Q5J6J2
Gene name |
SCPB |
Protein name |
Carboxypeptidase S1 homolog B |
Names |
Serine carboxypeptidase B, SPCB |
Species |
Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum) |
KEGG Pathway |
|
EC number |
3.4.16.6: Serine-type carboxypeptidases |
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 Q5J6J2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5J6J2-F1 | Predicted | AlphaFoldDB |
No variants for Q5J6J2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5J6J2 | |||||
No associated diseases with Q5J6J2
1 regional properties for Q5J6J2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Serine carboxypeptidase, serine active site | 236 - 243 | IPR018202 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.16.6 | Serine-type carboxypeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| anchored component of membrane | The component of a membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| serine-type carboxypeptidase activity | Catalysis of the hydrolysis of a single C-terminal amino acid residue from the C-terminus of a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
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 |
| MVSFCGVAAC | LLTVAGHLAQ | AQFPPKPEGV | TVLESKFGSG | ARITYKEPGL | CETTEGVKSY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AGYVHLPPGT | LRDFGVEQDY | PINTFFWFFE | ARKDPENAPL | GIWMNGGPGS | SSMFGMMTEN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GPCFVNADSN | STRLNPHSWN | NEVNMLYIDQ | PVQVGLSYDT | LANFTRNLVT | DEITKLKPGE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PIPEQNATFL | VGTYASRNMN | TTAHGTRHAA | MALWHFAQVW | FQEFPGYHPR | NNKISIATES |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YGGRYGPAFT | AFFEEQNQKI | KNGTWKGHEG | TMHVLHLDTL | MIVNGCIDRL | VQWPAYPQMA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YNNTYSIEAV | NASIHAGMLD | ALYRDGGCRD | KINHCRSLSS | VFDPENLGIN | STVNDVCKDA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ETFCSNDVRD | PYLKFSGRNY | YDIGQLDPSP | FPAPFYMAWL | NQPHVQAALG | VPLNWTQSND |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VVSTAFRAIG | DYPRPGWLEN | LAYLLENGIK | VSLVYGDRDY | ACNWFGGELS | SLGINYTDTH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EFHNAGYAGI | QINSSYIGGQ | VRQYGNLSFA | RVYEAGHEVP | SYQPETALQI | FHRSLFNKDI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ATGTKDTSSR | MDGGKFYGTS | GPADSFGFKN | KPPPQHVHFC | HILDTSTCTK | EQIQSVENGT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AAVRSWIIVD | SNSTSLFPEV | VGSGEPTPTP | MPGGATTLSA | HGFLYGVTLW | AVIVVAVIEL |
| AM |