RNH1_YEAST
ID RNH1_YEAST Reviewed; 348 AA.
AC Q04740; D6W060;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ribonuclease H;
DE Short=RNase H;
DE EC=3.1.26.4;
GN Name=RNH1; OrderedLocusNames=YMR234W; ORFNames=YM9959.16;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 157-348.
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=1650910; DOI=10.1007/bf00273935;
RA Itaya M., McKelvin D., Chatterjie S.K., Crouch R.J.;
RT "Selective cloning of genes encoding RNase H from Salmonella typhimurium,
RT Saccharomyces cerevisiae and Escherichia coli rnh mutant.";
RL Mol. Gen. Genet. 227:438-445(1991).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP STRUCTURE BY NMR OF 6-52.
RX PubMed=10448044; DOI=10.1006/jmbi.1999.2971;
RA Evans S.P., Bycroft M.;
RT "NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase
RT HI reveals a fold with a strong resemblance to the N-terminal domain of
RT ribosomal protein L9.";
RL J. Mol. Biol. 291:661-669(1999).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
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 -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR EMBL; Z49939; CAA90205.1; -; Genomic_DNA.
DR EMBL; X57160; CAA40448.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10134.1; -; Genomic_DNA.
DR PIR; S57601; S57601.
DR RefSeq; NP_013961.1; NM_001182741.1.
DR PDB; 1QHK; NMR; -; A=5-51.
DR PDBsum; 1QHK; -.
DR AlphaFoldDB; Q04740; -.
DR BMRB; Q04740; -.
DR SMR; Q04740; -.
DR BioGRID; 35412; 120.
DR DIP; DIP-6787N; -.
DR IntAct; Q04740; 5.
DR STRING; 4932.YMR234W; -.
DR MaxQB; Q04740; -.
DR PaxDb; Q04740; -.
DR PRIDE; Q04740; -.
DR EnsemblFungi; YMR234W_mRNA; YMR234W; YMR234W.
DR GeneID; 855274; -.
DR KEGG; sce:YMR234W; -.
DR SGD; S000004847; RNH1.
DR VEuPathDB; FungiDB:YMR234W; -.
DR eggNOG; KOG3752; Eukaryota.
DR GeneTree; ENSGT00390000003466; -.
DR HOGENOM; CLU_030894_0_0_1; -.
DR InParanoid; Q04740; -.
DR OMA; ELWYGLY; -.
DR BioCyc; YEAST:G3O-32915-MON; -.
DR BRENDA; 3.1.26.4; 984.
DR EvolutionaryTrace; Q04740; -.
DR PRO; PR:Q04740; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04740; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:SGD.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IDA:SGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.970.10; -; 2.
DR InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR InterPro; IPR017067; RNase_H1_euk.
DR InterPro; IPR011320; RNase_H1_N.
DR InterPro; IPR037056; RNase_H1_N_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF01693; Cauli_VI; 2.
DR Pfam; PF00075; RNase_H; 1.
DR PIRSF; PIRSF036852; Ribonuclease_H1_euk; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55658; SSF55658; 2.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..348
FT /note="Ribonuclease H"
FT /id="PRO_0000195438"
FT DOMAIN 184..346
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1QHK"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1QHK"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1QHK"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:1QHK"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1QHK"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1QHK"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:1QHK"
SQ SEQUENCE 348 AA; 39431 MW; 02403B2329126B90 CRC64;
MARQGNFYAV RKGRETGIYN TWNECKNQVD GYGGAIYKKF NSYEQAKSFL GQPNTTSNYG
SSTHAGGQVS KPHTTQKRVH RRNRPLHYSS LTSSSACSSL SSANTNTFYS VKSNVPNIES
KIFNNWKDCQ AYVKHKRGIT FKKFEDQLAA ENFISGMSAH DYKLMNISKE SFESKYKLSS
NTMYNKSMNV YCDGSSFGNG TSSSRAGYGA YFEGAPEENI SEPLLSGAQT NNRAEIEAVS
EALKKIWEKL TNEKEKVNYQ IKTDSEYVTK LLNDRYMTYD NKKLEGLPNS DLIVPLVQRF
VKVKKYYELN KECFKNNGKF QIEWVKGHDG DPGNEMADFL AKKGASRR
