ID   CBPYA_ARTOC             Reviewed;         541 AA.
AC   C5FWJ1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=MCYG_07094;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
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}.
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DR   EMBL; DS995706; EEQ34275.1; -; Genomic_DNA.
DR   RefSeq; XP_002845130.1; XM_002845084.1.
DR   AlphaFoldDB; C5FWJ1; -.
DR   SMR; C5FWJ1; -.
DR   STRING; 554155.C5FWJ1; -.
DR   ESTHER; artoc-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; C5FWJ1; 2 sites, No reported glycans.
DR   GeneID; 9228162; -.
DR   VEuPathDB; FungiDB:MCYG_07094; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000002035; 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..122
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407428"
FT   CHAIN           123..541
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407429"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        518
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        177..417
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..358
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..351
FT                   /evidence="ECO:0000250"
FT   DISULFID        380..387
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   541 AA;  60467 MW;  5AC030C02D6B5BE1 CRC64;
     MKLLMTGLLA SAAVAAAQEQ QVLQAEGSAQ QQPAPSIFDE TLKQFESGLE EGITHFWSEM
     KTNFKHYLPL ISVPKEHTRR ADSEWDHVVR GADVESVWVQ GANGEKHREI DGKLQSYDLR
     VKAVDPAELG IDPGVKQYSG YLDDNETDKH LFYWFFESRN DPKNDPVVLW LNGGPGCSSL
     TGLFLELGPA TIDKNLKIVP NPYSWNSNAS VIFLDQPVNV GFSYSGSSVS DTVAAGKDIY
     ALLTLFFKQF PEYATQDFHI SGESYAGHYI PVFASEILSH KNTNINLKSV LIGNGLTDPL
     TQYPQYRPMA CGDGGYPAVL DQGTCRSMDN SLERCLSLIE TCYSSESAWV CVPAAMYCNS
     AIIGPYQQTG MNPYDVRSKC EDMSSLCYPQ LNTITEWLNQ KSVMKALGVE VESYESCNGG
     INRDFLFHGD WMKPYHRLVP SLLEKIPVLI YAGDADFICN WLGNLAWTNA LEWPGHKKFA
     DAKMNDLKIV DNKSKGKKIG QVKSSGNFTF MRIFGAGHMV PLNQPEASLE FFNRWLRGEW
     R
//