P0CM89
Gene name |
YSH1 (CNBL2750) |
Protein name |
Endoribonuclease YSH1 |
Names |
mRNA 3'-end-processing protein YSH1 |
Species |
Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) (Filobasidiella neoformans) |
KEGG Pathway |
cnb:CNBL2750 |
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 P0CM89
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0CM89-F1 | Predicted | AlphaFoldDB |
No variants for P0CM89
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0CM89 | |||||
No associated diseases with P0CM89
4 regional properties for P0CM89
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Metallo-beta-lactamase | 40 - 252 | IPR001279 |
| domain | Zn-dependent metallo-hydrolase, RNA specificity domain | 407 - 472 | IPR011108 |
| domain | Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term | 501 - 750 | IPR021718 |
| domain | Beta-Casp domain | 269 - 392 | IPR022712 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| mRNA cleavage and polyadenylation specificity factor complex | A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| endoribonuclease activity | Catalysis of the hydrolysis of ester linkages within ribonucleic acid by creating internal breaks. |
| metal ion binding | Binding to a metal ion. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| mRNA polyadenylation | The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript. |
| pre-mRNA cleavage required for polyadenylation | The targeted, endonucleolytic cleavage of a pre-mRNA, required for polyadenylation of the 3' end. This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation. |
| sno(s)RNA 3'-end processing | Any process involved in forming the mature 3' end of a snoRNA family molecule, also referred to as an sRNA in Archaea. |
| snoRNA splicing | The process of removing sections of a primary snoRNA transcript to remove sequences not present in the mature form of the snoRNA and joining the remaining sections to form the mature form of the snoRNA. |
| termination of RNA polymerase II transcription | A transcription termination process that completes the production of a primary RNA polymerase II transcript. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIPRRHHFKP | APQPTVQVLQ | PPDEDAPSLT | ITMLGAGQEV | GRSCCVIEHR | GKKIVCDAGL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HPAQPGIGAL | PFIDELDWST | VDAMLITHFH | VDHAAALPYI | MEKTNFKDGN | GKVYMTHATK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AIYGLTMMDT | VRLNDQNPDT | SGRLYDEADV | QSSWQSTIAV | DYHQDIVIAG | GLRFTPYHAG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HVLGASMFLI | EIAGLKILYT | GDYSREEDRH | LVMAEIPPVK | PDVMICESTF | GVHTLPDRKE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KEEQFTTLVA | NIVRRGGRCL | MPIPSFGNGQ | ELALLLDEYW | NDHPELQNIP | VYFASSLFQR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GMRVYKTYVH | TMNANIRSRF | ARRDNPFDFR | FVKWLKDPQK | LRENKGPCVI | MSSPQFMSFG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSRDLLEEWA | PDSKNGVIVT | GYSIEGTMAR | TLLSEPDHIE | SLKGGNVPRR | LTVKEISFGA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HVDYAQNSKF | IQEIGAQHVV | LVHGEASQMG | RLRAALRDTY | AAKGQEINIH | TPKNCEPLTL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TFRQERMVKA | IGSLAATRPE | HGTSVKGLLV | SKDFSYTLLS | PADLHDFTGL | STSTIIQKQG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VAISVDWAVV | RWYLEGMYGE | VEEGVEEEGK | AAFIIMNGVQ | VVQISPTAVE | LRWKSSSSND |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MIADSALALL | LGIDGSPATA | KLTASPNKHA | CNHSNSHSHT | DLYPHTYPGD | KSAKDVASNP |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EFERLRMFLE | AHFGHVEGPN | LRPPLPPGAD | GDGNDDKDKD | GDDWLTMDVK | LDNQTARIDL |
| 730 | 740 | 750 | 760 | 770 | |
| ISMRVESESA | ELQKRVETVL | EMALTTVKSL | SQTFLGGGLD | VDMVKVEPNE | SDS |