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DescriptionRecName: Full=Ribonuclease H2 subunit A; Short=RNase H2 subunit A; EC=3.1.26.4; AltName: Full=RNase H(201); AltName: Full=RNase H(35); AltName: Full=Ribonuclease HI large subunit; Short=RNase HI large subunit; AltName: Full=Ribonuclease HI subunit A;
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MyHits synonymsRNH2A_YEAST , P53942 , D6W1A7 , 60B1005F674ECC88
match map segment
ipfam:RNase_HII  
Legends: 1, Divalent metal cation; 2, Divalent metal cation. {ECO:0000250}; 3, MUTAGEN D->A: Abolishes enzyme activity. {ECO:0000269|PubMed:14734815}; 4, MUTAGEN D->A: Strongly impairs enzyme activity. {ECO:0000269|PubMed:14734815}.
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   02-NOV-2016, entry version 133.
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;
GN   ORFNames=N2369;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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>3.3.CO;2-E;
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
RT   of six 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.,
RA   Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA   Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA   Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA   Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA   Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA   Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA   Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA   Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA   Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA   Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA   Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA   Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA   Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT   and its 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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
RT   is 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.,
RA   Dephoure N., 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
RP   RNH203, 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
RT   proteins.";
RL   Nucleic Acids Res. 32:407-414(2004).
RN   [8]
RP   ERRATUM.
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
CC       DNA replication, possibly by mediating the removal of lagging-
CC       strand Okazaki fragment RNA primers during DNA replication.
CC       Mediates the excision of single ribonucleotides from DNA:RNA
CC       duplexes.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester.
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
CC       monomer in the absence of substrate. May bind a second metal ion
CC       after substrate 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
CC       and RNH203.
CC   -!- INTERACTION:
CC       Q05635:RNH202; NbExp=3; IntAct=EBI-15663, EBI-33940;
CC       Q12338:RNH203; NbExp=2; IntAct=EBI-15663, EBI-33805;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC       {ECO:0000305}.
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   ProteinModelPortal; P53942; -.
DR   SMR; P53942; -.
DR   BioGrid; 35751; 69.
DR   DIP; DIP-4565N; -.
DR   IntAct; P53942; 3.
DR   MINT; MINT-532801; -.
DR   MaxQB; P53942; -.
DR   PRIDE; P53942; -.
DR   EnsemblFungi; YNL072W; YNL072W; YNL072W.
DR   GeneID; 855652; -.
DR   KEGG; sce:YNL072W; -.
DR   EuPathDB; FungiDB:YNL072W; -.
DR   SGD; S000005016; RNH201.
DR   GeneTree; ENSGT00390000010768; -.
DR   HOGENOM; HOG000100290; -.
DR   InParanoid; P53942; -.
DR   KO; K10743; -.
DR   OMA; REECRFF; -.
DR   OrthoDB; EOG092C57KP; -.
DR   BioCyc; YEAST:G3O-33101-MONOMER; -.
DR   PRO; PR:P53942; -.
DR   Proteomes; UP000002311; Chromosome XIV.
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_dom.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00729; TIGR00729; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN         1    307       Ribonuclease H2 subunit A.
FT                                /FTId=PRO_0000111718.
FT   METAL        39     39       Divalent metal cation.
FT   METAL        40     40       Divalent metal cation. {ECO:0000250}.
FT   METAL       155    155       Divalent metal cation.
FT   MUTAGEN      39     39       D->A: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:14734815}.
FT   MUTAGEN     155    155       D->A: Abolishes enzyme activity.
FT                                {ECO:0000269|PubMed:14734815}.
FT   MUTAGEN     183    183       D->A: Strongly impairs enzyme activity.
FT                                {ECO:0000269|PubMed:14734815}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        36    251       ipfam:RNase_HII [T]
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
//