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Protein

Cruzipain

Gene
N/A
Organism
Trypanosoma cruzi
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes chromogenic peptides at the carboxyl Arg or Lys; requires at least one more amino acid, preferably Arg, Phe, Val or Leu, between the terminal Arg or Lys and the amino-blocking group.
The cysteine protease may play an important role in the development and differentiation of the parasites at several stages of their life cycle.

Catalytic activityi

Broad endopeptidase specificity similar to that of cathepsin L.

Enzyme regulationi

Strongly inhibited by E-64 (L-trans-epoxysuccinylleucylamido(4-guanidino)butane), Leupeptin, and N-alpha-p-tosyl-L-lysine chloromethyl ketone.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1471
Active sitei2841
Active sitei3041

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.51. 6524.
SABIO-RKP25779.

Protein family/group databases

MEROPSiC01.075.

Names & Taxonomyi

Protein namesi
Recommended name:
Cruzipain (EC:3.4.22.51)
Alternative name(s):
Cruzaine
Major cysteine proteinase
OrganismiTrypanosoma cruzi
Taxonomic identifieri5693 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3563.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18CuratedAdd BLAST18
PropeptideiPRO_000002637219 – 122Activation peptide1 PublicationAdd BLAST104
ChainiPRO_0000026373123 – 467CruzipainAdd BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi144 ↔ 185
Glycosylationi169N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi178 ↔ 223
Disulfide bondi277 ↔ 325
Glycosylationi292N-linked (GlcNAc...)Sequence analysis1
Glycosylationi377N-linked (GlcNAc...)Sequence analysis1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei337 – 338Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP25779.

Expressioni

Developmental stagei

Present in all developmental stages.

Interactioni

Chemistry databases

BindingDBiP25779.

Structurei

Secondary structure

1467
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi125 – 128Combined sources4
Helixi129 – 132Combined sources4
Beta strandi143 – 145Combined sources3
Helixi147 – 162Combined sources16
Helixi172 – 178Combined sources7
Beta strandi180 – 182Combined sources3
Helixi184 – 186Combined sources3
Helixi190 – 200Combined sources11
Beta strandi204 – 207Combined sources4
Turni208 – 210Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi225 – 227Combined sources3
Beta strandi230 – 239Combined sources10
Helixi244 – 254Combined sources11
Beta strandi257 – 261Combined sources5
Helixi263 – 265Combined sources3
Helixi266 – 268Combined sources3
Beta strandi271 – 274Combined sources4
Beta strandi284 – 297Combined sources14
Beta strandi299 – 303Combined sources5
Turni307 – 309Combined sources3
Beta strandi315 – 322Combined sources8
Helixi324 – 326Combined sources3
Beta strandi329 – 336Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIMX-ray2.00A123-337[»]
1EWLX-ray2.00A123-337[»]
1EWMX-ray2.00A123-337[»]
1EWOX-ray2.10A123-337[»]
1EWPX-ray1.75A123-337[»]
1F29X-ray2.15A/B/C123-337[»]
1F2AX-ray1.60A123-337[»]
1F2BX-ray1.80A123-337[»]
1F2CX-ray2.00A123-337[»]
1ME3X-ray1.20A123-337[»]
1ME4X-ray1.20A123-337[»]
1U9QX-ray2.30X123-337[»]
2AIMX-ray2.20A123-337[»]
2OZ2X-ray1.95A/C123-337[»]
3HD3X-ray1.75A/B123-337[»]
3I06X-ray1.10A123-337[»]
3IUTX-ray1.20A123-337[»]
3KKUX-ray1.28A123-337[»]
3LXSX-ray1.50A/C123-337[»]
4KLBX-ray2.62A/B/C/D/E123-337[»]
4PI3X-ray1.27A/B122-337[»]
4QH6X-ray3.13A/B/C/D/E123-337[»]
4W5BX-ray2.70A/B/C123-337[»]
4W5CX-ray3.27A/B/C/D/E122-337[»]
4XUIX-ray2.51A/B/C122-337[»]
ProteinModelPortaliP25779.
SMRiP25779.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25779.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1542. Eukaryota.
COG4870. LUCA.

