ID   CBPYA_ARTGP             Reviewed;         543 AA.
AC   E4USS9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=MGYG_03599;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Vacuolar carboxypeptidase involved in degradation of small
CC       peptides. Digests preferentially peptides containing an aliphatic or
CC       hydrophobic residue in P1' position, as well as methionine, leucine or
CC       phenylalanine in P1 position of ester substrate (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS989824; EFR00594.1; -; Genomic_DNA.
DR   RefSeq; XP_003173424.1; XM_003173376.1.
DR   AlphaFoldDB; E4USS9; -.
DR   SMR; E4USS9; -.
DR   STRING; 535722.E4USS9; -.
DR   ESTHER; triru-q5j6j0; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; E4USS9; 2 sites, No reported glycans.
DR   GeneID; 10028703; -.
DR   VEuPathDB; FungiDB:MGYG_03599; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; E4USS9; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407426"
FT   CHAIN           125..543
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407427"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        520
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        179..419
FT                   /evidence="ECO:0000250"
FT   DISULFID        313..327
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        382..389
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   543 AA;  60846 MW;  01C8974ABAEC31F3 CRC64;
     MKLLTTGLLA SAALVAAQEQ QVLRADEVFG KAPLPDASIF DETIKQFQSS IEDGISHFWS
     EMKTNFKDYL PMISLPKKHN RRPDSEWDHV VRGADVESVW VQGADGEKRR EIDGKLKNYD
     LRVKSVDPSQ LGIDPGVKQY SGYLDDNDAD KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
     SLTGLFLELG PATIDKNLKV VHNPYSWNSN ASVIFLDQPV NVGFSYSGSS VSDTVAAGKD
     VYALLTLFFK QFPEYATQDF HISGESYAGH YIPVFAAEIL SHKNTNINLK SALIGNGLTD
     PLTQYPHYRP MACGDGGYPA VLDQGTCRSM DNSLERCLSL IETCYSSESA WVCVPAAMYC
     NSAILAPYQQ TGMNPYDVRS KCEDMGSLCY PQLNAITEWL NQKSVMKALG VEVESYESCN
     SGINRDFLFH GDWMKPFHRL VPSVLEKIPV LIYAGDADFI CNWLGNQAWT EALEWPGHKK
     FTEAKLQDLK IVDNKNKGKK IGQVKSSGNF TFMRIFGAGH MVPLNQPEAS LEFFNRWLRG
     EWH
//