SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

E9D269

- DPEP1_COCPS

UniProt

E9D269 - DPEP1_COCPS

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Putative dipeptidase CPSG_03667
Gene
CPSG_03667
Organism
Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Hydrolyzes a wide range of dipeptides By similarity.

Catalytic activityi

Hydrolysis of dipeptides.

Cofactori

Zinc By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Zinc 1; catalytic By similarity
Metal bindingi69 – 691Zinc 1; catalytic By similarity
Metal bindingi178 – 1781Zinc 1; catalytic By similarity
Metal bindingi178 – 1781Zinc 2; catalytic By similarity
Binding sitei205 – 2051Substrate By similarity
Metal bindingi250 – 2501Zinc 2; catalytic By similarity
Metal bindingi271 – 2711Zinc 2; catalytic By similarity
Binding sitei282 – 2821Substrate By similarity
Binding sitei342 – 3421Substrate By similarity

GO - Molecular functioni

  1. dipeptidase activity Source: UniProtKB-KW
  2. dipeptidyl-peptidase activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. metalloexopeptidase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative dipeptidase CPSG_03667 (EC:3.4.13.19)
    Gene namesi
    ORF Names:CPSG_03667
    OrganismiCoccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus)
    Taxonomic identifieri443226 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides
    ProteomesiUP000002497: Unassembled WGS sequence

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434 Reviewed prediction
    Add
    BLAST
    Chaini35 – 444410Putative dipeptidase CPSG_03667
    PRO_0000411214Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi118 ↔ 207 By similarity
    Glycosylationi413 – 4131N-linked (GlcNAc...) Reviewed prediction

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliE9D269.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M19 family.

    Keywords - Domaini

    Signal

    Phylogenomic databases

    OrthoDBiEOG7XM371.

    Family and domain databases

    InterProiIPR000180. Dipep_AS.
    IPR008257. Renal_dipep_fam.
    [Graphical view]
    PANTHERiPTHR10443. PTHR10443. 1 hit.
    PfamiPF01244. Peptidase_M19. 1 hit.
    [Graphical view]
    PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    E9D269-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQRTEHNGS WLRNAGSLLS VLACVAVLAS PASATPASAA AAATPRTDDY    50
    LKRAERILKF TPLIDGHNDL PNFIRKTTKN QIYEGKIPFE DELPGHTDLK 100
    RLRKGRVGGQ FWSVYTPCPD PPVPIDDPTW SVRDTLEQID VTKRLIEKYS 150
    RDLQFCGDAR CARRAFRRGK IASFLGIEGG HQIGNSLGDL RRVYELGVRY 200
    ITVTHNCDNA FATAQSTVAD GLPDTGLMKP FGIEFVKEMN RLGMLVDLSH 250
    VSANTMRDTL KVARAPVIFS HSSAYAVSNH LRNVPDDVLK EVAKNNGVVM 300
    VTFVSRFVNV ENPDAADINT VVDHIFHIAK VAGWDHVGIG GDYDGTVYLP 350
    KGLEDVSKYP HLIARVLERG ATTQQVRKLV GENILRVWTE VERIAKRLQK 400
    TELPNEAYWE GRNWTRPAKR DLNADFEGRS VPLFTSASNG DFCD 444
    Length:444
    Mass (Da):49,382
    Last modified:April 5, 2011 - v1
    Checksum:iD89082950FCE9BB2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL636490 Genomic DNA. Translation: EFW19283.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL636490 Genomic DNA. Translation: EFW19283.1 .

    3D structure databases

    ProteinModelPortali E9D269.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    OrthoDBi EOG7XM371.

    Family and domain databases

    InterProi IPR000180. Dipep_AS.
    IPR008257. Renal_dipep_fam.
    [Graphical view ]
    PANTHERi PTHR10443. PTHR10443. 1 hit.
    Pfami PF01244. Peptidase_M19. 1 hit.
    [Graphical view ]
    PROSITEi PS00869. RENAL_DIPEPTIDASE_1. 1 hit.
    PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RMSCC 757 / Silveira.

    Entry informationi

    Entry nameiDPEP1_COCPS
    AccessioniPrimary (citable) accession number: E9D269
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: April 5, 2011
    Last modified: September 3, 2014
    This is version 14 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi