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Protein

Aspergillopepsin-1

Gene

pepA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei101PROSITE-ProRule annotation1
Active sitei283PROSITE-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:3.4.23.18By similarity)
Alternative name(s):
Aspartic protease pepA
Aspergillopepsin I
Aspergillopeptidase A
Proctase B1 Publication
Gene namesi
Name:pepA1 Publication
Synonyms:prtB1 Publication
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002592021 – 69Activation peptide1 PublicationAdd BLAST49
ChainiPRO_000002592170 – 394Aspergillopepsin-1Add BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi319 ↔ 354PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP55325.

Structurei

3D structure databases

ProteinModelPortaliP55325.
SMRiP55325.
ModBaseiSearch...
MobiDBiSearch...

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

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.

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.

P55325-1 [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
DTGSADLWGF 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 LDDEIVSAHY
310 320 330 340 350
EQVSGAQESY EAGGYVFSCS TDLPDFTVVI GDYKAVVPGK YINYAPVSTG
360 370 380 390
SSTCYGGIQS NSGLGLSILG DVFLKSQYVV FNSEGPKLGF AAQA
Length:394
Mass (Da):41,230
Last modified:October 1, 1996 - v1
Checksum:i1A2877C31915F154
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16T → S in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti44V → I in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti49L → M in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti109G → V in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti138S → T in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti299H → Y in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti310Y → E in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti322 – 323DL → NP in BAA08123 (PubMed:7787314).Curated2
Sequence conflicti340K → R in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti347V → I in BAA08123 (PubMed:7787314).Curated1
Sequence conflicti355Y → F in BAA08123 (PubMed:7787314).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49839 Genomic DNA. Translation: BAA08640.1.
D49838 mRNA. Translation: BAA08639.1.
D45177 mRNA. Translation: BAA08123.1.

Similar proteinsi

Entry informationi

Entry nameiPEPA_ASPNG
AccessioniPrimary (citable) accession number: P55325
Secondary accession number(s): Q00207, Q12371
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 5, 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

Direct protein sequencing

Documents

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