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Q5J6J0

- CBPYA_TRIRU

UniProt

Q5J6J0 - CBPYA_TRIRU

Protein

Carboxypeptidase Y homolog A

Gene

cpyA

Organism
Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate By similarity.By similarity

    Catalytic activityi

    Release of a C-terminal amino acid with broad specificity.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei259 – 2591PROSITE-ProRule annotation
    Active sitei451 – 4511PROSITE-ProRule annotation
    Active sitei513 – 5131PROSITE-ProRule annotation

    GO - Molecular functioni

    1. serine-type carboxypeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Protease

    Protein family/group databases

    MEROPSiS10.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase Y homolog A (EC:3.4.16.5)
    Gene namesi
    Name:cpyA
    Synonyms:ScpC
    OrganismiTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
    Taxonomic identifieri5551 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

    Subcellular locationi

    Vacuole By similarity

    GO - Cellular componenti

    1. vacuole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 124107By similarityPRO_0000407484Add
    BLAST
    Chaini125 – 536412Carboxypeptidase Y homolog APRO_0000407485Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi172 ↔ 412By similarity
    Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi306 ↔ 320By similarity
    Disulfide bondi330 ↔ 353By similarity
    Disulfide bondi337 ↔ 346By similarity
    Disulfide bondi375 ↔ 382By similarity
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliQ5J6J0.
    SMRiQ5J6J0. Positions 120-533.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S10 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view]
    PANTHERiPTHR11802. PTHR11802. 1 hit.
    PfamiPF00450. Peptidase_S10. 1 hit.
    [Graphical view]
    PRINTSiPR00724. CRBOXYPTASEC.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q5J6J0-1 [UniParc]FASTAAdd to Basket

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    MKFFTTGLLA TAALAAAQEQ QVLQAEDGMG RAPLPDSSIF DETLQKFQSS    50
    LEDGISHFWS EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW 100
    VQGADGEKRR EIDGKLHNYD LRVKAVDPGV KQYSGYLDDN DADKHLFYWF 150
    FESRNDPKND PVVLWLNGGP GCSSLTGLFL ELGPATIDKN LKVVSNPYSW 200
    NSNASVIFLD QPVNVGFSYS GSSVSDTVAA GKDVYALLTL FFKQFPEYAT 250
    QDFHISGESY AGHYIPVFAA EILSHKNTNI NLKSALIGNG LTDPLTQYPQ 300
    YRPMACGEGG YPAVLDQGTC RSMDNSLERC LSLIETCYSS ESAWVCVPAA 350
    MYCNSAILAP YQQTGMNPYD VRTKCEDMAS LCYPQLNAIT EWLNQKPVMQ 400
    ALGVEVESYE SCNSGINRDF LFHGDWMKPY HRLVPSVLEK IPVLIYAGDA 450
    DFICNWLGNK AWTEALEWPG HKKFAETKLE DLKIVDNKNK GKKIGQVKSS 500
    GNFTFMRIFG AGHMVPLNQP EASLEFLNRW LRGEWH 536
    Length:536
    Mass (Da):60,099
    Last modified:February 15, 2005 - v1
    Checksum:i0AFB2B9200435C27
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY497024 Genomic DNA. Translation: AAS76668.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY497024 Genomic DNA. Translation: AAS76668.1 .

    3D structure databases

    ProteinModelPortali Q5J6J0.
    SMRi Q5J6J0. Positions 120-533.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S10.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view ]
    PANTHERi PTHR11802. PTHR11802. 1 hit.
    Pfami PF00450. Peptidase_S10. 1 hit.
    [Graphical view ]
    PRINTSi PR00724. CRBOXYPTASEC.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Trichophyton rubrum secreted and membrane-associated carboxypeptidases."
      Zaugg C., Jousson O., Lechenne B., Staib P., Monod M.
      Int. J. Med. Microbiol. 298:669-682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiCBPYA_TRIRU
    AccessioniPrimary (citable) accession number: Q5J6J0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 36 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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