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 Q10835
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q10835-F1 | Predicted | AlphaFoldDB |
No variants for Q10835
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q10835 | |||||
No associated diseases with Q10835
11 regional properties for Q10835
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Hemopexin-like domain | 279 - 468 | IPR000585 |
| domain | Peptidase M10, metallopeptidase | 110 - 265 | IPR001818 |
| domain | Peptidoglycan binding-like | 32 - 89 | IPR002477 |
| domain | Peptidase, metallopeptidase | 107 - 266 | IPR006026 |
| conserved_site | Hemopexin, conserved site | 321 - 336 | IPR018486 |
| repeat | Hemopexin-like repeats | 279 - 330 | IPR018487-1 |
| repeat | Hemopexin-like repeats | 329 - 375 | IPR018487-2 |
| repeat | Hemopexin-like repeats | 377 - 427 | IPR018487-3 |
| repeat | Hemopexin-like repeats | 426 - 469 | IPR018487-4 |
| binding_site | Peptidase M10A, cysteine switch, zinc binding site | 92 - 99 | IPR021158 |
| domain | Peptidase M10A, catalytic domain | 110 - 265 | IPR033739 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular matrix | A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| collagen binding | Binding to collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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. |
| zinc ion binding | Binding to a zinc ion (Zn). |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| bone morphogenesis | The process in which bones are generated and organized. |
| collagen catabolic process | The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. |
| extracellular matrix disassembly | A process that results in the breakdown of the extracellular matrix. |
| 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 |
| SSLSVLVLSL | SFAYCLSAPV | PQDEDSELTP | GDLQLAEHYL | NRLYSSSSNP | VGMLRMKNVN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SIETKLKEMQ | SFFGLEVTGK | LNEDTLDIMK | QPRCGVPDVG | QYNFFPRKLK | WPRNNLTYRI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VNYTPDLSTS | EVDRAIKKAL | KVWSDVTPLN | FTRLRTGTAD | IMVSFGKKEH | GDYYPFDGPD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GLLAHAFPPG | EKLGGDTHFD | DDEMFSTDNK | GYNLFVVAAH | EFGHALGLDH | SRDPGSLMFP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VYTYTETSRF | VLPDDDVQGI | QVLYGPGNRD | PHPKHPKTPE | KCDPDLSIDA | ITELRGEKMI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FKDRFFWRVH | PQMTDAELVL | IKSFWPELPN | KLDAAYEHPA | KDLSYLFRGK | KFWALNGYDI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VEDYPKKLHE | LGFPKTLKAI | DAAVYNKDTG | KTFFFTEDSY | WSFDEEARTL | DKGFPRLISE |
| 430 | 440 | 450 | 460 | ||
| DFPGIGEKVD | AAYQRNGYLY | FFNGALQFEY | SIWSQRITRI | LKTNFVLMC |