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 C5G8H4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C5G8H4-F1 | Predicted | AlphaFoldDB |
No variants for C5G8H4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C5G8H4 | |||||
No associated diseases with C5G8H4
1 regional properties for C5G8H4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M28 | 165 - 340 | IPR007484 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| vacuolar membrane | The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| metalloexopeptidase activity | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of 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 |
| MATPRAQKFN | PIAFTPGPVT | LITTIVYLAL | LIPILVISLV | VPPAPETSPE | GVNLTEAWRD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LQHLTGGFHP | YNSRRNDDVH | QWLLRRIDSI | LRPTVEAGER | PSANNDIPDV | FVFDDNQSNL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TYSNGGVGKA | AIVGVYFEGT | NIIVYIRGTE | DDPENWWERS | NGKPKGKGGV | LVNAHYDSVS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TGYGATDNGM | GVVSLLQLLK | YFTTPGNKPR | KGLVLLFNNG | EEDYLNGAHV | FSQHPLSNFT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HTFLNLEGAG | AGGRAALFRT | TDTEVTRFYQ | NAKHPFGSVL | AADGFKMGLL | RSQTDYVVFN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GILGLRGLDL | AFIAPRSRYH | TDQDDARHTS | VDSLWHMLSA | AIGTTEGLVS | YTGTDFDGKS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QGLDKVNSGT | GTLGVWFDMF | GSAFAVFRLH | TLFALSVTLL | IVAPLVIFIT | AIVLSKTDRM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YLFSMSKSLG | GTDERVSLRG | LRGLFRTPII | LAVATVIPIG | LAYLLEKVNP | YIVHSSQFSV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WSMMISVWIF | LAWFLACAAD | FFRPSALHRA | YSYTWIFIAT | WVMLVINTVY | ANQKGIAAGY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FVFFYFSGSF | LATWVSYLEL | FALPRKGDFA | RQAIMHSGRP | PSSLRSRLLT | PSADELPSDT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GPHAEYPGDA | DETDPTESTS | LLRGQRTTFA | NYRTGGTDGV | VEGTDEGPSF | KHEQSWSWTL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PRWTWVLQLL | LLAPIVLILV | GQLALFLTTS | MSQVGSDGVS | TFIVYLACAV | FTTLLFAPLF |
| 730 | 740 | 750 | 760 | 770 | 780 |
| PFIHRFTYHI | PTFLFLVFVG | TLIYNLVAFP | FSPANRLKMF | FIQEVNLDDG | SNTVSLSGIQ |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PYLTDAINSI | PSAAGQNITC | DQSAFGKLEK | CSWAGLPPRV | LGQDHDRDTG | IVSSDWMSYN |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ITKTVGENKA | RIEISGRNTR | ACKLKFDKPV | ADFQVSGSAV | DHRMPHTSGQ | GVAEIRLWSR |
| 910 | 920 | 930 | 940 | 950 | 960 |
| TWDRTWVVDI | CWHDSHDKPE | DDDGDDEKQD | APRNGLSGKV | ICLWSDSNQS | DVIPALDELR |
| 970 | 980 | ||||
| LYTPNWVAIS | KSADGLVEAS | HGITIQ |