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Protein

Peptidyl-Lys metalloendopeptidase

Gene

MEP

Organism
Grifola frondosa (Maitake) (Polyporus frondosus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage in proteins: -Xaa-|-Lys-(in which Xaa may be Pro).

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited by chelating agents such as EDTA and 1,10-phenanthroline.1 Publication

pH dependencei

Optimum pH is 9.5. Active from pH 6 to pH 10.5. Stable from pH 5 to pH 10.1 Publication

Temperature dependencei

Thermostable for 3 hours up to 80 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi298Zinc; catalytic1 Publication1
Active sitei2991 Publication1
Metal bindingi302Zinc; catalytic1 Publication1
Metal bindingi311Zinc; catalytic1 Publication1
Sitei314Transition state stabilizerCurated1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.20. 2512.

Protein family/group databases

MEROPSiM35.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-Lys metalloendopeptidase (EC:3.4.24.20)
Short name:
MEP
Alternative name(s):
GfMEP
Gene namesi
Name:MEP
OrganismiGrifola frondosa (Maitake) (Polyporus frondosus)
Taxonomic identifieri5627 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeGrifola

Subcellular locationi

  • Secreted Curated

  • Note: Binds strongly to beta-1,3-glucan and chitin, major polysaccharides constituting the fungal cell wall.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
PropeptideiPRO_000004339919 – 1812 PublicationsAdd BLAST163
ChainiPRO_0000043400182 – 348Peptidyl-Lys metalloendopeptidaseAdd BLAST167

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi186 ↔ 2561 Publication
Glycosylationi223O-linked (Man); partial1 Publication1
Disulfide bondi258 ↔ 2781 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi183 – 185Combined sources3
Helixi188 – 214Combined sources27
Helixi220 – 226Combined sources7
Helixi231 – 245Combined sources15
Helixi249 – 251Combined sources3
Beta strandi253 – 255Combined sources3
Beta strandi274 – 277Combined sources4
Helixi279 – 283Combined sources5
Beta strandi286 – 288Combined sources3
Helixi292 – 302Combined sources11
Helixi304 – 306Combined sources3
Helixi315 – 325Combined sources11
Helixi327 – 330Combined sources4
Helixi334 – 342Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G12X-ray1.60A182-348[»]
1GE5X-ray2.00A182-348[»]
1GE6X-ray2.20A182-348[»]
1GE7X-ray2.00A/B182-348[»]
ProteinModelPortaliP81054.
SMRiP81054.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81054.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi193 – 201Poly-Ala9

Sequence similaritiesi

Belongs to the peptidase M35 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK08646.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR029463. Lys_MEP.
IPR024079. MetalloPept_cat_dom.
[Graphical view]
PfamiPF14521. Aspzincin_M35. 1 hit.
[Graphical view]
SMARTiSM01351. Aspzincin_M35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P81054-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSSVMVALV SLAVAVSANP GLSLKVSGPE AVDGVNNLKV VTTITNTGDE
60 70 80 90 100
TLKLLNDPRG ALHTMPTDTF AITNESGETP SFIGVKVKYV PSMAAKSTGE
110 120 130 140 150
NVFAVIAPGQ SVNVEHDLSA AYNFTSSGAG TYALEALNVF NYIDPETNEP
160 170 180 190 200
VEIWADAEAH TTAVSGKLAV VRATPTLTRP VTYNGCSSSE QSALAAAASA
210 220 230 240 250
AQSYVAESLS YLQTHTAATP RYTTWFGSYI SSRHSTVLQH YTDMNSNDFS
260 270 280 290 300
SYSFDCTCTA AGTFAYVYPN RFGTVYLCGA FWKAPTTGTD SQAGTLVHES
310 320 330 340
SHFTRNGGTK DYAYGQAAAK SLATMDPDKA VMNADNHEYF SENNPAQS
Length:348
Mass (Da):36,879
Last modified:December 6, 2005 - v2
Checksum:i5F3859F10B423C79
GO

Mass spectrometryi

Molecular mass is 18028 Da from positions 182 - 348. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076805 mRNA. Translation: BAB82381.1.

Genome annotation databases

KEGGiag:BAB82381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076805 mRNA. Translation: BAB82381.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G12X-ray1.60A182-348[»]
1GE5X-ray2.00A182-348[»]
1GE6X-ray2.20A182-348[»]
1GE7X-ray2.00A/B182-348[»]
ProteinModelPortaliP81054.
SMRiP81054.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM35.004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAB82381.

Phylogenomic databases

KOiK08646.

Enzyme and pathway databases

BRENDAi3.4.24.20. 2512.

Miscellaneous databases

EvolutionaryTraceiP81054.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR029463. Lys_MEP.
IPR024079. MetalloPept_cat_dom.
[Graphical view]
PfamiPF14521. Aspzincin_M35. 1 hit.
[Graphical view]
SMARTiSM01351. Aspzincin_M35. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLMP_GRIFR
AccessioniPrimary (citable) accession number: P81054
Secondary accession number(s): Q8WZH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 95 of the entry and version 2 of the sequence. [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.