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C4JQN7 (DPEP2_UNCRE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 24. 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 UREG_03382

EC=3.4.13.19
Gene names
ORF Names:UREG_03382
OrganismUncinocarpus reesii (strain UAMH 1704) [Complete proteome]
Taxonomic identifier336963 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesOnygenaceaeUncinocarpus

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
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.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the peptidase M19 family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   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

   Cellular_componentintegral component of membrane

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

Chain1 – 453453Putative dipeptidase UREG_03382
PRO_0000411220

Regions

Transmembrane41 – 6323Helical; Potential

Sites

Metal binding951Zinc 1; catalytic By similarity
Metal binding971Zinc 1; catalytic By similarity
Metal binding2081Zinc 1; catalytic By similarity
Metal binding2081Zinc 2; catalytic By similarity
Metal binding2651Zinc 2; catalytic By similarity
Metal binding2861Zinc 2; catalytic By similarity
Binding site2211Substrate By similarity
Binding site2971Substrate By similarity
Binding site3571Substrate By similarity

Amino acid modifications

Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Disulfide bond147 ↔ 223 By similarity

Sequences

Sequence LengthMass (Da)Tools
C4JQN7 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 6E5A7FB4C93CD013

FASTA45350,043
        10         20         30         40         50         60 
MSTRDHVKQS PMPVQEGYPR SSKEFSPPSS RSRKRTWVRN LTMSLLIAAG AATFSKYIFP 

        70         80         90        100        110        120 
LGSILGAGSL QPIDPHDYAA RADRILSTTP LIDGHNDLPY LIRLETKNKI YDHEKLPFEA 

       130        140        150        160        170        180 
GLLSHTDAKK IRQGKLGGQF WSVYVECPAD PSAGIDDPSW AVRDTLEQID VAKRLVDEYP 

       190        200        210        220        230        240 
DLLEYCETAS CARSAFKKGR VGSFLGIEVH DLGVRYITVT HNCDNAFATA ASTVAAGKPD 

       250        260        270        280        290        300 
HGLTDFGREF VKEMNRLGML IDLSHVSHQT MRDVLSVTNA PVIFSHSSSY ALSKHLRNVP 

       310        320        330        340        350        360 
DDVLRTVTKN GGVVMVTFVP LFLKVNDPAS VTIHDAVDHI LHVAKVAGWD HVGIGSDFDG 

       370        380        390        400        410        420 
TAVVPKGLEN VSKYPRLVEL LLERGVTDEQ ARKLVGENLL RVWSKAEDIA YAIQASGQKP 

       430        440        450 
NEETWSGRKW TAAADIPMPS MFNDSAERRK QLE 

« Hide

References

[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UAMH 1704.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476616 Genomic DNA. Translation: EEP78536.1.
RefSeqXP_002543865.1. XM_002543819.1.

3D structure databases

ProteinModelPortalC4JQN7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8440221.
KEGGure:UREG_03382.

Phylogenomic databases

KOK01273.
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 nameDPEP2_UNCRE
AccessionPrimary (citable) accession number: C4JQN7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 7, 2009
Last modified: February 19, 2014
This is version 24 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