Q10712
Gene name |
LAPA1 (LAP, LAP2) |
Protein name |
Leucine aminopeptidase 1, chloroplastic |
Names |
DR57, Leucyl aminopeptidase 1, LAP 1, Proline aminopeptidase 1, Prolyl aminopeptidase 1 |
Species |
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
KEGG Pathway |
sly:544017 |
EC number |
3.4.11.1: 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
3 structures for Q10712
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4KSI | X-ray | 220 A | A | 54-571 | PDB |
| 5D8N | X-ray | 215 A | A/B/C | 54-571 | PDB |
| AF-Q10712-F1 | Predicted | AlphaFoldDB |
No variants for Q10712
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q10712 | |||||
No associated diseases with Q10712
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.11.1 | Aminopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| 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. |
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein hexamerization | The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits. |
| 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 |
| MATLRVSSLF | ASSSSSLHSN | PSVFTKYQSS | PKWAFSFPVT | PLCSKRSKRI | VHCIAGDTLG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTRPNESDAP | KISIGAKDTA | VVQWQGDLLA | IGATENDMAR | DENSKFKNPL | LQQLDSELNG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LLSAASSEED | FSGKSGQSVN | LRFPGGRITL | VGLGSSASSP | TSYHSLGQAA | AAAAKSSQAR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NIAVALASTD | GLSAESKINS | ASAIATGVVL | GSFEDNRFRS | ESKKSTLESL | DILGLGTGPE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IERKIKYAEH | VCAGVILGRE | LVNAPANIVT | PAVLAEEAKK | IASTYSDVIS | VNILDAEQCK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELKMGAYLAV | AAAATENPPY | FIHLCFKTPT | KERKTKLALV | GKGLTFDSGG | YNLKVGAGSR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IELMKNDMGG | AAAVLGAAKA | LGEIRPSRVE | VHFIVAACEN | MISAEGMRPG | DIVTASNGKT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IEVNNTDAEG | RLTLADALIY | ACNQGVEKII | DLATLTGAIM | VALGPSVAGA | FTPNDDLARE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VVEAAEASGE | KLWRMPMEES | YWESMKSGSG | DMINTGPGNG | GAITGALFLK | QFVDEKVQWL |
| 550 | 560 | 570 | |||
| HLDVAGPVWS | DEKKNATGYG | VSTLVEWVLR | N |