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Ribonuclease H2 subunit A (RNase H2 subunit A) (EC 3.1.26.4) (RNase H(201)) (RNase H(35)) (Ribonuclease HI large subunit) (RNase HI large subunit) (Ribonuclease HI subunit A)

 RNH2A_YEAST             Reviewed;         307 AA.
P53942; D6W1A7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
12-SEP-2018, entry version 148.
RecName: 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;
Name=RNH201; Synonyms=RNH35; OrderedLocusNames=YNL072W;
ORFNames=N2369;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8701611;
DOI=10.1002/(SICI)1097-0061(19960330)12:4<391::AID-YEA921>3.3.CO;2-E;
Poehlmann R., Philippsen P.;
"Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
reveals 12 new open reading frames (ORFs) and an ancient duplication
of six ORFs.";
Yeast 12:391-402(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
CHARACTERIZATION.
PubMed=9462832; DOI=10.1016/S0014-5793(97)01528-7;
Frank P., Braunshofer-Reiter C., Wintersberger U.;
"Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and
is evolutionarily related to prokaryotic RNase HII.";
FEBS Lett. 421:23-26(1998).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNH202 AND
RNH203, AND MUTAGENESIS OF ASP-39; ASP-155 AND ASP-183.
PubMed=14734815; DOI=10.1093/nar/gkh209;
Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J.;
"RNase H2 of Saccharomyces cerevisiae is a complex of three
proteins.";
Nucleic Acids Res. 32:407-414(2004).
[8]
ERRATUM.
Jeong H.-S., Backlund P.S., Chen H.-C., Karavanov A.A., Crouch R.J.;
Nucleic Acids Res. 32:1616-1616(2004).
-!- FUNCTION: Catalytic subunit of RNase HII, an endonuclease that
specifically degrades the RNA of RNA:DNA hybrids. Participates in
DNA replication, possibly by mediating the removal of lagging-
strand Okazaki fragment RNA primers during DNA replication.
Mediates the excision of single ribonucleotides from DNA:RNA
duplexes.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Manganese or magnesium. Binds 1 divalent metal ion per
monomer in the absence of substrate. May bind a second metal ion
after substrate binding. {ECO:0000250};
-!- SUBUNIT: The RNase 2 complex is a heterotrimer composed of the
catalytic subunit RNH201 and of the non-catalytic subunits RNH202
and RNH203.
-!- INTERACTION:
Q05635:RNH202; NbExp=3; IntAct=EBI-15663, EBI-33940;
Q12338:RNH203; NbExp=2; IntAct=EBI-15663, EBI-33805;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X86470; CAA60188.1; -; Genomic_DNA.
EMBL; Z71348; CAA95946.1; -; Genomic_DNA.
EMBL; BK006947; DAA10473.1; -; Genomic_DNA.
PIR; S53908; S53908.
RefSeq; NP_014327.1; NM_001182910.1.
ProteinModelPortal; P53942; -.
SMR; P53942; -.
BioGrid; 35751; 230.
ComplexPortal; CPX-1720; RNase H2 complex.
DIP; DIP-4565N; -.
IntAct; P53942; 3.
MINT; P53942; -.
STRING; 4932.YNL072W; -.
MaxQB; P53942; -.
PaxDb; P53942; -.
PRIDE; P53942; -.
EnsemblFungi; YNL072W; YNL072W; YNL072W.
GeneID; 855652; -.
KEGG; sce:YNL072W; -.
EuPathDB; FungiDB:YNL072W; -.
SGD; S000005016; RNH201.
GeneTree; ENSGT00390000010768; -.
HOGENOM; HOG000100290; -.
InParanoid; P53942; -.
KO; K10743; -.
OMA; REECRFF; -.
OrthoDB; EOG092C57KP; -.
BioCyc; YEAST:G3O-33101-MONOMER; -.
PRO; PR:P53942; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0032299; C:ribonuclease H2 complex; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:SGD.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:SGD.
GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
Gene3D; 1.10.10.460; -; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR004649; RNase_H2_suA.
InterPro; IPR001352; RNase_HII/HIII.
InterPro; IPR024567; RNase_HII/HIII_dom.
InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
PANTHER; PTHR10954; PTHR10954; 1.
Pfam; PF01351; RNase_HII; 1.
SUPFAM; SSF53098; SSF53098; 1.
TIGRFAMs; TIGR00729; TIGR00729; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
Nuclease; Nucleus; Reference proteome.
CHAIN 1 307 Ribonuclease H2 subunit A.
/FTId=PRO_0000111718.
METAL 39 39 Divalent metal cation.
METAL 40 40 Divalent metal cation. {ECO:0000250}.
METAL 155 155 Divalent metal cation.
MUTAGEN 39 39 D->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:14734815}.
MUTAGEN 155 155 D->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:14734815}.
MUTAGEN 183 183 D->A: Strongly impairs enzyme activity.
{ECO:0000269|PubMed:14734815}.
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


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