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Entry version 126 (08 May 2019)
Sequence version 1 (01 May 1992)
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Protein

Cruzipain

Gene
N/A
Organism
Trypanosoma cruzi
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Broad endopeptidase specificity similar to that of cathepsin L. EC:3.4.22.51

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1471
Active sitei2841
Active sitei3041

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.22.51 6524

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P25779

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C01.075

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cruzipain (EC:3.4.22.51)
Alternative name(s):
Cruzaine
Major cysteine proteinase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTrypanosoma cruzi
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5693 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3563

Drug and drug target database

More...
DrugBanki
DB04427 3-[[N-[4-Methyl-Piperazinyl]Carbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonic Acid Benzyloxy-Amide
DB02051 3-[N-[Benzyloxycarbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonic Acid 4-Nitro-Phenyl Ester
DB02200 3-[N-[Benzyloxycarbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonylmethylbenzene
DB01871 [1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester
DB02128 [1-(3-Hydroxy-2-Oxo-1-Phenethyl-Propylcarbamoyl)2-Phenyl-Ethyl]-Carbamic Acid Pyridin-4-Ylmethyl Ester
DB03536 Benzoyl-Arginine-Alanine-Methyl Ketone
DB03691 WRR-112
DB04502 WRR-204
DB03573 WRR-99

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18CuratedAdd BLAST18
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002637219 – 122Activation peptide1 PublicationAdd BLAST104
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000026373123 – 467CruzipainAdd BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi144 ↔ 185
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi169N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi178 ↔ 223
Disulfide bondi277 ↔ 325
Glycosylationi292N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi377N-linked (GlcNAc...) asparagineSequence analysis1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei337 – 338Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Present in all developmental stages.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P25779

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1467
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P25779

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P25779

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1542 Eukaryota
COG4870 LUCA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02248 Peptidase_C1A, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR021981 DUF3586
IPR038765 Papain-like_cys_pep_sf
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR000668 Peptidase_C1A_C
IPR039417 Peptidase_C1A_papain-like
IPR013201 Prot_inhib_I29

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12131 DUF3586, 1 hit
PF08246 Inhibitor_I29, 1 hit
PF00112 Peptidase_C1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00705 PAPAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00848 Inhibitor_I29, 1 hit
SM00645 Pept_C1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54001 SSF54001, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB93EBA49B511363D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti357S → C (PubMed:2038364).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
A60667
S16162

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
SMRiP25779
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP25779
ChEMBLiCHEMBL3563
DrugBankiDB04427 3-[[N-[4-Methyl-Piperazinyl]Carbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonic Acid Benzyloxy-Amide
DB02051 3-[N-[Benzyloxycarbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonic Acid 4-Nitro-Phenyl Ester
DB02200 3-[N-[Benzyloxycarbonyl]-Phenylalaninyl-Amino]-5-Phenyl-Pentane-1-Sulfonylmethylbenzene
DB01871 [1-(1-Benzyl-3-Hydroxy-2-Oxo-Propylcarbamoyl)-2-Phenyl-Ethyl]-Carbamic Acid Benzyl Ester
DB02128 [1-(3-Hydroxy-2-Oxo-1-Phenethyl-Propylcarbamoyl)2-Phenyl-Ethyl]-Carbamic Acid Pyridin-4-Ylmethyl Ester
DB03536 Benzoyl-Arginine-Alanine-Methyl Ketone
DB03691 WRR-112
DB04502 WRR-204
DB03573 WRR-99

Protein family/group databases

MEROPSiC01.075

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1542 Eukaryota
COG4870 LUCA

Enzyme and pathway databases

BRENDAi3.4.22.51 6524
SABIO-RKiP25779

Miscellaneous databases

EvolutionaryTraceiP25779

Family and domain databases

CDDicd02248 Peptidase_C1A, 1 hit
InterProiView protein in InterPro
IPR021981 DUF3586
IPR038765 Papain-like_cys_pep_sf
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR000668 Peptidase_C1A_C
IPR039417 Peptidase_C1A_papain-like
IPR013201 Prot_inhib_I29
PfamiView protein in Pfam
PF12131 DUF3586, 1 hit
PF08246 Inhibitor_I29, 1 hit
PF00112 Peptidase_C1, 1 hit
PRINTSiPR00705 PAPAIN
SMARTiView protein in SMART
SM00848 Inhibitor_I29, 1 hit
SM00645 Pept_C1, 1 hit
SUPFAMiSSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCYSP_TRYCR
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P25779
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 8, 2019
This is version 126 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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