HO_YEAST
ID HO_YEAST Reviewed; 586 AA.
AC P09932; D6VRC8; Q12183;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Homothallic switching endonuclease;
DE Short=Ho endonuclease;
GN Name=HO; OrderedLocusNames=YDL227C;
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].
RX PubMed=3025649; DOI=10.1128/mcb.6.12.4281-4294.1986;
RA Russell D.W., Jensen R., Zoller M.J., Burke J., Errede B., Smith M.,
RA Herskowitz I.;
RT "Structure of the Saccharomyces cerevisiae HO gene and analysis of its
RT upstream regulatory region.";
RL Mol. Cell. Biol. 6:4281-4294(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8590483; DOI=10.1007/bf00326435;
RA Meiron H., Nahon E., Raveh D.;
RT "Identification of the heterothallic mutation in HO-endonuclease of S.
RT cerevisiae using HO/ho chimeric genes.";
RL Curr. Genet. 28:367-373(1995).
RN [3]
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 [4]
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 [5]
RP REVIEW.
RX PubMed=2005783; DOI=10.1016/0076-6879(91)94011-z;
RA Herskowitz I., Jensen R.;
RT "Putting the HO gene to work: practical uses for mating-type switching.";
RL Methods Enzymol. 194:132-146(1991).
RN [6]
RP DEGRADATION.
RX PubMed=10963670; DOI=10.1073/pnas.97.18.10077;
RA Kaplun L., Ivantsiv Y., Kornitzer D., Raveh D.;
RT "Functions of the DNA damage response pathway target Ho endonuclease of
RT yeast for degradation via the ubiquitin-26S proteasome system.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10077-10082(2000).
RN [7]
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).
CC -!- FUNCTION: Initiation of mating type interconversion. This protein is a
CC site-specific endonuclease that cleaves a site in the mat locus on
CC chromosome III. The double-strand break is followed by a unidirectional
CC gene conversion event that replaces the information at the mat locus by
CC information copied from either of the two homologous loci (HMR and HML)
CC that reside at the extremity of the chromosome III. Endonuclease
CC expression takes place in late G1 just before cells enter S phase.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Rapidly degraded via the ubiquitin-26S proteasome system through
CC two ubiquitin-conjugating enzymes UBC2/RAD6 and UBC3/CDC34.
CC -!- MISCELLANEOUS: The metal-binding domain form zinc-fingers that are
CC involved in binding of the DNA.
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DR EMBL; M14678; AAA34683.1; -; Genomic_DNA.
DR EMBL; X90957; CAA62447.1; -; Genomic_DNA.
DR EMBL; Z74275; CAA98806.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11638.1; -; Genomic_DNA.
DR PIR; S59301; S59301.
DR RefSeq; NP_010054.1; NM_001180287.1.
DR AlphaFoldDB; P09932; -.
DR SMR; P09932; -.
DR BioGRID; 31883; 29.
DR STRING; 4932.YDL227C; -.
DR iPTMnet; P09932; -.
DR PaxDb; P09932; -.
DR PRIDE; P09932; -.
DR EnsemblFungi; YDL227C_mRNA; YDL227C; YDL227C.
DR GeneID; 851371; -.
DR KEGG; sce:YDL227C; -.
DR SGD; S000002386; HO.
DR VEuPathDB; FungiDB:YDL227C; -.
DR eggNOG; ENOG502QUGM; Eukaryota.
DR HOGENOM; CLU_033909_0_0_1; -.
DR InParanoid; P09932; -.
DR OMA; YCRSGHK; -.
DR BioCyc; YEAST:G3O-29607-MON; -.
DR PRO; PR:P09932; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P09932; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IDA:SGD.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0007533; P:mating type switching; IMP:SGD.
DR Gene3D; 3.10.28.10; -; 2.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR007868; Hom_end_hint.
DR InterPro; IPR007869; Homing_endonuc_PI-Sce.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR004042; Intein_endonuc.
DR Pfam; PF05204; Hom_end; 1.
DR Pfam; PF05203; Hom_end_hint; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF55608; SSF55608; 2.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..586
FT /note="Homothallic switching endonuclease"
FT /id="PRO_0000084030"
FT DOMAIN 215..370
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT CONFLICT 189
FT /note="A -> T (in Ref. 1; AAA34683)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> G (in Ref. 1; AAA34683)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="S -> L (in Ref. 1; AAA34683)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="L -> H (in Ref. 1; AAA34683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 66089 MW; 95771394D177823A CRC64;
MLSENTTILM ANGEIKDIAN VTANSYVMCA DGSAARVINV TQGYQKIYNI QQKTKHRAFE
GEPGRLDPRR RTVYQRLALQ CTAGHKLSVR VPTKPLLEKS GRNATKYKVR WRNLQQCQTL
DGRIIIIPKN HHKTFPMTVE GEFAAKRFIE EMERSKGEYF NFDIEVRDLD YLDAQLRISS
CIRFGPVLAG NGVLSKFLTG RSDLVTPAVK SMAWMLGLWL GDSTTKEPEI SVDSLDPKLM
ESLRENAKIW GLYLTVCDDH VPLRAKHVRL HYGDGPDENR KTRNLRKNNP FWKAVTILKF
KRDLDGEKQI PEFMYGEHIE VREAFLAGLI DSDGYVVKKG EGPESYKIAI QTVYSSIMDG
IVHISRSLGM SATVTTRSAR EEIIEGRKVQ CQFTYDCNVA GGTTSQNVLS YCRSGHKTRE
VPPIIKREPV YFSFTDDFQG ESTVYGLTIE GHKNFLLGNK IEVKSCRGCC VGEQLKISQK
KNLKHCVACP RKGIKYFYKD WSGKNRVCAR CYGRYKFSGH HCINCKYVPE AREVKKAKDK
GEKLGITPEG LPVKGPECIK CGGILQFDAV RGPHKSCGNN AGARIC
