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Q2TYA1

- CBPYA_ASPOR

UniProt

Q2TYA1 - CBPYA_ASPOR

Protein

Carboxypeptidase Y homolog A

Gene

cpyA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (24 Jan 2006)
      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 sitei265 – 2651PROSITE-ProRule annotation
    Active sitei457 – 4571PROSITE-ProRule annotation
    Active sitei519 – 5191PROSITE-ProRule annotation

    GO - Molecular functioni

    1. serine-type carboxypeptidase activity Source: ASPGD

    GO - Biological processi

    1. proteolysis Source: ASPGD

    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
    ORF Names:AO090103000332
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 8

    Subcellular locationi

    Vacuole 3 Publications
    Note: Requires vps10 for correct vacuolar localization.

    GO - Cellular componenti

    1. fungal-type vacuole lumen Source: UniProtKB

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 123106By similarityPRO_0000407437Add
    BLAST
    Chaini124 – 542419Carboxypeptidase Y homolog APRO_0000407438Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi178 ↔ 418By similarity
    Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi312 ↔ 326By similarity
    Disulfide bondi336 ↔ 359By similarity
    Disulfide bondi343 ↔ 352By similarity
    Disulfide bondi381 ↔ 388By similarity
    Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Interactioni

    Protein-protein interaction databases

    STRINGi5062.CADAORAP00010017.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2TYA1.
    SMRiQ2TYA1. Positions 123-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S10 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2939.
    HOGENOMiHOG000198296.
    KOiK13289.
    OMAiWPGQKEY.
    OrthoDBiEOG7XDBR1.

    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.
    PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q2TYA1-1 [UniParc]FASTAAdd to Basket

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    MRVLPATLLV GAASAAVPPL QQVLGRPEEG MSFSKPLHAF QEQLKTLSED    50
    ARKLWDEVAN YFPDSMDHSP IFSLPKKHTR RPDSHWDHIV RGSDVQKIWV 100
    NNADGEKERE IDGKLEAYDL RIKKADPSAL GIDPNVKQYT GYLDDNGNDK 150
    HLFYWFFESR NDPKNDPVVL WLNGGPGCSS LTGLFMELGP SSIDENIKPV 200
    YNDFSWNSNA SVIFLDQPVN VGYSYSGSAV SDTVAAGKDV YALLSLFFKQ 250
    FPEYAEQDFH IAGESYAGHY IPVFASEILA HKNRNINLKS VLIGNGLTDG 300
    LTQYGYYRPM GCGEGGYKAV LDEATCESMD NALPRCRSMI ESCYNSESAW 350
    VCVPASIYCN NALIGPYQRT GQNVYDVRSK CEDESNLCYK GMGYVSEYLN 400
    KAEVREAVGA EVGGYDSCNF DINRNFLFHG DWMKPYHRLV PGLLEQIPVL 450
    IYAGDADYIC NWLGNKAWTE ALEWPGQKEY ASAELEDLKI EQNEHTGKKI 500
    GQVKSHGNFT FMRLYGGGHM VPMDQPEASL EFFNRWLGGE WF 542
    Length:542
    Mass (Da):60,892
    Last modified:January 24, 2006 - v1
    Checksum:iBD339D3954E9EB3A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007174 Genomic DNA. Translation: BAE65772.1.
    RefSeqiXP_001826905.1. XM_001826853.2.

    Genome annotation databases

    EnsemblFungiiCADAORAT00010224; CADAORAP00010017; CADAORAG00010224.
    GeneIDi5999027.
    KEGGiaor:AOR_1_542034.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP007174 Genomic DNA. Translation: BAE65772.1 .
    RefSeqi XP_001826905.1. XM_001826853.2.

    3D structure databases

    ProteinModelPortali Q2TYA1.
    SMRi Q2TYA1. Positions 123-539.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5062.CADAORAP00010017.

    Protein family/group databases

    MEROPSi S10.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00010224 ; CADAORAP00010017 ; CADAORAG00010224 .
    GeneIDi 5999027.
    KEGGi aor:AOR_1_542034.

    Phylogenomic databases

    eggNOGi COG2939.
    HOGENOMi HOG000198296.
    KOi K13289.
    OMAi WPGQKEY.
    OrthoDBi EOG7XDBR1.

    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 PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.
    2. "Visualization of vacuoles in Aspergillus oryzae by expression of CPY-EGFP."
      Ohneda M., Arioka M., Nakajima H., Kitamoto K.
      Fungal Genet. Biol. 37:29-38(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    3. "Isolation and characterization of Aspergillus oryzae vacuolar protein sorting mutants."
      Ohneda M., Arioka M., Kitamoto K.
      Appl. Environ. Microbiol. 71:4856-4861(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    4. "Enhanced production and secretion of heterologous proteins by the filamentous fungus Aspergillus oryzae via disruption of vacuolar protein sorting receptor gene Aovps10."
      Yoon J., Aishan T., Maruyama J., Kitamoto K.
      Appl. Environ. Microbiol. 76:5718-5727(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiCBPYA_ASPOR
    AccessioniPrimary (citable) accession number: Q2TYA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 3, 2011
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 50 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, Reference 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