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Protein

Homothallic switching endonuclease

Gene

HO

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Initiation of mating type interconversion. This protein is a site-specific endonuclease that cleaves a site in the mat locus on chromosome III. The double-strand break is followed by a unidirectional gene conversion event that replaces the information at the mat locus by information copied from either of the two homologous loci (HMR and HML) that reside at the extremity of the chromosome III. Endonuclease expression takes place in late G1 just before cells enter S phase.

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • endonuclease activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • gene conversion at mating-type locus, DNA double-strand break formation Source: SGD
  • intein-mediated protein splicing Source: InterPro
  • mating type switching Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29607-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Homothallic switching endonuclease
Short name:
Ho endonuclease
Gene namesi
Name:HO
Ordered Locus Names:YDL227C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL227C.
SGDiS000002386. HO.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 586586Homothallic switching endonucleasePRO_0000084030Add
BLAST

Post-translational modificationi

Rapidly degraded via the ubiquitin-26S proteasome system through two ubiquitin-conjugating enzymes UBC2/RAD6 and UBC3/CDC34.

PTM databases

iPTMnetiP09932.

Interactioni

Protein-protein interaction databases

BioGridi31883. 24 interactions.
MINTiMINT-4480073.

Structurei

3D structure databases

ProteinModelPortaliP09932.
SMRiP09932. Positions 2-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini215 – 370156DOD-type homing endonucleasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DOD-type homing endonuclease domain.PROSITE-ProRule annotation

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000112934.
InParanoidiP09932.
OrthoDBiEOG74XSG8.

Family and domain databases

Gene3Di2.170.16.10. 1 hit.
3.10.28.10. 1 hit.
InterProiIPR028992. Hedgehog/Intein_dom.
IPR003587. Hint_dom_N.
IPR007868. Hom_end_hint.
IPR007869. Homing_endonuc_PI-Sce.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR004042. Intein_endonuc.
[Graphical view]
PfamiPF05204. Hom_end. 1 hit.
PF05203. Hom_end_hint. 1 hit.
[Graphical view]
PRINTSiPR00379. INTEIN.
SMARTiSM00306. HintN. 1 hit.
[Graphical view]
SUPFAMiSSF51294. SSF51294. 2 hits.
SSF55608. SSF55608. 2 hits.
PROSITEiPS50819. INTEIN_ENDONUCLEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09932-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSENTTILM ANGEIKDIAN VTANSYVMCA DGSAARVINV TQGYQKIYNI
60 70 80 90 100
QQKTKHRAFE GEPGRLDPRR RTVYQRLALQ CTAGHKLSVR VPTKPLLEKS
110 120 130 140 150
GRNATKYKVR WRNLQQCQTL DGRIIIIPKN HHKTFPMTVE GEFAAKRFIE
160 170 180 190 200
EMERSKGEYF NFDIEVRDLD YLDAQLRISS CIRFGPVLAG NGVLSKFLTG
210 220 230 240 250
RSDLVTPAVK SMAWMLGLWL GDSTTKEPEI SVDSLDPKLM ESLRENAKIW
260 270 280 290 300
GLYLTVCDDH VPLRAKHVRL HYGDGPDENR KTRNLRKNNP FWKAVTILKF
310 320 330 340 350
KRDLDGEKQI PEFMYGEHIE VREAFLAGLI DSDGYVVKKG EGPESYKIAI
360 370 380 390 400
QTVYSSIMDG IVHISRSLGM SATVTTRSAR EEIIEGRKVQ CQFTYDCNVA
410 420 430 440 450
GGTTSQNVLS YCRSGHKTRE VPPIIKREPV YFSFTDDFQG ESTVYGLTIE
460 470 480 490 500
GHKNFLLGNK IEVKSCRGCC VGEQLKISQK KNLKHCVACP RKGIKYFYKD
510 520 530 540 550
WSGKNRVCAR CYGRYKFSGH HCINCKYVPE AREVKKAKDK GEKLGITPEG
560 570 580
LPVKGPECIK CGGILQFDAV RGPHKSCGNN AGARIC
Length:586
Mass (Da):66,089
Last modified:November 1, 1997 - v2
Checksum:i95771394D177823A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891A → T in AAA34683 (PubMed:3025649).Curated
Sequence conflicti223 – 2231S → G in AAA34683 (PubMed:3025649).Curated
Sequence conflicti405 – 4051S → L in AAA34683 (PubMed:3025649).Curated
Sequence conflicti475 – 4751L → H in AAA34683 (PubMed:3025649).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14678 Genomic DNA. Translation: AAA34683.1.
X90957 Genomic DNA. Translation: CAA62447.1.
Z74275 Genomic DNA. Translation: CAA98806.1.
BK006938 Genomic DNA. Translation: DAA11638.1.
PIRiS59301.
RefSeqiNP_010054.1. NM_001180287.1.

