Q95PM0
Gene name |
rhodesain |
Protein name |
Cysteine protease |
Names |
|
Species |
Trypanosoma brucei rhodesiense |
KEGG Pathway |
|
EC number |
|
Protein Class |
CYSTEINE PROTEASE FAMILY C1-RELATED (PTHR12411) |

Descriptions
Pro-rhodesain is the lysosomal cathepsin L-like cysteine protease of Trypanosoma brucei rhodesiense, the causative agent of Human African Trypanosomiasis. Autoinhibition in pro-rhodesain is mediated by a prodomain that blocks the active site, maintaining the enzyme in an inactive state until it reaches the acidic environment of the lysosome where it undergoes autocleavage. The autocleavage of prodomain relieves the autoinhibited state of pro-rhodesain in a pH-dependent manner, and lower pH values result in more efficient autocleavage.
Autoinhibitory domains (AIDs)
Target domain |
126-342 (Protease domain) |
Relief mechanism |
Cleavage |
Assay |
Structural analysis, Mutagenesis experiment |
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

No variants for Q95PM0
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q95PM0 |
No associated diseases with Q95PM0
Functions
Description | ||
---|---|---|
EC Number | ||
Subcellular Localization |
|
|
PANTHER Family | PTHR12411 | CYSTEINE PROTEASE FAMILY C1-RELATED |
PANTHER Subfamily | PTHR12411:SF947 | CATHEPSIN O |
PANTHER Protein Class |
cysteine protease
protein modifying enzyme |
|
PANTHER Pathway Category | No pathway information available |
No GO annotations of cellular component
Name | Definition |
---|---|
No GO annotations for cellular component |
1 GO annotations of molecular function
Name | Definition |
---|---|
cysteine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. |
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 |
MPRTEMVRFV | RLPVVLLAMA | ACLASVALGS | LHVEESLEMR | FAAFKKKYGK | VYKDAKEEAF |
70 | 80 | 90 | 100 | 110 | 120 |
RFRAFEENME | QAKIQAAANP | YATFGVTPFS | DMTREEFRAR | YRNGASYFAA | AQKRLRKTVN |
130 | 140 | 150 | 160 | 170 | 180 |
VTTGRAPAAV | DWREKGAVTP | VKDQGQCGSC | WAFSTIGNIE | GQWQVAGNPL | VSLSEQMLVS |
190 | 200 | 210 | 220 | 230 | 240 |
CDTIDFGCGG | GLMDNAFNWI | VNSNGGNVFT | EASYPYVSGN | GEQPQCQMNG | HEIGAAITDH |
250 | 260 | 270 | 280 | 290 | 300 |
VDLPQDEDAI | AAYLAENGPL | AIAVDATSFM | DYNGGILTSC | TSEQLDHGVL | LVGYNDSSNP |
310 | 320 | 330 | 340 | 350 | 360 |
PYWIIKNSWS | NMWGEDGYIR | IEKGTNQCLM | NQAVSSAVVG | GPTPPPPPPP | PPSATFTQDF |
370 | 380 | 390 | 400 | 410 | 420 |
CEGKGCTKGC | SHATFPTGEC | VQTTGVGSVI | ATCGASNLTQ | IIYPLSRSCS | GLSVPITVPL |
430 | 440 | ||||
DKCIPILIGS | VEYHCSTNPP | TKAARLVPHQ |