ID   CBPYA_TRITO             Reviewed;         543 AA.
AC   A5YCB8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; Synonyms=CarbY;
OS   Trichophyton tonsurans (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Abdel-Rahman S.M., Preuett B.L., Gaedigk A.;
RT   "Multi-locus genotyping identifies infections with multiple strains of T.
RT   tonsurans.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; EF490685; ABQ96589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5YCB8; -.
DR   SMR; A5YCB8; -.
DR   ESTHER; triru-q5j6j0; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   VEuPathDB; FungiDB:TESG_05174; -.
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; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407486"
FT   CHAIN           125..543
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407487"
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;  60739 MW;  EBBDFC83148B999F CRC64;
     MKFLTTGLLA TAALAAAQEQ QVLQAEDGMG QAPQRGSSIF DETLQKFQSS LEDGISHFWS
     EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW VQGADGEKRR EIDGKLHNYD
     LRVKAVDPSK LGVDAGVKQY SGYLDDNDAD KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
     SLTGLFLELG PATIDKNLKV VSNPYSWNSN ASVIFLDQPV NVGFSYSGSS VSDTVAAGKD
     IYALLTLFFK QFPEYATQDF HISGESYAGH YIPVFAAEIL SHKNTNINLK SALIGNGLTD
     PLTQYPQYRP MACGEGGYPA VLDQGTCRSM DNSLERCLSL IETCYSSESA WICVPAAMYC
     NSAILAPYQQ TGMNPYDVRN KCEDMASLCY PQLNVITEWL NQKSVMQALG VEVESYESCN
     SGINRDFLFH GDWMKPYHRL VPSVLEKIPV LIYAGDADFI CNWLGNQAWT DALEWPGHKK
     FAEAKLEDLK IVDNKNKGKK IGQVKSSGNF TFMRIFGAGH MVPLNQPEAS LEFLNRWLRG
     EWH