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 B6K327
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B6K327-F1 | Predicted | AlphaFoldDB |
No variants for B6K327
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B6K327 | |||||
No associated diseases with B6K327
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 |
| MQFGKSLLKH | VYTRTFKSSL | TCSIFAFTLL | MIFFVLDWKR | MNVYPRLDEI | PGLNVLRAWD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLQEITKSPH | PYNSHASDVV | RNYILEELYK | LKKQDEGNVE | VIDDLSSTTT | FIMPDTNIRS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YFEGSNILVR | FRGDNERLRP | ILLSSHFDSV | STGFGATDNG | MGVASALELA | RYYAEHKPER |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DLIINFNNAE | EDYLYGARAF | TEHEWSKNVT | AFLNLEGAGA | GGKALLFRST | NNHVARSYFK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SNRFAFASVL | GIDAFKRGVI | KSETDYVVYE | KMNNGTAGLD | LAFFRNRGIY | HTERDDIQHT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SIFSLNHMLV | NAFISLRNLL | DEKSQHFKGS | SPLYFPVFGS | YWQINLNLHL | FLNVVFLIAC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PAILFMCLFR | FPSLYAQLKK | PCYLICFTLS | SLFVLIFDYV | VVQSLTKLNP | YVIHSSPDAV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LAFFFLTNLL | GLVYSFRYVA | THSRMSNEEL | SCIEIVLIWY | VSMFWYISLL | IATLTSIVRG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LGSLYFVNFG | FFCSFFCCIL | TLIRVRYFVD | RMVTINRPAN | PEQMPLVQST | SGNAYGTSRY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PQHRLKAVVS | KSASVKLNDN | LWSVLFFSCL | VPLPLFTCYN | LLSEVFIPAV | HQSLIDGPYS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NTCYKFAVIL | VFMAIINSSP | FVFRALSKKS | SAILLMLWVS | LLFNILRAEP | FNEKAPIKFR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VFQHLNLDTS | ENLFHVQNIE | PYTQKVLNDY | PKIISDTSYQ | CVDRDCFYEA | EEPTLGFDGP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LQNAINITLH | KSLNSSLAEL | RVDAFETKWC | YFDFSVPVYV | DSINGFEVQE | EHQSLRLGVR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| NFGTPFVVKT | VAKDEDSPTN | VTVTCMWDEF | DHDKIPSYTS | LLNYIPAWSV | LTKNSTGLLK |
| MSKTHVM |