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Entry version 137 (02 Jun 2021)
Sequence version 1 (01 Mar 2003)
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Protein

Subtilisin-like protease 1

Gene

SUB1

Organism
Plasmodium falciparum (isolate 3D7)
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

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 (PubMed:18083098, PubMed:19214190, PubMed:21220481, PubMed:29459732).

Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress (PubMed:18083098, PubMed:19214190, PubMed:29459732).

Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes (PubMed:19214190, PubMed:29459732).

Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form (PubMed:21220481).

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

p54 and probably p47 forms are inhibited by the non-covalent interaction with the cleaved propeptide (PubMed:19214190). Inhibited by subtilisin propeptide-like protein SUB1-ProM (PubMed:31942933). Inhibited by small molecule MRT12113 (PubMed:18083098).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi338Calcium 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei372Charge relay systemPROSITE-ProRule annotation1
Metal bindingi381Calcium 1By similarity1
Metal bindingi392Calcium 2By similarity1
Metal bindingi392Calcium 3By similarity1
Metal bindingi396Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi399Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi400Calcium 3By similarity1
Metal bindingi401Calcium 2By similarity1
Metal bindingi402Calcium 3By similarity1
Metal bindingi404Calcium 3By similarity1
Metal bindingi406Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi408Calcium 2By similarity1
Metal bindingi409Calcium 3By similarity1
Active sitei428Charge relay systemPROSITE-ProRule annotation1
Metal bindingi439Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi442Calcium 1By similarity1
Metal bindingi444Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi446Calcium 1; via carbonyl oxygenBy similarity1
Active sitei606Charge relay systemPROSITE-ProRule annotation1

<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

GO - Biological processi

<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, Serine protease
LigandCalcium, Metal-binding

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S08.012

<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%5Fand%5Ftaxonomy%5Fsection">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:
Subtilisin-like protease 11 Publication (EC:3.4.21.624 Publications)
Alternative name(s):
PfSUB11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SUB11 Publication
ORF Names:PF3D7_0507500Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiPlasmodium falciparum (isolate 3D7)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri36329 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaSarAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001450 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
PlasmoDB:PF3D7_0507500

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Blood stage parasites are not viable (PubMed:18083098, PubMed:29459732). Initial schizont development is normal but merozoite egress is abolished due to a failure to rupture the parasitophorous vacuole membrane (PubMed:29459732).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi606S → A: Loss of catalytic activity. Blood stage parasites are not viable. 1 Publication1

<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 – 25By similarityAdd BLAST25
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_000045020026 – 217Inhibition peptideBy similarityAdd BLAST192
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_5004308256218 – 688Subtilisin-like protease 1Sequence analysisAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi112N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi171N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi261N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi317N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi322N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 bondi369 ↔ 479By similarity
Glycosylationi417N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi458 ↔ 475By similarity
Glycosylationi488N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi501N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi520N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi521 ↔ 534By similarity
Glycosylationi603N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi675N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The propeptide (p31) is cleaved, probably by autocatalysis, during the transport to or in the Golgi apparatus, and remains non-covalently associated with the p54 form as an inhibitor. p54 is further cleaved into the p45 form (By similarity). This cleavage is likely occurring in the exoneme prior to egress and may be mediated by PMX/plasmepsin X (By similarity).By similarity
The disulfide bond between Cys-521 and Cys-534 acts as a redox-sensitive disulfide switch. The oxidized form is required for catalytic activity.By similarity
The relevance of the N-glycosylation is not clear. In an insect expression system, SUB1 glycosylation appears to affect its processing into the active mature form suggesting that SUB1 may not be N-glycosylated in parasites.By similarity

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>Sitei217 – 218Cleavage; by autolysisBy similarity2
Sitei249 – 250CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8I0V0

<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

Expressed during the parasite blood stage, specifically in schizonts (at protein level).1 Publication

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer between p54 form and propeptide p31; the interaction inhibits p54 catalytic activity.

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q8I0V0, 3 interactors

<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

3D structure databases

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

More...
SMRi
Q8I0V0

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini343 – 661Peptidase S8PROSITE-ProRule annotationAdd BLAST319

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni99 – 129DisorderedSequence analysisAdd BLAST31
Regioni264 – 284DisorderedSequence analysisAdd BLAST21
Regioni303 – 332DisorderedSequence analysisAdd BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi106 – 125Polar residuesSequence analysisAdd BLAST20
Compositional biasi303 – 330Polar residuesSequence analysisAdd BLAST28

<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 S8 family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_455979_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8I0V0

Identification of Orthologs from Complete Genome Data

More...
OMAi
FKCIDYC

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07473, Peptidases_S8_Subtilisin_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.200, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017314, Pept_S8A_PfSUB_1
IPR000209, Peptidase_S8/S53_dom
IPR036852, Peptidase_S8/S53_dom_sf
IPR023827, Peptidase_S8_Asp-AS
IPR022398, Peptidase_S8_His-AS
IPR023828, Peptidase_S8_Ser-AS
IPR015500, Peptidase_S8_subtilisin-rel
IPR034204, PfSUB1-like_cat_dom
IPR041089, SUB1_ProdP9

