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RNH2_MAGSA
ID   RNH2_MAGSA              Reviewed;         201 AA.
AC   Q50412; Q2W032;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Ribonuclease HII;
DE            Short=RNase HII;
DE            EC=3.1.26.4;
GN   Name=rnhB; OrderedLocusNames=amb3989;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7499342; DOI=10.1074/jbc.270.47.28392;
RA   Nakamura C., Burgess G.J., Sode K., Matsunaga T.;
RT   "An iron-regulated gene, magA encoding an iron transport protein of
RT   Magnetospirillum sp. strain AMB-1.";
RL   J. Biol. Chem. 270:28392-28396(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC       the absence of substrate. May bind a second metal ion after substrate
CC       binding. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}.
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DR   EMBL; D32253; BAA06983.1; -; Genomic_DNA.
DR   EMBL; AP007255; BAE52793.1; -; Genomic_DNA.
DR   RefSeq; WP_011386343.1; NC_007626.1.
DR   AlphaFoldDB; Q50412; -.
DR   SMR; Q50412; -.
DR   STRING; 342108.amb3989; -.
DR   EnsemblBacteria; BAE52793; BAE52793; amb3989.
DR   KEGG; mag:amb3989; -.
DR   HOGENOM; CLU_036532_3_2_5; -.
DR   OMA; YPTKLHL; -.
DR   OrthoDB; 1685277at2; -.
DR   Proteomes; UP000007058; 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.
DR   PROSITE; PS51975; RNASE_H_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..201
FT                   /note="Ribonuclease HII"
FT                   /id="PRO_0000111589"
FT   DOMAIN          12..201
FT                   /note="RNase H type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT   BINDING         18
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  21597 MW;  0D01B23CF85DD2A2 CRC64;
     MPDLALEFEI GGIVCGIDEV GRGPLAGPVV AAAVILDPAR LPKTLLERLD DSKKLSKRNR
     EELAELVPAT AILGFGEASV EEIDRINILQ ATFLAMRRAY DALGRECAHA LVDGNRPPGL
     PCPVRCVVGG DGISLSIAAA SVVAKVRRDA MMADLARAHP EFGWERNAGY GTAEHLDALK
     RLGPTPHHRR SFAPVAQYML F
 
 
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