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C5FK77 (DPEP1_ARTOC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 25. 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 MCYG_02918

EC=3.4.13.19
Gene names
ORF Names:MCYG_02918
OrganismArthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) [Complete proteome]
Taxonomic identifier554155 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeArthroderma

Protein attributes

Sequence length427 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 – 2929 Potential
Chain30 – 427398Putative dipeptidase MCYG_02918
PRO_0000411212

Sites

Metal binding551Zinc 1; catalytic By similarity
Metal binding571Zinc 1; catalytic By similarity
Metal binding1671Zinc 1; catalytic By similarity
Metal binding1671Zinc 2; catalytic By similarity
Metal binding2381Zinc 2; catalytic By similarity
Metal binding2591Zinc 2; catalytic By similarity
Binding site1941Substrate By similarity
Binding site2701Substrate By similarity
Binding site3301Substrate By similarity

Amino acid modifications

Glycosylation4021N-linked (GlcNAc...) Potential
Disulfide bond106 ↔ 196 By similarity

Sequences

Sequence LengthMass (Da)Tools
C5FK77 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 319F365AADE47FED

FASTA42747,242
        10         20         30         40         50         60 
MAPERRSRLS DAGILVSLLA LTSLVPVQAA VTTSKPDYAK RAERVLRSTP LIDGHNDLPF 

        70         80         90        100        110        120 
AIRRSTHDQI YDGKVPFETA LKGQTDLPRM RKGRMGGQFW SVYVGCPSDP NTPIDFPTFA 

       130        140        150        160        170        180 
TRDTLEQIDV ARRLVDKYSK DLMYCDNPAC AKKAFREGKI GSFIGIEGGH QVGSSIAALR 

       190        200        210        220        230        240 
QAFYAGARYM TLTHNCDNAW ATAASTVRAG KPDLGMTEFG PALIKEMNRL GMLVDLSHVS 

       250        260        270        280        290        300 
HQTMRDVLKV TKAPVIFSHS SAYAVSKHLR NVPDDVLKTV AKNNGVVMVT FVRSFVNIDN 

       310        320        330        340        350        360 
PDSVTVDDIV KHIFHIAEVA GWDHVGLGGD YDGTTELPKG LEDVSKYPYL IEKVLEHGAT 

       370        380        390        400        410        420 
EEQARKLIGE NILRVWTEVE KIGKRIQNSG ALPVEEVWQG RNWTQSLTKR STFIPTESPT 


QLEFGCD 

« 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-4605 / CBS 113480.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS995703 Genomic DNA. Translation: EEQ30099.1.
RefSeqXP_002847412.1. XM_002847366.1.

3D structure databases

ProteinModelPortalC5FK77.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9224858.

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_ARTOC
AccessionPrimary (citable) accession number: C5FK77
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 25 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