O61142
Gene name |
SUB1 |
Protein name |
Subtilisin-like protease 1 |
Names |
EC 3.4.21.62 , PfSUB-1 |
Species |
Plasmodium falciparum |
KEGG Pathway |
|
EC number |
3.4.21.62: Serine endopeptidases |
Protein Class |
PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED (PTHR42884) |
Descriptions
Plasmodium Sub1 is a serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Autoinhibition of Plasmodium Sub1 is mediated by its prodomain-driven enzyme dimerization, which is a pH-dependent process controlling enzyme activity before merozoite egress. The prodomain (PD) is composed of belt subunit and bacterial PD-like domain, and promotes assembly of inactive enzyme homodimers at acidic pH, while Sub1 is primarily monomeric at neutral pH. This mechanism ensures that Sub1 activation occurs precisely when and where needed, contributing to the tightly regulated egress of Plasmodium merozoites from host cells.
Autoinhibitory domains (AIDs)
Target domain |
330-668 (Catalytic core of Sub1) |
Relief mechanism |
Cleavage |
Assay |
Deletion assay, Structural analysis |
Target domain |
330-668 (Catalytic core of Sub1) |
Relief mechanism |
Cleavage |
Assay |
Deletion assay, Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
3 structures for O61142
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4LVN | X-ray | 225 A | PDB | ||
| 4LVO | X-ray | 226 A | PDB | ||
| AF-O61142-F1 | Predicted | AlphaFoldDB |
No variants for O61142
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O61142 | |||||
No associated diseases with O61142
6 regional properties for O61142
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase S8/S53 domain | 368 - 641 | IPR000209 |
| active_site | Peptidase S8, subtilisin, His-active site | 430 - 440 | IPR022398 |
| active_site | Peptidase S8, subtilisin, Asp-active site | 370 - 381 | IPR023827 |
| active_site | Peptidase S8, subtilisin, Ser-active site | 606 - 616 | IPR023828 |
| domain | Subtilisin SUB1-like catalytic domain | 370 - 640 | IPR034204 |
| domain | SUB1 protease prodomain ProdP9 | 140 - 219 | IPR041089 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.21.62 | Serine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | PTHR42884 | PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED |
| PANTHER Subfamily | PTHR42884:SF14 | NEUROENDOCRINE CONVERTASE 1 |
| PANTHER Protein Class |
serine protease
protein modifying enzyme |
|
| PANTHER Pathway Category |
Endothelin signaling pathway furin Alzheimer disease-presenilin pathway Furin Alzheimer disease-amyloid secretase pathway Furin |
|
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| serine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in 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 |
| MMLNKKVVAL | CTLTLHLFCI | FLCLGKEVRS | EENGKIQDDA | KKIVSELRFL | EKVEDVIEKS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NIGGNEVDAD | ENSFNPDTEV | PIEEIEEIKM | RELKDVKEEK | NKNDNHNNNN | NNNNISSSSS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SSSNTFGEEK | EEVSKKKKKL | RLIVSENHAT | TPSFFQESLL | EPDVLSFLES | KGNLSNLKNI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NSMIIELKED | TTDDELISYI | KILEEKGALI | ESDKLVSADN | IDISGIKDAI | RRGEENIDVN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DYKSMLEVEN | DAEDYDKMFG | MFNESHAATS | KRKRHSTNER | GYDTFSSPSY | KTYSKSDYLY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DDDNNNNNYY | YSHSSNGHNS | SSRNSSSSRS | RPGKYHFNDE | FRNLQWGLDL | SRLDETQELI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NEHQVMSTRI | CVIDSGIDYN | HPDLKDNIEL | NLKELHGRKG | FDDDNNGIVD | DIYGANFVNN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SGNPMDDNYH | GTHVSGIISA | IGNNNIGVVG | VDVNSKLIIC | KALDEHKLGR | LGDMFKCLDY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| CISRNAHMIN | GSFSFDEYSG | IFNSSVEYLQ | RKGILFFVSA | SNCSHPKSST | PDIRKCDLSI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NAKYPPILST | VYDNVISVAN | LKKNDNNNHY | SLSINSFYSN | KYCQLAAPGT | NIYSTAPHNS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YRKLNGTSMA | APHVAAIASL | IFSINPDLSY | KKVIQILKDS | IVYLPSLKNM | VAWAGYADIN |
| 670 | 680 | ||||
| KAVNLAIKSK | KTYINSNISN | KWKKKSRYLH |