ID   CBPYA_PARBA             Reviewed;         550 AA.
AC   C1GXD8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=PAAG_03512;
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293998; EEH41226.1; -; Genomic_DNA.
DR   RefSeq; XP_002794967.1; XM_002794921.2.
DR   AlphaFoldDB; C1GXD8; -.
DR   SMR; C1GXD8; -.
DR   STRING; 502779.C1GXD8; -.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EEH41226; EEH41226; PAAG_03512.
DR   GeneID; 9098180; -.
DR   KEGG; pbl:PAAG_03512; -.
DR   VEuPathDB; FungiDB:PAAG_03512; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000002059; Partially assembled 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; 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   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..131
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407461"
FT   CHAIN           132..550
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407462"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        463
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        525
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        185..424
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..333
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..366
FT                   /evidence="ECO:0000250"
FT   DISULFID        350..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        388..394
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  62138 MW;  8DE428F1D18102CB CRC64;
     MKSLVLGLLV GSAIASGPLQ HVLHAPPEPE PEPEPEPQVV KDPFEELRDT FDRLRNKAGD
     IWDDVMDNIP NIISNIRPPT IPPKKFTRLP DSEWTHIVRG ADLEALWVDD ESGYKHRKVD
     GKLAQYDLRI RAVDPSNLGI DNVKQYSGYL DDNLNDKHLF YWFFESRNDP DGDPVMLWLN
     GGPGCSSLTG MFFELGPSSI TEDIKVKYNP YSWNSNSSII FLDQPVNVGF SYSSQPVSDT
     VAAAKDIYAL LTLFFTQFPQ YSTQDFHIAG ESYAGHYIPV IASEIMHHKD RNINLQSVMI
     GNGLTDPYTQ YPLYRPMACG EGGYPNVLDS ETCRSMDKAL PRCLSMIKSC YDVESTFTCL
     PASIYCNNAL IGPYQSTGRN PYDVRIDCKG NGLCYPQLNY ITDYLNQPYV MKSLGVEVDS
     YESCNMDINR NFLLHGDWMK PYHRLVPYLL AQMPVLIYAG DADFICNWLG NKAWTEALEY
     PGHTKYAQSP MENLTMVNSE GINEIFGEVK SHSNLTFMRI FKAGHMTPFD TPQASLEFAN
     SWLSGEWSEV