Q89MT4
Gene name |
pepA |
Protein name |
Probable cytosol aminopeptidase |
Names |
Leucine aminopeptidase, LAP, Leucyl aminopeptidase |
Species |
Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) |
KEGG Pathway |
bja:blr4108 |
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
1 structures for Q89MT4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q89MT4-F1 | Predicted | AlphaFoldDB |
No variants for Q89MT4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q89MT4 | |||||
No associated diseases with Q89MT4
6 regional properties for Q89MT4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FYVE zinc finger | 126 - 202 | IPR000306-1 |
| domain | FYVE zinc finger | 267 - 333 | IPR000306-2 |
| domain | Zinc finger C2H2-type | 41 - 62 | IPR013087 |
| domain | Zinc finger, FYVE-related | 145 - 201 | IPR017455-1 |
| domain | Zinc finger, FYVE-related | 275 - 332 | IPR017455-2 |
| domain | Rabenosyn, Rab binding domain | 483 - 523 | IPR021565 |
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 | |
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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminopeptidase activity | Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain. |
| 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. |
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 |
| MSDAIKVGFV | PLSAAARGIL | VVFCDDGLKL | GPATAKALGG | ATELVKRAAS | AAAFKGKSGA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ALDILAPEGV | KATRLIVIGA | GKATGLKAND | FLKFGGVAAG | KLSATAAAMT | IMAELPDGAM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TSEQAVAIAA | GLRLRAYKFD | RYKTKKKDGE | EGGSRADISL | AVGDVAAAKK | AFASAGHVVD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GVIIARDLVN | EPPNVLFPEE | FARRASLLRK | LGVKVEVLDV | KAMDKLGMGA | LLGVGQGSTR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PSRTVIMRWD | GGKKGEAPVA | FVGKGVCFDT | GGISIKPAGS | MEDMKGDMGG | AACVVGLMHA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LAARKAKANV | VGAIGLVENM | PDGNAQRPGD | IVTSMSGQTI | EIINTDAEGR | LVLADVLWYV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AKKTKPKFMV | DLATLTGAIV | VALGTEHAGM | FSNNDELADR | LLTAGIESGE | KVWRLPLGPE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YDKLIDSQFA | DMKNTGGRHG | GSITAAQFLQ | RFVDGTPWAH | LDIAGTAMGA | PKTDINQSWG |
| 490 | |||||
| SGYGVRLLDR | LVADHYERK |