Family and domain databases

InterProiIPR021981. DUF3586.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF12131. DUF3586. 1 hit.
PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25779-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGWARALLL AAVLVVMACL VPAATASLHA EETLTSQFAE FKQKHGRVYE
60 70 80 90 100
SAAEEAFRLS VFRENLFLAR LHAAANPHAT FGVTPFSDLT REEFRSRYHN
110 120 130 140 150
GAAHFAAAQE RARVPVKVEV VGAPAAVDWR ARGAVTAVKD QGQCGSCWAF
160 170 180 190 200
SAIGNVECQW FLAGHPLTNL SEQMLVSCDK TDSGCSGGLM NNAFEWIVQE
210 220 230 240 250
NNGAVYTEDS YPYASGEGIS PPCTTSGHTV GATITGHVEL PQDEAQIAAW
260 270 280 290 300
LAVNGPVAVA VDASSWMTYT GGVMTSCVSE QLDHGVLLVG YNDSAAVPYW
310 320 330 340 350
IIKNSWTTQW GEEGYIRIAK GSNQCLVKEE ASSAVVGGPG PTPEPTTTTT
360 370 380 390 400
TSAPGPSPSY FVQMSCTDAA CIVGCENVTL PTGQCLLTTS GVSAIVTCGA
410 420 430 440 450
ETLTEEVFLT STHCSGPSVR SSVPLNKCNR LLRGSVEFFC GSSSSGRLAD
460
VDRQRRHQPY HSRHRRL
Length:467
Mass (Da):49,836
Last modified:May 1, 1992 - v1
Checksum:iB93EBA49B511363D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti357S → C (PubMed:2038364).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti9L → S in clone 1800-2. 1
Natural varianti35T → A in clone 1800-2. 1
Natural varianti39A → V in clone 1800-2. 1
Natural varianti51S → N in clone 1800-4. 1
Natural varianti56A → R in clone 1800-2. 1
Natural varianti76N → G in clone 1800-4. 1
Natural varianti109Q → G in clone 1800-4. 1
Natural varianti117K → N in clone 1800-2. 1
Natural varianti146S → G.1
Natural varianti157 – 158EC → SG in strain: RA. 2
Natural varianti186S → G in clones 1800-2 and 1800-4. 1
Natural varianti204A → G in strain: RA. 1
Natural varianti250 – 251WL → CV in clones 1800-2 and 1800-4. 2
Natural varianti261 – 262VD → H in strain: RA. 2
Natural varianti286V → F in clone 1800-4. 1
Natural varianti286V → L in strain: RA. 1
Natural varianti308T → A in clone 1800-2. 1
Natural varianti313E → D.1
Natural varianti409L → F in clone 1800-2. 1
Natural varianti427K → Q in clone 1800-2. 1
Natural varianti430R → W in clone 1800-2. 1
Natural varianti457H → Y in clone 1800-2. 1
Natural varianti461H → Q in clone 1800-2. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84342 Genomic DNA. Translation: AAA30181.1.
M69121 Genomic DNA. Translation: AAA30269.1.
M69121 Genomic DNA. Translation: AAA30270.1.
X54414 mRNA. Translation: CAA38278.1.
M27305 Genomic DNA. Translation: AAA30180.1.
PIRiA60667.
S16162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84342 Genomic DNA. Translation: AAA30181.1.
M69121 Genomic DNA. Translation: AAA30269.1.
M69121 Genomic DNA. Translation: AAA30270.1.
X54414 mRNA. Translation: CAA38278.1.
M27305 Genomic DNA. Translation: AAA30180.1.
PIRiA60667.
S16162.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIMX-ray2.00A123-337[»]
1EWLX-ray2.00A123-337[»]
1EWMX-ray2.00A123-337[»]
1EWOX-ray2.10A123-337[»]
1EWPX-ray1.75A123-337[»]
1F29X-ray2.15A/B/C123-337[»]
1F2AX-ray1.60A123-337[»]
1F2BX-ray1.80A123-337[»]
1F2CX-ray2.00A123-337[»]
1ME3X-ray1.20A123-337[»]
1ME4X-ray1.20A123-337[»]
1U9QX-ray2.30X123-337[»]
2AIMX-ray2.20A123-337[»]
2OZ2X-ray1.95A/C123-337[»]
3HD3X-ray1.75A/B123-337[»]
3I06X-ray1.10A123-337[»]
3IUTX-ray1.20A123-337[»]
3KKUX-ray1.28A123-337[»]
3LXSX-ray1.50A/C123-337[»]
4KLBX-ray2.62A/B/C/D/E123-337[»]
4PI3X-ray1.27A/B122-337[»]
4QH6X-ray3.13A/B/C/D/E123-337[»]
4W5BX-ray2.70A/B/C123-337[»]
4W5CX-ray3.27A/B/C/D/E122-337[»]
4XUIX-ray2.51A/B/C122-337[»]
ProteinModelPortaliP25779.
SMRiP25779.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP25779.
ChEMBLiCHEMBL3563.

Protein family/group databases

MEROPSiC01.075.

Proteomic databases

PaxDbiP25779.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1542. Eukaryota.
COG4870. LUCA.

Enzyme and pathway databases

BRENDAi3.4.22.51. 6524.
SABIO-RKP25779.

Miscellaneous databases

EvolutionaryTraceiP25779.

Family and domain databases

InterProiIPR021981. DUF3586.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF12131. DUF3586. 1 hit.
PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYSP_TRYCR
AccessioniPrimary (citable) accession number: P25779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

Purified cruzipain is able to degrade itself, yielding a complex mixture of small peptides, and a major 25 kDa fragment.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.