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A5YCB8

- CBPYA_TRITO

UniProt

A5YCB8 - CBPYA_TRITO

Protein

Carboxypeptidase Y homolog A

Gene

CPYA

Organism
Trichophyton tonsurans (Scalp ringworm fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 24 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      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 sitei266 – 2661PROSITE-ProRule annotation
    Active sitei458 – 4581PROSITE-ProRule annotation
    Active sitei520 – 5201PROSITE-ProRule annotation

    GO - Molecular functioni

    1. serine-type carboxypeptidase activity Source: InterPro

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Protease

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase Y homolog A (EC:3.4.16.5)
    Gene namesi
    Name:CPYA
    Synonyms:CarbY
    OrganismiTrichophyton tonsurans (Scalp ringworm fungus)
    Taxonomic identifieri34387 [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_0000407486Add
    BLAST
    Chaini125 – 543419Carboxypeptidase Y homolog APRO_0000407487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi179 ↔ 419By similarity
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi313 ↔ 327By similarity
    Disulfide bondi337 ↔ 360By similarity
    Disulfide bondi344 ↔ 353By similarity
    Disulfide bondi382 ↔ 389By similarity
    Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliA5YCB8.
    SMRiA5YCB8. Positions 124-540.
    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.

    A5YCB8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFLTTGLLA TAALAAAQEQ QVLQAEDGMG QAPQRGSSIF DETLQKFQSS    50
    LEDGISHFWS EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW 100
    VQGADGEKRR EIDGKLHNYD LRVKAVDPSK LGVDAGVKQY SGYLDDNDAD 150
    KHLFYWFFES RNDPKNDPVV LWLNGGPGCS SLTGLFLELG PATIDKNLKV 200
    VSNPYSWNSN ASVIFLDQPV NVGFSYSGSS VSDTVAAGKD IYALLTLFFK 250
    QFPEYATQDF HISGESYAGH YIPVFAAEIL SHKNTNINLK SALIGNGLTD 300
    PLTQYPQYRP MACGEGGYPA VLDQGTCRSM DNSLERCLSL IETCYSSESA 350
    WICVPAAMYC NSAILAPYQQ TGMNPYDVRN KCEDMASLCY PQLNVITEWL 400
    NQKSVMQALG VEVESYESCN SGINRDFLFH GDWMKPYHRL VPSVLEKIPV 450
    LIYAGDADFI CNWLGNQAWT DALEWPGHKK FAEAKLEDLK IVDNKNKGKK 500
    IGQVKSSGNF TFMRIFGAGH MVPLNQPEAS LEFLNRWLRG EWH 543
    Length:543
    Mass (Da):60,739
    Last modified:July 10, 2007 - v1
    Checksum:iEBBDFC83148B999F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF490685 Genomic DNA. Translation: ABQ96589.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF490685 Genomic DNA. Translation: ABQ96589.1 .

    3D structure databases

    ProteinModelPortali A5YCB8.
    SMRi A5YCB8. Positions 124-540.
    ModBasei Search...
    MobiDBi Search...

    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. "Multi-locus genotyping identifies infections with multiple strains of T. tonsurans."
      Abdel-Rahman S.M., Preuett B.L., Gaedigk A.
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiCBPYA_TRITO
    AccessioniPrimary (citable) accession number: A5YCB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 24 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