RNH2A_YEAST
ID RNH2A_YEAST Reviewed; 307 AA.
AC P53942; D6W1A7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ribonuclease H2 subunit A;
DE Short=RNase H2 subunit A;
DE EC=3.1.26.4;
DE AltName: Full=RNase H(201);
DE AltName: Full=RNase H(35);
DE AltName: Full=Ribonuclease HI large subunit;
DE Short=RNase HI large subunit;
DE AltName: Full=Ribonuclease HI subunit A;
GN Name=RNH201; Synonyms=RNH35; OrderedLocusNames=YNL072W; ORFNames=N2369;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701611;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA Poehlmann R., Philippsen P.;
RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT ORFs.";
RL Yeast 12:391-402(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=9462832; DOI=10.1016/s0014-5793(97)01528-7;
RA Frank P., Braunshofer-Reiter C., Wintersberger U.;
RT "Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is
RT evolutionarily related to prokaryotic RNase HII.";
RL FEBS Lett. 421:23-26(1998).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNH202 AND RNH203,
RP AND MUTAGENESIS OF ASP-39; ASP-155 AND ASP-183.
RX PubMed=14734815; DOI=10.1093/nar/gkh209;
RA Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J.;
RT "RNase H2 of Saccharomyces cerevisiae is a complex of three proteins.";
RL Nucleic Acids Res. 32:407-414(2004).
RN [8]
RP ERRATUM OF PUBMED:14734815.
RA Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J.;
RL Nucleic Acids Res. 32:1616-1616(2004).
CC -!- FUNCTION: Catalytic subunit of RNase HII, an endonuclease that
CC specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA
CC replication, possibly by mediating the removal of lagging-strand
CC Okazaki fragment RNA primers during DNA replication. Mediates the
CC excision of single ribonucleotides from DNA:RNA duplexes.
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 -!- SUBUNIT: The RNase 2 complex is a heterotrimer composed of the
CC catalytic subunit RNH201 and of the non-catalytic subunits RNH202 and
CC RNH203.
CC -!- INTERACTION:
CC P53942; Q05635: RNH202; NbExp=3; IntAct=EBI-15663, EBI-33940;
CC P53942; Q12338: RNH203; NbExp=2; IntAct=EBI-15663, EBI-33805;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC {ECO:0000305}.
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DR EMBL; X86470; CAA60188.1; -; Genomic_DNA.
DR EMBL; Z71348; CAA95946.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10473.1; -; Genomic_DNA.
DR PIR; S53908; S53908.
DR RefSeq; NP_014327.1; NM_001182910.1.
DR AlphaFoldDB; P53942; -.
DR SMR; P53942; -.
DR BioGRID; 35751; 237.
DR ComplexPortal; CPX-1720; RNase H2 complex.
DR DIP; DIP-4565N; -.
DR IntAct; P53942; 3.
DR MINT; P53942; -.
DR STRING; 4932.YNL072W; -.
DR MaxQB; P53942; -.
DR PaxDb; P53942; -.
DR PRIDE; P53942; -.
DR EnsemblFungi; YNL072W_mRNA; YNL072W; YNL072W.
DR GeneID; 855652; -.
DR KEGG; sce:YNL072W; -.
DR SGD; S000005016; RNH201.
DR VEuPathDB; FungiDB:YNL072W; -.
DR eggNOG; KOG2299; Eukaryota.
DR GeneTree; ENSGT00390000010768; -.
DR HOGENOM; CLU_036532_0_1_1; -.
DR InParanoid; P53942; -.
DR OMA; REECRFF; -.
DR BioCyc; YEAST:G3O-33101-MON; -.
DR BRENDA; 3.1.26.4; 984.
DR PRO; PR:P53942; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53942; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:SGD.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR Gene3D; 1.10.10.460; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR004649; RNase_H2_suA.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10954; PTHR10954; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00729; TIGR00729; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..307
FT /note="Ribonuclease H2 subunit A"
FT /id="PRO_0000111718"
FT DOMAIN 33..260
FT /note="RNase H type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01319"
FT BINDING 39
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT MUTAGEN 39
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:14734815"
FT MUTAGEN 155
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:14734815"
FT MUTAGEN 183
FT /note="D->A: Strongly impairs enzyme activity."
FT /evidence="ECO:0000269|PubMed:14734815"
SQ SEQUENCE 307 AA; 34875 MW; 60B1005F674ECC88 CRC64;
MVPPTVEASL ESPYTKSYFS PVPSALLEQN DSPIIMGIDE AGRGPVLGPM VYAVAYSTQK
YQDETIIPNY EFDDSKKLTD PIRRMLFSKI YQDNEELTQI GYATTCITPL DISRGMSKFP
PTRNYNLNEQ AHDVTMALID GVIKQNVKLS HVYVDTVGPP ASYQKKLEQR FPGVKFTVAK
KADSLYCMVS VASVVAKVTR DILVESLKRD PDEILGSGYP SDPKTVAWLK RNQTSLMGWP
ANMVRFSWQT CQTLLDDASK NSIPIKWEEQ YMDSRKNAAQ KTKQLQLQMV AKPVRRKRLR
TLDNWYR
