A2QAF9
Gene name |
An01g11360 |
Protein name |
Methionine aminopeptidase 2-1 |
Names |
MAP 2-1, MetAP 2-1, Peptidase M |
Species |
Aspergillus niger (strain CBS 51388 / FGSC A1513) |
KEGG Pathway |
|
EC number |
3.4.11.18: Aminopeptidases |
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 A2QAF9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2QAF9-F1 | Predicted | AlphaFoldDB |
No variants for A2QAF9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A2QAF9 | |||||
No associated diseases with A2QAF9
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.11.18 | Aminopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| metalloaminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein initiator methionine removal | The protein modification process in which the translation-initiating methionine or formylmethionine residue is removed from a protein. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGSKSPEGHR | QTPDASNSSE | LKPANPNPKP | ARNGSQSADL | DGGNLDDDND | DDGEANEEAG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VKTSADSTDK | KKKRKRSKKK | TKKGTLPLKQ | SSPPRVLVSS | LFPSGYPIGE | CVPYQDDNTS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RTTDEELRYN | SRLWDKDFLD | EYRQAAEIHR | QVRQYAQNEL | IKPGASLTTI | AEGIEDGVRA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LSGHQGLEPG | DGFKAGMGFP | TGLCLNNVAA | HWTPNPGAKD | VFLDKSDVLK | VDFGVHVNGR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IVDSAFTVAF | DHTYDNLLTA | VKEATNTGIM | HAGIDARVSE | IGAAIQEVME | SYEVEIAGKT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HPVKAIRNIT | GHDILRYNIH | GGKQVPFIKN | DRPDKMEEGE | VFAIETFGST | GRGVLHDDVG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LCLSNVFSKA | NAPQVGVYGY | GRNTDVSGAN | LRLSSAKNLL | KTIDANFGSL | VFCRRYLERL |
| 430 | 440 | 450 | 460 | 470 | |
| GVEKYHLGMR | HLIDNGIVEY | YEPLVDVKGS | YTAQFEHTIL | LHNGGKEVIS | RGDDY |