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

7 structures for Q95PM0

Entry ID Method Resolution Chain Position Source
2P7U X-ray 165 A A 126-340 PDB
2P86 X-ray 116 A A 126-340 PDB
6EX8 X-ray 160 A A/B 126-342 PDB
6EXO X-ray 190 A A/B 126-340 PDB
6EXQ X-ray 250 A A/B 126-340 PDB
7AVM X-ray 280 A A 21-342 PDB
AF-Q95PM0-F1 Predicted AlphaFoldDB

No variants for Q95PM0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q95PM0

No associated diseases with Q95PM0

3 regional properties for Q95PM0

Type Name Position InterPro Accession
domain Zinc finger, RING-type 438 - 479 IPR001841
domain Zinc finger, RanBP2-type 300 - 329 IPR001876
domain SWIB/MDM2 domain 25 - 108 IPR003121

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