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Protein

Aspergillopepsin-1

Gene

pepA

Organism
Aspergillus phoenicis (Aspergillus saitoi)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but also accepts a lysine residue in the P1 position, leading to the activation of trypsinogen and chymotrypsinogen A.3 Publications

Catalytic activityi

Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.1 Publication

pH dependencei

Optimum pH is 2.9-3.3.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei101PROSITE-ProRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionAspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspergillopepsin-1Curated (EC:3.4.23.181 Publication)
Alternative name(s):
Aspartic protease pepA
Aspergillopepsin I1 Publication
Aspergillopeptidase A
Protease type XIII
Gene namesi
Name:pepA
OrganismiAspergillus phoenicis (Aspergillus saitoi)
Taxonomic identifieri5063 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi145D → S: Changes specificity toward basic substrates. 1 Publication1

Protein family/group databases

Allergomei8264. Asp sa AP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002592421 – 69Activation peptide1 PublicationAdd BLAST49
ChainiPRO_000002592570 – 394Aspergillopepsin-1Add BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi129O-linked (Man...) serine1 Publication1
Glycosylationi304O-linked (Man...) serine1 Publication1
Disulfide bondi319 ↔ 354PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi72 – 78Combined sources7
Turni80 – 82Combined sources3
Beta strandi85 – 92Combined sources8
Beta strandi94 – 101Combined sources8
Beta strandi107 – 110Combined sources4
Helixi116 – 119Combined sources4
Beta strandi138 – 142Combined sources5
Beta strandi144 – 146Combined sources3
Beta strandi148 – 160Combined sources13
Beta strandi163 – 176Combined sources14
Helixi178 – 181Combined sources4
Beta strandi188 – 191Combined sources4
Helixi195 – 197Combined sources3
Beta strandi201 – 203Combined sources3
Helixi208 – 212Combined sources5
Helixi213 – 215Combined sources3
Beta strandi216 – 226Combined sources11
Beta strandi229 – 237Combined sources9
Helixi240 – 242Combined sources3
Beta strandi243 – 245Combined sources3
Beta strandi248 – 251Combined sources4
Beta strandi260 – 263Combined sources4
Beta strandi265 – 268Combined sources4
Beta strandi278 – 282Combined sources5
Beta strandi288 – 291Combined sources4
Helixi293 – 300Combined sources8
Beta strandi310 – 314Combined sources5
Beta strandi316 – 318Combined sources3
Beta strandi326 – 330Combined sources5
Beta strandi333 – 337Combined sources5
Helixi339 – 342Combined sources4
Beta strandi343 – 348Combined sources6
Beta strandi352 – 360Combined sources9
Turni362 – 364Combined sources3
Beta strandi366 – 369Combined sources4
Helixi371 – 374Combined sources4
Beta strandi377 – 382Combined sources6
Turni383 – 386Combined sources4
Beta strandi387 – 393Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IBQX-ray2.14A/B70-394[»]
ProteinModelPortaliQ12567.
SMRiQ12567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini85 – 391Peptidase A1PROSITE-ProRule annotationAdd BLAST307

Sequence similaritiesi

Belongs to the peptidase A1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

CDDicd06097. Aspergillopepsin_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiView protein in InterPro
IPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR034163. Aspergillopepsin-like_cat_dom.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiView protein in Pfam
PF00026. Asp. 1 hit.
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiView protein in PROSITE
PS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q12567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVFSKTAAL VLGLSTAVSA APAPTRKGFT INQIARPANK TRTVNLPGLY
60 70 80 90 100
ARSLAKFGGT VPQSVKEAAS KGSAVTTPQN NDEEYLTPVT VGKSTLHLDF
110 120 130 140 150
DTGSADLWVF SDELPSSEQT GHDLYTPSSS ATKLSGYSWD ISYGDGSSAS
160 170 180 190 200
GDVYRDTVTV GGVTTNKQAV EAASKISSEF VQDTANDGLL GLAFSSINTV
210 220 230 240 250
QPKAQTTFFD TVKSQLDSPL FAVQLKHDAP GVYDFGYIDD SKYTGSITYT
260 270 280 290 300
DADSSQGYWG FSTDGYSIGD GSSSSSGFSA IADTGTTLIL LDDEIVSAYY
310 320 330 340 350
EQVSGAQESY EAGGYVFSCS TDLPDFTVVI GDYKAVVPGK YINYAPVSTG
360 370 380 390
SSTCYGGIQS NSGLGLSILG DVFLKSQYVV FNSEGPKLGF AAQA
Length:394
Mass (Da):41,298
Last modified:November 1, 1997 - v1
Checksum:i70FC32D747101551
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25318 Genomic DNA. Translation: BAA04988.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25318 Genomic DNA. Translation: BAA04988.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IBQX-ray2.14A/B70-394[»]
ProteinModelPortaliQ12567.
SMRiQ12567.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei8264. Asp sa AP.
MEROPSiA01.016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ12567.

Family and domain databases

CDDicd06097. Aspergillopepsin_like. 1 hit.
Gene3Di2.40.70.10. 2 hits.
InterProiView protein in InterPro
IPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR034163. Aspergillopepsin-like_cat_dom.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiView protein in Pfam
PF00026. Asp. 1 hit.
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiView protein in PROSITE
PS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPEPA_ASPPH
AccessioniPrimary (citable) accession number: Q12567
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 10, 2017
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.