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Protein

Neutral protease 2 homolog mep20

Gene

mep20

Organism
Neosartorya fumigata (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine. May be involved in virulence (By similarity).By similarity

Catalytic activityi

Preferential cleavage of bonds with hydrophobic residues in P1'; also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi299Zinc; catalyticPROSITE-ProRule annotation1
Active sitei300PROSITE-ProRule annotation1
Metal bindingi303Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi314Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM35.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral protease 2 homolog mep20 (EC:3.4.24.39)
Alternative name(s):
Deuterolysin mep20
Gene namesi
Name:mep20
OrganismiNeosartorya fumigata (Aspergillus fumigatus)
Taxonomic identifieri746128 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000040706420 – 172By similarityAdd BLAST153
ChainiPRO_0000407065173 – 365Neutral protease 2 homolog mep20Add BLAST193

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi73N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi178 ↔ 249By similarity
Disulfide bondi256 ↔ 274By similarity
Glycosylationi351N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ09016.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M35 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001384. Peptidase_M35.
[Graphical view]
PfamiPF02102. Peptidase_M35. 1 hit.
[Graphical view]
PRINTSiPR00768. DEUTEROLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q09016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTILASAI LALINGALAL PANTPTLDVT LTQVDNTRIK ATVKNTGNEK
60 70 80 90 100
VTFVHLNFFQ DAAPVKKVSL FRNGTEVEFT GIKRRLLTEG LSDDGLTTLA
110 120 130 140 150
PGGTFEDEFD VASTGDLTEG GTVTIRTDGF VPITTDRKVS GYIPYQSNEL
160 170 180 190 200
EIEVDPAKAA AVPQAIKLLD RRTKVASCSG SRASALSTAL RNAGSLANAA
210 220 230 240 250
ASAASSGSST RFQEYFKTTS RRPENVGGRF RAVGREASSQ SSGKTTYYCN
260 270 280 290 300
DPYGYCDSNT LAYTLPSSNL IANCDIYYSY LPALTSSCHA QDQATTTLHE
310 320 330 340 350
FTHAPAVYSP GTDDYAYGYR ASTALSASQA LLNADTYALF ANGSPLLPLS
360
NHSKCRNTMV WRTLL
Length:365
Mass (Da):39,031
Last modified:November 1, 1996 - v1
Checksum:i61495EA7CF94C345
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24146 Genomic DNA. Translation: AAB07644.1.
PIRiJC4379.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24146 Genomic DNA. Translation: AAB07644.1.
PIRiJC4379.

3D structure databases

ProteinModelPortaliQ09016.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM35.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001384. Peptidase_M35.
[Graphical view]
PfamiPF02102. Peptidase_M35. 1 hit.
[Graphical view]
PRINTSiPR00768. DEUTEROLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMEP20_ASPFM
AccessioniPrimary (citable) accession number: Q09016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.