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E5R2Q7 (DPEP1_ARTGP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative dipeptidase MGYG_00085

EC=3.4.13.19
Gene names
ORF Names:MGYG_00085
OrganismArthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum gypseum) [Complete proteome]
Taxonomic identifier535722 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeArthroderma

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolyzes a wide range of dipeptides By similarity.

Catalytic activity

Hydrolysis of dipeptides.

Cofactor

Zinc By similarity.

Sequence similarities

Belongs to the peptidase M19 family.

Ontologies

Keywords
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionDipeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondipeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 425394Putative dipeptidase MGYG_00085
PRO_0000411211

Sites

Metal binding561Zinc 1; catalytic By similarity
Metal binding581Zinc 1; catalytic By similarity
Metal binding1681Zinc 1; catalytic By similarity
Metal binding1681Zinc 2; catalytic By similarity
Metal binding2391Zinc 2; catalytic By similarity
Metal binding2601Zinc 2; catalytic By similarity
Binding site1951Substrate By similarity
Binding site2711Substrate By similarity
Binding site3311Substrate By similarity

Amino acid modifications

Glycosylation4031N-linked (GlcNAc...) Potential
Disulfide bond107 ↔ 197 By similarity

Sequences

Sequence LengthMass (Da)Tools
E5R2Q7 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 8CF4ECF0EF852F64

FASTA42546,723
        10         20         30         40         50         60 
MAPERRSRLS ETAGLFVSLL ALTSIVPVQA VATVPQTDYA KRAERVLRSA PLIDGHNDLP 

        70         80         90        100        110        120 
YAIRKSTRDQ IYDGKLPFET SLKGHTDLPR MRKGRMGGQF WSVFIACPSD PNAPIDLPTF 

       130        140        150        160        170        180 
ATRDTLEQID VARRLVDKYS KDLMFCDNPG CAKRAFRQGK IGSFLGIEGG HQVGSSIAAL 

       190        200        210        220        230        240 
RQAFYAGARY MTITHNCDNA WATAASTVRA GKPDLGMTDF GPALIKEMNR LGMLVDLSHV 

       250        260        270        280        290        300 
SHQSMRDILK VTKAPVIFSH SSAYEVSKHL RNVPDDVLKT VAKNNGVVMV TFVRTFVNVD 

       310        320        330        340        350        360 
DPDSVDVNTI VKHIFHIAKV AGWDHVGLGG DYDGTTELPK GLEDVSKYPY LIEKVLEAGA 

       370        380        390        400        410        420 
TEEQARKLVG ENVLRVWTEV EQIAKKIQRS GALPVEEVWK GRNGTALSER STFIEGPAPL 


AYGCD 

« Hide

References

[1]"Comparative genome analysis of Trichophyton rubrum and related dermatophytes reveals candidate genes involved in infection."
Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., Rossi A., Saif S. expand/collapse author list , Samalova M., Saunders C.W., Shea T., Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.
MBio 3:E259-E259(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4604 / CBS 118893.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS989822 Genomic DNA. Translation: EFQ97041.1.
RefSeqXP_003175993.1. XM_003175945.1.

3D structure databases

ProteinModelPortalE5R2Q7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10031304.

Phylogenomic databases

OrthoDBEOG7XM371.

Family and domain databases

InterProIPR028536. Dpep1-like.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF12. PTHR10443:SF12. 1 hit.
PfamPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEPS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPEP1_ARTGP
AccessionPrimary (citable) accession number: E5R2Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: February 8, 2011
Last modified: February 19, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries