A1CAQ1
Gene name |
ampp (ACLA_012470) |
Protein name |
Probable Xaa-Pro aminopeptidase P |
Names |
AMPP, Aminopeptidase P, Aminoacylproline aminopeptidase, Prolidase |
Species |
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
KEGG Pathway |
act:ACLA_012470 |
EC number |
3.4.11.9: 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 A1CAQ1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1CAQ1-F1 | Predicted | AlphaFoldDB |
No variants for A1CAQ1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1CAQ1 | |||||
No associated diseases with A1CAQ1
1 regional properties for A1CAQ1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Amidohydrolase-related | 50 - 431 | IPR006680 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.11.9 | 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 |
|---|---|
| cellular anatomical entity | A part of a cellular organism that is either an immaterial entity or a material entity with granularity above the level of a protein complex but below that of an anatomical system. Or, a substance produced by a cellular organism with granularity above the level of a protein complex. |
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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
| MLFSRSPFRL | CRISAVGQTR | QLPFSRPRFL | SASVARYAID | METVNTSERL | ARLRQLMQEH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KVDVYIVPSE | DSHQSEYIAP | CDGRREFISG | FSGSAGTAIV | SMTKAALSTD | GRYFNQASKQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LDSNWLLLKR | GVENVPTWQE | WTTEQAEGGK | VVGVDPSLIT | APGARSLAET | LRKNGSSLVG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VQQNLVDLVW | GEDRPAPPRE | KVRVHPDKFA | GKSFQEKITD | LRKELENKKT | AGFVISMLDE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IAWLFNLRGS | DIPYNPVFFA | YAIITPTTAD | LYIDEEKLTP | EVTSHLGQDV | VIKPYDSIFA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DATALSEARK | QDAGEAAAKF | LLSNKASWAL | SLSLGGEEHV | EETRSPIADA | KAVKNEAELA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GMRACHIRDG | AALIEYFAWL | ENELVSKKTS | LDEVDAADKL | EQIRSKHDLF | AGLSFDTISS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TGPNGAVIHY | KPEKGSCAII | DPEAIYLCDS | GAQYLDGTTD | VTRTFHFGQP | TELEKKAFTL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VLKGMIAIDS | AVFPKGTSGF | ALDVLARQFL | WKEGLDYLHG | TGHGIGSYLN | VHEGPIGIGT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RVQYTEVPIA | PGNVISDEPG | FYEDGKFGIR | IEICLADVIM | AREVQTTHKF | GDKPWLGFEH |
| 610 | 620 | 630 | 640 | 650 | |
| VTMAPIGRNL | IEPSLLSESE | LKWVNDYHAE | IWEKTHHFFE | NDEFTRSWLQ | RETQPISK |