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P30574

- CBPY_CANAX

UniProt

P30574 - CBPY_CANAX

Protein

Carboxypeptidase Y

Gene

CPY1

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    • Comment

    Functioni

    Involved in degradation of small peptides.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei269 – 2691By similarity
    Active sitei461 – 4611By similarity
    Binding sitei464 – 4641SubstrateBy similarity
    Active sitei518 – 5181By similarity
    Binding sitei519 – 5191SubstrateBy similarity

    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 (EC:3.4.16.5)
    Alternative name(s):
    Carboxypeptidase YSCY
    Gene namesi
    Name:CPY1
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    Subcellular locationi

    Vacuole
    Note: Lysosome-like vacuoles.

    GO - Cellular componenti

    1. vacuole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 127106Sequence AnalysisPRO_0000004289Add
    BLAST
    Chaini128 – 542415Carboxypeptidase YPRO_0000004290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi182 ↔ 421By similarity
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi316 ↔ 330By similarity
    Disulfide bondi340 ↔ 363By similarity
    Disulfide bondi347 ↔ 356By similarity
    Disulfide bondi385 ↔ 391By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Inductioni

    Transiently down-regulated during the early events of yeast to hyphae conversion.

    Structurei

    3D structure databases

    ProteinModelPortaliP30574.
    SMRiP30574. Positions 132-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S10 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2939.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    IPR008442. Propeptide_carboxypepY.
    [Graphical view]
    PANTHERiPTHR11802. PTHR11802. 1 hit.
    PfamiPF05388. Carbpep_Y_N. 1 hit.
    PF00450. Peptidase_S10. 1 hit.
    [Graphical view]
    PRINTSiPR00724. CRBOXYPTASEC.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P30574-1 [UniParc]FASTAAdd to Basket

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    MKLSKSTLIA TLALTATSTN ALVVQNPFSN IQQALKLDLS YDKLTSKLTD    50
    TFEQGKANII STIAKVMNEP LDGLTPEIKN IWSEMLMKFP NSITELNFKA 100
    PPKKGKITTQ QFDFHVTDAQ VPNHKLRIKS TPKDLGIDTV KQYSGYLDVV 150
    DEDKHFFYYF FESRNDPKND PVILWLNGGP GCSSLTGLFF ELGPSSIDKN 200
    LKPVYNPHSW NANASVIFLD QPINVGYSYS SQSVSNTIAA GKDVYAFLQL 250
    FFKNFPEYAN LDFHIAGESY AGHYIPAFAS EILTHPERNF NLTSVLIGNG 300
    LTDPLVQYEY YEPMACGEGG EPSVLEPEEC DGMLNSLPRC LSLIESCYES 350
    GSVWSCVPAT IYCNNGQMGP YQKTGRNVYD IRTMCEGSSL CYSQLEYIDQ 400
    YLNLPEVKKA LGAEVDEYQS CNFDINRNFM FAGDWMKPYQ KNVIDLLEKE 450
    LPVLIYAGDK DFICNWLGNQ AWTNRLEWSG SKGFTKAPVK SWKVGKNAAG 500
    EVKNYKHFTF LRVFGGGHMV PYDQPENALD MVNRWISGDY KY 542
    Length:542
    Mass (Da):61,044
    Last modified:November 1, 1995 - v2
    Checksum:i7FA6B9F82F9D44AF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95182 Genomic DNA. Translation: AAA34326.2.
    PIRiJC1380.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95182 Genomic DNA. Translation: AAA34326.2 .
    PIRi JC1380.

    3D structure databases

    ProteinModelPortali P30574.
    SMRi P30574. Positions 132-540.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S10.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG2939.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    IPR008442. Propeptide_carboxypepY.
    [Graphical view ]
    PANTHERi PTHR11802. PTHR11802. 1 hit.
    Pfami PF05388. Carbpep_Y_N. 1 hit.
    PF00450. Peptidase_S10. 1 hit.
    [Graphical view ]
    PRINTSi PR00724. CRBOXYPTASEC.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The carboxypeptidase Y-encoding gene from Candida albicans and its transcription during yeast-to-hyphae conversion."
      Mukhtar M., Logan D.A., Kaufer N.F.
      Gene 121:173-177(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiCBPY_CANAX
    AccessioniPrimary (citable) accession number: P30574
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 82 of the entry and version 2 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