ID   CBPYA_TRIRU             Reviewed;         536 AA.
AC   Q5J6J0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; Synonyms=ScpC;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18222721; DOI=10.1016/j.ijmm.2007.11.005;
RA   Zaugg C., Jousson O., Lechenne B., Staib P., Monod M.;
RT   "Trichophyton rubrum secreted and membrane-associated carboxypeptidases.";
RL   Int. J. Med. Microbiol. 298:669-682(2008).
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; AY497024; AAS76668.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5J6J0; -.
DR   SMR; Q5J6J0; -.
DR   ESTHER; triru-q5j6j0; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; Q5J6J0; 2 sites, No reported glycans.
DR   VEuPathDB; FungiDB:TERG_08255; -.
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   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407484"
FT   CHAIN           125..536
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407485"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        451
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        172..412
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..320
FT                   /evidence="ECO:0000250"
FT   DISULFID        330..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..346
FT                   /evidence="ECO:0000250"
FT   DISULFID        375..382
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   536 AA;  60099 MW;  0AFB2B9200435C27 CRC64;
     MKFFTTGLLA TAALAAAQEQ QVLQAEDGMG RAPLPDSSIF DETLQKFQSS LEDGISHFWS
     EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW VQGADGEKRR EIDGKLHNYD
     LRVKAVDPGV KQYSGYLDDN DADKHLFYWF FESRNDPKND PVVLWLNGGP GCSSLTGLFL
     ELGPATIDKN LKVVSNPYSW NSNASVIFLD QPVNVGFSYS GSSVSDTVAA GKDVYALLTL
     FFKQFPEYAT QDFHISGESY AGHYIPVFAA EILSHKNTNI NLKSALIGNG LTDPLTQYPQ
     YRPMACGEGG YPAVLDQGTC RSMDNSLERC LSLIETCYSS ESAWVCVPAA MYCNSAILAP
     YQQTGMNPYD VRTKCEDMAS LCYPQLNAIT EWLNQKPVMQ ALGVEVESYE SCNSGINRDF
     LFHGDWMKPY HRLVPSVLEK IPVLIYAGDA DFICNWLGNK AWTEALEWPG HKKFAETKLE
     DLKIVDNKNK GKKIGQVKSS GNFTFMRIFG AGHMVPLNQP EASLEFLNRW LRGEWH
//