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RNH_HELPY
ID   RNH_HELPY               Reviewed;         143 AA.
AC   P56120;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Ribonuclease HI;
DE            Short=RNase HI;
DE            EC=3.1.26.4;
GN   Name=rnhA; OrderedLocusNames=HP_0661;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a
CC       regulatory site, or after substrate binding. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD07724.1; -; Genomic_DNA.
DR   PIR; E64602; E64602.
DR   RefSeq; NP_207455.1; NC_000915.1.
DR   RefSeq; WP_001155448.1; NC_018939.1.
DR   AlphaFoldDB; P56120; -.
DR   SMR; P56120; -.
DR   IntAct; P56120; 18.
DR   MINT; P56120; -.
DR   STRING; 85962.C694_03420; -.
DR   PaxDb; P56120; -.
DR   EnsemblBacteria; AAD07724; AAD07724; HP_0661.
DR   KEGG; hpy:HP_0661; -.
DR   PATRIC; fig|85962.47.peg.711; -.
DR   eggNOG; COG0328; Bacteria.
DR   OMA; MQEIEIF; -.
DR   PhylomeDB; P56120; -.
DR   Proteomes; UP000000429; 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; IBA:GO_Central.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
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; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..143
FT                   /note="Ribonuclease HI"
FT                   /id="PRO_0000195379"
FT   DOMAIN          1..136
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   143 AA;  16247 MW;  AACFDB2FAEC14753 CRC64;
     MQEIEIFCDG SSLGNPGPGG YAAILRYKDK EKTISGGEEF TTNNRMELRA LNEALKILKR
     PCRITLYSDS QYVCQAINVW LANWQKKNFS KVKNVDLWKE FLEVSKGHSI VAVWIKGHNG
     HAENERCDSL AKLEAQKRVK TTT
 
 
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