P0CM08
Gene name |
YAF9 (CNI04050) |
Protein name |
Protein AF-9 homolog |
Names |
|
Species |
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans) |
KEGG Pathway |
cne:CNI04050 |
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 P0CM08
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0CM08-F1 | Predicted | AlphaFoldDB |
No variants for P0CM08
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0CM08 | |||||
No associated diseases with P0CM08
No regional properties for P0CM08
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P0CM08 | |||
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| NuA4 histone acetyltransferase complex | A complex having histone acetylase activity on chromatin, as well as ATPase, DNA helicase and structural DNA binding activities. The complex is thought to be involved in double-strand DNA break repair. Subunits of the human complex include HTATIP/TIP60, TRRAP, RUVBL1, BUVBL2, beta-actin and BAF53/ACTL6A. In yeast, the complex has 13 subunits, including the catalytic subunit Esa1 (homologous to human Tip60). |
| Swr1 complex | A multisubunit protein complex that is involved in chromatin remodeling. It is required for the incorporation of the histone variant H2AZ into chromatin. In S. cerevisiae, the complex contains Swr1p, a Swi2/Snf2-related ATPase, and 12 additional subunits. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| histone binding | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| chromatin remodeling | A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication. |
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| histone acetylation | The modification of a histone by the addition of an acetyl group. |
| regulation of transcription by RNA polymerase II | Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSERVRGIQ | VHRPIIFGSH | ARLLTEAEKQ | LAPAGHTHKW | TVFLNSAASP | PLKQGEPPDY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EDIDYLPGGA | DDLSYFIRKV | TFKLHETYAT | PNRVIDKPPY | RVSETGWGEF | TVQIRIQLIP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ESSEKPLGLQ | HNIKLHHWGA | PVEPLPVVSG | APTPTPVPTE | SNTEVKLEPD | TPAPLEESVT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PAPTIQRPAS | EPATNEPGSN | QGTPAPPGGD | STEQIKVDVA | TPALEVIEPS | ATPAPLSLAA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RLPIHAWQYD | EIVFSDPPRQ | FLDILNAHPP | TPLPAKSRRP | RDQREDYEAR | KKGKSAARGA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVTASARASR | AGTVDTAAAG | TPAPAQIGIP | GEPGSADVPL | EFTQEMLKGE | HNAMLDARVK |
| 370 | 380 | 390 | |||
| IVEQMDRWRE | RLIALEKELA | KAKEDVKATA | AM |