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Protein

Extracellular metalloproteinase mep

Gene

mep

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

Functioni

Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor (By similarity). Catalyzes the hydrolysis of elastin.By similarity

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi429Zinc; catalyticPROSITE-ProRule annotation1
Active sitei430PROSITE-ProRule annotation1
Metal bindingi433Zinc; 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

MEROPSiM36.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular metalloproteinase mep (EC:3.4.24.-)
Alternative name(s):
Elastinolytic metalloproteinase mep
Fungalysin mep
Gene namesi
Name:mep
ORF Names:AFUA_8G07080
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiFungiDB:Afu8g07080.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei3123. Asp f 5.0101.
75. Asp f 5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002924319 – 2451 PublicationAdd BLAST227
ChainiPRO_0000029244246 – 634Extracellular metalloproteinase mepAdd BLAST389

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi286N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein, Zymogen

Expressioni

Inductioni

Expression is controlled by the prtT transcription factor.2 Publications

Structurei

Secondary structure

1634
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi34 – 37Combined sources4
Beta strandi44 – 46Combined sources3
Helixi48 – 54Combined sources7
Helixi67 – 78Combined sources12
Beta strandi83 – 86Combined sources4
Beta strandi98 – 106Combined sources9
Beta strandi109 – 120Combined sources12
Beta strandi124 – 131Combined sources8
Helixi142 – 145Combined sources4
Helixi152 – 163Combined sources12
Beta strandi168 – 175Combined sources8
Beta strandi182 – 190Combined sources9
Beta strandi196 – 203Combined sources8
Beta strandi209 – 218Combined sources10
Beta strandi223 – 231Combined sources9
Helixi232 – 234Combined sources3
Beta strandi236 – 244Combined sources9
Beta strandi247 – 250Combined sources4
Helixi258 – 260Combined sources3
Beta strandi264 – 267Combined sources4
Turni272 – 277Combined sources6
Beta strandi288 – 299Combined sources12
Helixi331 – 334Combined sources4
Helixi335 – 355Combined sources21
Turni360 – 363Combined sources4
Beta strandi372 – 374Combined sources3
Beta strandi380 – 384Combined sources5
Beta strandi393 – 396Combined sources4
Beta strandi404 – 408Combined sources5
Beta strandi413 – 416Combined sources4
Helixi420 – 422Combined sources3
Helixi424 – 439Combined sources16
Helixi452 – 470Combined sources19
Helixi485 – 488Combined sources4
Beta strandi494 – 497Combined sources4
Turni503 – 505Combined sources3
Helixi510 – 515Combined sources6
Helixi519 – 541Combined sources23
Beta strandi546 – 548Combined sources3
Beta strandi555 – 558Combined sources4
Helixi559 – 573Combined sources15
Helixi580 – 595Combined sources16
Helixi600 – 609Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4K90X-ray1.80A246-634[»]
B31-245[»]
ProteinModelPortaliP46075.
SMRiP46075.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M36 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000159216.
InParanoidiP46075.
KOiK01417.
OMAiEEAGNFQ.
OrthoDBiEOG092C0WE3.

Family and domain databases

InterProiIPR011096. FTP_domain.
IPR001842. Peptidase_M36.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF02128. Peptidase_M36. 1 hit.
[Graphical view]
PRINTSiPR00999. FUNGALYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGLLLAGAL ALPASVFAHP AHQSYGLNRR TVDLNAFRLK SLAKYVNATE
60 70 80 90 100
TVIEAPSSFA PFKPQSYVEV ATQHVKMIAP DATFRVVDDH YVGDNGVAHV
110 120 130 140 150
HFRQTANGLD IDNADFNVNV GKDGKVFSYG NSFYTGQIPS SAALTKRDFS
160 170 180 190 200
DPVTALKGTT NTLQLPITVD SASSESTEEK ESYVFKGVSG TVSDPKAKLV
210 220 230 240 250
YFVKDDGTLA LAWRVETDID SNWLLTYIDA KSGEEIHGVV DYVAEADYQV
260 270 280 290 300
YAWGINDPTE GERTVIKDPW DSVASEFTWI SDGSTNYTTS RGNNGIAQSN
310 320 330 340 350
PSGGSSYLNN YRPSSSSLSF KYPYSVSSSP PSSYIDASII QLFYTANIYH
360 370 380 390 400
DLLYTLGFTE KAGNFEYNTN GQGGLGNDYV ILNAQDGSGT NNANFATPPD
410 420 430 440 450
GQPGRMRMYV WTESTPYRDG SFEAGIVIHE YTHGLSNRLT GGPANSNCLN
460 470 480 490 500
ALESGGMGEG WSDFMATAIR LKPGDKRSTD YTMGEWASNR AGGIRQYPYS
510 520 530 540 550
TSLSTNPLTY TSVNSLNAVH AIGTVWASML YEVLWNLIDK HGKNDAPKPT
560 570 580 590 600
LRDGVPTDGK YLAMKLVMDG MALQPCNPNF VQARDAILDA DTALTGGENQ
610 620 630
CEIWTAFAKR GLGAGAKYSS RNRVGSTEVP SGVC
Length:634
Mass (Da):68,708
Last modified:January 10, 2006 - v3
Checksum:iB9F9A8D83E1FEBBF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti305S → P in CAA83015 (PubMed:7715453).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti137Q → K in strain: Isolate 13. 1
Natural varianti197A → P in strain: Isolate 13. 1
Natural varianti419D → N in strain: Isolate 13. 1
Natural varianti448 – 450CLN → SLY in strain: Isolate 13. 3
Natural varianti482T → A in strain: Isolate 13. 1
Natural varianti529M → I in strain: Isolate 13. 1
Natural varianti573L → F in strain: Isolate 13. 1
Natural varianti578P → A in strain: Isolate 13. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30424 Genomic DNA. Translation: CAA83015.1.
L29566 Genomic DNA. Translation: AAB07708.1.
AAHF01000013 Genomic DNA. Translation: EAL85468.1.
PIRiS61435.
RefSeqiXP_747506.1. XM_742413.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003091; CADAFUAP00003091; CADAFUAG00003091.
GeneIDi3504960.
KEGGiafm:AFUA_8G07080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30424 Genomic DNA. Translation: CAA83015.1.
L29566 Genomic DNA. Translation: AAB07708.1.
AAHF01000013 Genomic DNA. Translation: EAL85468.1.
PIRiS61435.
RefSeqiXP_747506.1. XM_742413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4K90X-ray1.80A246-634[»]
B31-245[»]
ProteinModelPortaliP46075.
SMRiP46075.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3123. Asp f 5.0101.
75. Asp f 5.
MEROPSiM36.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00003091; CADAFUAP00003091; CADAFUAG00003091.
GeneIDi3504960.
KEGGiafm:AFUA_8G07080.

Organism-specific databases

EuPathDBiFungiDB:Afu8g07080.

Phylogenomic databases

HOGENOMiHOG000159216.
InParanoidiP46075.
KOiK01417.
OMAiEEAGNFQ.
OrthoDBiEOG092C0WE3.

Family and domain databases

InterProiIPR011096. FTP_domain.
IPR001842. Peptidase_M36.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF02128. Peptidase_M36. 1 hit.
[Graphical view]
PRINTSiPR00999. FUNGALYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiELM_ASPFU
AccessioniPrimary (citable) accession number: P46075
Secondary accession number(s): P46074, Q4WBR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 10, 2006
Last modified: November 2, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.