBL:BAI29059.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29059.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29059.1, 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_00052,
CC       ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS01082238}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         EC=3.1.26.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00052,
CC         ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS01118389};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS01082248};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00052};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-Rule:MF_00052};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00052,
CC       ECO:0000256|SAAS:SAAS01082247}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000256|HAMAP-
CC       Rule:MF_00052, ECO:0000256|RuleBase:RU003515,
CC       ECO:0000256|SAAS:SAAS01082243}.
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DR   EMBL; AP010958; BAI29059.1; -; Genomic_DNA.
DR   RefSeq; WP_000569430.1; NC_013353.1.
DR   SMR; C8U1Q1; -.
DR   EnsemblBacteria; BAI29059; BAI29059; ECO103_0181.
DR   KEGG; eoh:ECO103_0181; -.
DR   HOGENOM; HOG000100288; -.
DR   KO; K03470; -.
DR   OMA; NILHASM; -.
DR   BioCyc; ECOL585395:ECO103_RS00925-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA 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; 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_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   PANTHER; PTHR10954:SF18; PTHR10954:SF18; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1Q1.
DR   SWISS-2DPAGE; C8U1Q1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|SAAS:SAAS01082168};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS01082244};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS01082211};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|SAAS:SAAS01082195};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|SAAS:SAAS01082227};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS01082185}.
FT   DOMAIN       13    188       RNase_HII. {ECO:0000259|Pfam:PF01351}.
FT   METAL        16     16       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
FT   METAL        17     17       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
FT   METAL       108    108       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
SQ   SEQUENCE   198 AA;  21526 MW;  25350722EB5D7864 CRC64;
     MIEFVYPHTQ LVAGVDEVGR GPLVGAVVTA AVILDPARPI AGLNDSKKLS EKRRLALYEE
     IKEKALSWSL GRAEPHEIDE LNILHATMLA MQRAVAGLHI APEYVLIDGN RCPKLPMPAM
     AVVKGDSRVP EISAASILAK VTRDAEMAAL DIVFPQYGFA QHKGYPTAFH LEKLAEHGAT
     EHHRRSFGPV KRALGLAS
//

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