RNH2B_YEAST
ID RNH2B_YEAST Reviewed; 350 AA.
AC Q05635; D6VSQ9; Q6Q5R1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ribonuclease H2 subunit B;
DE Short=RNase H2 subunit B;
DE Short=Rnh2B;
DE AltName: Full=RNase H(202);
DE AltName: Full=Ribonuclease HI subunit B;
GN Name=RNH202; OrderedLocusNames=YDR279W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH RNH201 AND RNH203.
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 [7]
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).
RN [8]
RP FUNCTION.
RX PubMed=16193328; DOI=10.1007/s00294-005-0014-5;
RA Ii M., Brill S.J.;
RT "Roles of SGS1, MUS81, and RAD51 in the repair of lagging-strand
RT replication defects in Saccharomyces cerevisiae.";
RL Curr. Genet. 48:213-225(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Non catalytic subunit of RNase H2, 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 {ECO:0000269|PubMed:16193328}.
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 Q05635; P53942: RNH201; NbExp=3; IntAct=EBI-33940, EBI-15663;
CC Q05635; Q12338: RNH203; NbExp=2; IntAct=EBI-33940, EBI-33805;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RNase H2 subunit B family. Highly divergent.
CC {ECO:0000305}.
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DR EMBL; U51030; AAB64447.1; -; Genomic_DNA.
DR EMBL; AY557789; AAS56115.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12119.1; -; Genomic_DNA.
DR PIR; S70135; S70135.
DR RefSeq; NP_010565.3; NM_001180587.3.
DR AlphaFoldDB; Q05635; -.
DR BioGRID; 32332; 137.
DR ComplexPortal; CPX-1720; RNase H2 complex.
DR DIP; DIP-1838N; -.
DR IntAct; Q05635; 6.
DR MINT; Q05635; -.
DR STRING; 4932.YDR279W; -.
DR iPTMnet; Q05635; -.
DR MaxQB; Q05635; -.
DR PaxDb; Q05635; -.
DR PRIDE; Q05635; -.
DR EnsemblFungi; YDR279W_mRNA; YDR279W; YDR279W.
DR GeneID; 851873; -.
DR KEGG; sce:YDR279W; -.
DR SGD; S000002687; RNH202.
DR VEuPathDB; FungiDB:YDR279W; -.
DR eggNOG; ENOG502RB2X; Eukaryota.
DR HOGENOM; CLU_802143_0_0_1; -.
DR InParanoid; Q05635; -.
DR OMA; DNHDKNW; -.
DR BioCyc; YEAST:G3O-29844-MON; -.
DR PRO; PR:Q05635; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05635; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:SGD.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IC:SGD.
DR GO; GO:0006298; P:mismatch repair; IC:ComplexPortal.
DR GO; GO:0006401; P:RNA catabolic process; IDA:SGD.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR CDD; cd09270; RNase_H2-B; 1.
DR InterPro; IPR040456; RNase_H2_suB.
DR InterPro; IPR019024; RNase_H2_suB_wHTH.
DR InterPro; IPR041195; Rnh202_N.
DR Pfam; PF09468; RNase_H2-Ydr279; 1.
DR Pfam; PF17745; Ydr279_N; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Nucleus; Reference proteome.
FT CHAIN 1..350
FT /note="Ribonuclease H2 subunit B"
FT /id="PRO_0000248383"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 83
FT /note="N -> S (in Ref. 3; AAS56115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 39484 MW; 68578B3018579583 CRC64;
MTVSNIGGEE RLIILPDDYE TSKTINTFTL PPPSNITSKP RIELFENING KLYEIRSFQF
GKGPSYSHEE DLANDKYHYT KENHPIKSTF IVNTSDPTDG YVFNSSKIHF CSLYDIAFSL
IGFYYRNSVS ADEQDYSNSS DTGENQKSNS KTNEKFLTVR DYHDFLTDNH DKNWENISLS
RLKSGLAKVS ETIEEAGDVY YKITSAMITQ FLLGKVSKIV ENFPPSIPTL KNAPTEIKQC
YKVVMATNLL VSLIPRAAYH NLLTFSPTMD SGCLNPDIKA SFIELENYET TNELQNAERE
LLMKSAMNVG LNSNGRVSLP VKKVTKKIVQ NKKPKVAIGK GAIDGFFKRK