Genome annotation databases

EnsemblFungiiYDL227C; YDL227C; YDL227C.
GeneIDi851371.
KEGGisce:YDL227C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14678 Genomic DNA. Translation: AAA34683.1.
X90957 Genomic DNA. Translation: CAA62447.1.
Z74275 Genomic DNA. Translation: CAA98806.1.
BK006938 Genomic DNA. Translation: DAA11638.1.
PIRiS59301.
RefSeqiNP_010054.1. NM_001180287.1.

3D structure databases

ProteinModelPortaliP09932.
SMRiP09932. Positions 2-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31883. 24 interactions.
MINTiMINT-4480073.

PTM databases

iPTMnetiP09932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL227C; YDL227C; YDL227C.
GeneIDi851371.
KEGGisce:YDL227C.

Organism-specific databases

EuPathDBiFungiDB:YDL227C.
SGDiS000002386. HO.

Phylogenomic databases

HOGENOMiHOG000112934.
InParanoidiP09932.
OrthoDBiEOG74XSG8.

Enzyme and pathway databases

BioCyciYEAST:G3O-29607-MONOMER.

Miscellaneous databases

PROiP09932.

Family and domain databases

Gene3Di2.170.16.10. 1 hit.
3.10.28.10. 1 hit.
InterProiIPR028992. Hedgehog/Intein_dom.
IPR003587. Hint_dom_N.
IPR007868. Hom_end_hint.
IPR007869. Homing_endonuc_PI-Sce.
IPR027434. Homing_endonucl.
IPR006142. INTEIN.
IPR004042. Intein_endonuc.
[Graphical view]
PfamiPF05204. Hom_end. 1 hit.
PF05203. Hom_end_hint. 1 hit.
[Graphical view]
PRINTSiPR00379. INTEIN.
SMARTiSM00306. HintN. 1 hit.
[Graphical view]
SUPFAMiSSF51294. SSF51294. 2 hits.
SSF55608. SSF55608. 2 hits.
PROSITEiPS50819. INTEIN_ENDONUCLEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Saccharomyces cerevisiae HO gene and analysis of its upstream regulatory region."
    Russell D.W., Jensen R., Zoller M.J., Burke J., Errede B., Smith M., Herskowitz I.
    Mol. Cell. Biol. 6:4281-4294(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of the heterothallic mutation in HO-endonuclease of S. cerevisiae using HO/ho chimeric genes."
    Meiron H., Nahon E., Raveh D.
    Curr. Genet. 28:367-373(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Putting the HO gene to work: practical uses for mating-type switching."
    Herskowitz I., Jensen R.
    Methods Enzymol. 194:132-146(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Functions of the DNA damage response pathway target Ho endonuclease of yeast for degradation via the ubiquitin-26S proteasome system."
    Kaplun L., Ivantsiv Y., Kornitzer D., Raveh D.
    Proc. Natl. Acad. Sci. U.S.A. 97:10077-10082(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHO_YEAST
AccessioniPrimary (citable) accession number: P09932
Secondary accession number(s): D6VRC8, Q12183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The metal-binding domain form zinc-fingers that are involved in binding of the DNA.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.