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Protein

Vacuolar protease A

Gene

pep2

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Vacuolar aspartic endopeptidase which is probably also secreted and contributes to virulence.1 Publication

Catalytic activityi

Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei103 – 1031PROSITE-ProRule annotation
Active sitei287 – 2871PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Biological processi

Virulence

Protein family/group databases

MEROPSiA01.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protease A (EC:3.4.23.25)
Alternative name(s):
Aspartic endopeptidase pep2
Aspartic protease pep2
Gene namesi
Name:pep2
ORF Names:AFUA_3G11400
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiFungiDB:Afu3g11400.

Subcellular locationi

  • Vacuole lumen 1 Publication
  • Secreted 1 Publication

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • intracellular Source: ASPGD
  • vacuolar lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Propeptidei19 – 7052Activation peptidePRO_5000147257Add
BLAST
Chaini71 – 398328Vacuolar protease APRO_5000147258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi116 ↔ 121By similarity
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi321 ↔ 354By similarity
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiO42630.

Structurei

3D structure databases

ProteinModelPortaliO42630.
SMRiO42630. Positions 73-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 395311Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000197681.
InParanoidiO42630.
KOiK01381.
OMAiYTHNIDA.
OrthoDBiEOG092C33N0.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 2 hits.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O42630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSTSLLTAS VLLGSASAAV HKLKLNKVPL DEQLYTHNID AHVRALGQKY
60 70 80 90 100
MGIRPNVHQE LLEENSLNDM SRHDVLVDNF LNAQYFSEIS LGTPPQKFKV
110 120 130 140 150
VLDTGSSNLW VPGSDCSSIA CFLHNKYDSS ASSTYKANGT EFAIKYGSGE
160 170 180 190 200
LSGFVSQDTL QIGDLKVVKQ DFAEATNEPG LAFAFGRFDG ILGLGYDTIS
210 220 230 240 250
VNKIVPPFYN MLDQGLLDEP VFAFYLGDTN KEGDNSEASF GGVDKNHYTG
260 270 280 290 300
ELTKIPLRRK AYWEVDFDAI ALGDNVAELE NTGIILDTGT SLIALPSTLA
310 320 330 340 350
DLLNKEIGAK KGFTGQYSIE CDKRDSLPDL TFTLAGHNFT IGPYDYTLEV
360 370 380 390
QGSCISSFMG MDFPEPVGPL AILGDAFLRK WYSVYDLGNN AVGLAKAK
Length:398
Mass (Da):43,355
Last modified:June 1, 1998 - v1
Checksum:i52741DFEDBEEAF3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132504 Genomic DNA. Translation: CAA10674.1.
Y15744 mRNA. Translation: CAA75754.1.
AAHF01000002 Genomic DNA. Translation: EAL92441.1.
RefSeqiXP_754479.1. XM_749386.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00005075; CADAFUAP00005075; CADAFUAG00005075.
GeneIDi3512540.
KEGGiafm:AFUA_3G11400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132504 Genomic DNA. Translation: CAA10674.1.
Y15744 mRNA. Translation: CAA75754.1.
AAHF01000002 Genomic DNA. Translation: EAL92441.1.
RefSeqiXP_754479.1. XM_749386.1.

3D structure databases

ProteinModelPortaliO42630.
SMRiO42630. Positions 73-397.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiA01.018.

Proteomic databases

PRIDEiO42630.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00005075; CADAFUAP00005075; CADAFUAG00005075.
GeneIDi3512540.
KEGGiafm:AFUA_3G11400.

Organism-specific databases

EuPathDBiFungiDB:Afu3g11400.

Phylogenomic databases

HOGENOMiHOG000197681.
InParanoidiO42630.
KOiK01381.
OMAiYTHNIDA.
OrthoDBiEOG092C33N0.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 2 hits.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARP_ASPFU
AccessioniPrimary (citable) accession number: O42630
Secondary accession number(s): Q4WY12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: June 1, 1998
Last modified: September 7, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.