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00082, Peptidase_S8, 1 hit
PF18213, SUB1_ProdP9, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037900, Subtilisin_rel_PfSUB_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00723, SUBTILISIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52743, SSF52743, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51892, SUBTILASE, 1 hit
PS00136, SUBTILASE_ASP, 1 hit
PS00137, SUBTILASE_HIS, 1 hit
PS00138, SUBTILASE_SER, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q8I0V0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMLNKKVVAL CTLTLHLFCI FLCLGKEVRS EENGKIQDDA KKIVSELRFL
60 70 80 90 100
EKVEDVIEKS NIGGNEVDAD ENSFNPDTEV PIEEIEEIKM RELKDVKEEK
110 120 130 140 150
NKNDNHNNNN NNISSSSSSS SNTFGEEKEE VSKKKKKLRL IVSENHATTP
160 170 180 190 200
SFFQESLLEP DVLSFLESKG NLSNLKNINS MIIELKEDTT DDELISYIKI
210 220 230 240 250
LEEKGALIES DKLVSADNID ISGIKDAIRR GEENIDVNDY KSMLEVENDA
260 270 280 290 300
EDYDKMFGMF NESHAATSKR KRHSTNERGY DTFSSPSYKT YSKSDYLYDD
310 320 330 340 350
DNNNNNYYYS HSSNGHNSSS RNSSSSRSRP GKYHFNDEFR NLQWGLDLSR
360 370 380 390 400
LDETQELINE HQVMSTRICV IDSGIDYNHP DLKDNIELNL KELHGRKGFD
410 420 430 440 450
DDNNGIVDDI YGANFVNNSG NPMDDNYHGT HVSGIISAIG NNNIGVVGVD
460 470 480 490 500
VNSKLIICKA LDEHKLGRLG DMFKCLDYCI SRNAHMINGS FSFDEYSGIF
510 520 530 540 550
NSSVEYLQRK GILFFVSASN CSHPKSSTPD IRKCDLSINA KYPPILSTVY
560 570 580 590 600
DNVISVANLK KNDNNNHYSL SINSFYSNKY CQLAAPGTNI YSTAPHNSYR
610 620 630 640 650
KLNGTSMAAP HVAAIASLIF SINPDLSYKK VIQILKDSIV YLPSLKNMVA
660 670 680
WAGYADINKA VNLAIKSKKT YINSNISNKW KKKSRYLH
Length:688
Mass (Da):77,647
Last modified:March 1, 2003 - 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:iFACFEFB495AEF4F7
GO

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
AL844504 Genomic DNA Translation: CAD51440.1

NCBI Reference Sequences

More...
RefSeqi
XP_001351633.1, XM_001351597.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
CAD51440; CAD51440; PF3D7_0507500

GeneDB pathogen genome database from Sanger Institute

More...
GeneDBi
PF3D7_0507500.1:pep

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
812875

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pfa:PF3D7_0507500

<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
AL844504 Genomic DNA Translation: CAD51440.1
RefSeqiXP_001351633.1, XM_001351597.1

3D structure databases

SMRiQ8I0V0
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ8I0V0, 3 interactors

Protein family/group databases

MEROPSiS08.012

Proteomic databases

PRIDEiQ8I0V0

Genome annotation databases

EnsemblProtistsiCAD51440; CAD51440; PF3D7_0507500
GeneDBiPF3D7_0507500.1:pep
GeneIDi812875
KEGGipfa:PF3D7_0507500

Organism-specific databases

VEuPathDBiPlasmoDB:PF3D7_0507500

Phylogenomic databases

HOGENOMiCLU_455979_0_0_1
InParanoidiQ8I0V0
OMAiFKCIDYC

Family and domain databases

CDDicd07473, Peptidases_S8_Subtilisin_like, 1 hit
Gene3Di3.40.50.200, 1 hit
InterProiView protein in InterPro
IPR017314, Pept_S8A_PfSUB_1
IPR000209, Peptidase_S8/S53_dom
IPR036852, Peptidase_S8/S53_dom_sf
IPR023827, Peptidase_S8_Asp-AS
IPR022398, Peptidase_S8_His-AS
IPR023828, Peptidase_S8_Ser-AS
IPR015500, Peptidase_S8_subtilisin-rel
IPR034204, PfSUB1-like_cat_dom
IPR041089, SUB1_ProdP9
PfamiView protein in Pfam
PF00082, Peptidase_S8, 1 hit
PF18213, SUB1_ProdP9, 1 hit
PIRSFiPIRSF037900, Subtilisin_rel_PfSUB_1, 1 hit
PRINTSiPR00723, SUBTILISIN
SUPFAMiSSF52743, SSF52743, 1 hit
PROSITEiView protein in PROSITE
PS51892, SUBTILASE, 1 hit
PS00136, SUBTILASE_ASP, 1 hit
PS00137, SUBTILASE_HIS, 1 hit
PS00138, SUBTILASE_SER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiSUB1_PLAF7
<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: Q8I0V0
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 17, 2020
Last sequence update: March 1, 2003
Last modified: June 2, 2021
This is version 137 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

Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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