P09932
Gene name |
HO (YDL227C) |
Protein name |
Homothallic switching endonuclease |
Names |
Ho endonuclease |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YDL227C |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P09932
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P09932-F1 | Predicted | AlphaFoldDB |
15 variants for P09932
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s04-48011 | 8 | I>V | No | SGRP | |
| s04-47824 | 70 | R>H | No | SGRP | |
| s04-47468 | 189 | A>T | No | SGRP | |
| s04-47366 | 223 | S>G | No | SGRP | |
| s04-47365 | 223 | S>N | No | SGRP | |
| s04-47204 | 277 | D>H | No | SGRP | |
| s04-46858 | 392 | Q>R | No | SGRP | |
| s04-46849 | 395 | Y>C | No | SGRP | |
| s04-46845 | 396 | D>E | No | SGRP | |
| s04-46819 | 405 | S>L | No | SGRP | |
| s04-46628 | 469 | C>S | No | SGRP | |
| s04-46609 | 475 | L>H | No | SGRP | |
| s04-46549 | 495 | K>R | No | SGRP | |
| s04-46532 | 501 | W>R | No | SGRP | |
| s04-46482 | 517 | F>L | No | SGRP |
No associated diseases with P09932
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| endonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks. |
| metal ion binding | Binding to a metal ion. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| gene conversion at mating-type locus | The conversion of the mating-type locus from one allele to another resulting from the recombinational repair of a site-specific double-strand break at the mating-type locus with information from a silent donor sequence. There is no reciprocal exchange of information because the mating-type locus copies information from the donor sequence and the donor sequence remains unchanged. |
| intein-mediated protein splicing | The removal of an internal amino acid sequence (an intein) from a protein during protein maturation; the excision of inteins is precise and the N- and C-terminal exteins are joined by a normal peptide bond. Protein splicing involves 4 nucleophilic displacements by the 3 conserved splice junction residues. |
| mating type switching | The conversion of a single-cell organism from one mating type to another by the precise replacement of a DNA sequence at the expressed mating type locus with a copy of a sequence from a donor locus. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLSENTTILM | ANGEIKDIAN | VTANSYVMCA | DGSAARVINV | TQGYQKIYNI | QQKTKHRAFE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GEPGRLDPRR | RTVYQRLALQ | CTAGHKLSVR | VPTKPLLEKS | GRNATKYKVR | WRNLQQCQTL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DGRIIIIPKN | HHKTFPMTVE | GEFAAKRFIE | EMERSKGEYF | NFDIEVRDLD | YLDAQLRISS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CIRFGPVLAG | NGVLSKFLTG | RSDLVTPAVK | SMAWMLGLWL | GDSTTKEPEI | SVDSLDPKLM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ESLRENAKIW | GLYLTVCDDH | VPLRAKHVRL | HYGDGPDENR | KTRNLRKNNP | FWKAVTILKF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KRDLDGEKQI | PEFMYGEHIE | VREAFLAGLI | DSDGYVVKKG | EGPESYKIAI | QTVYSSIMDG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IVHISRSLGM | SATVTTRSAR | EEIIEGRKVQ | CQFTYDCNVA | GGTTSQNVLS | YCRSGHKTRE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VPPIIKREPV | YFSFTDDFQG | ESTVYGLTIE | GHKNFLLGNK | IEVKSCRGCC | VGEQLKISQK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KNLKHCVACP | RKGIKYFYKD | WSGKNRVCAR | CYGRYKFSGH | HCINCKYVPE | AREVKKAKDK |
| 550 | 560 | 570 | 580 | ||
| GEKLGITPEG | LPVKGPECIK | CGGILQFDAV | RGPHKSCGNN | AGARIC |