ID   CBPYA_PENRW             Reviewed;         550 AA.
AC   B6HPP6;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=Pc22g00890;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(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; AM920437; CAP97377.1; -; Genomic_DNA.
DR   RefSeq; XP_002564134.1; XM_002564088.1.
DR   AlphaFoldDB; B6HPP6; -.
DR   SMR; B6HPP6; -.
DR   STRING; 1108849.XP_002564134.1; -.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; CAP97377; CAP97377; PCH_Pc22g00890.
DR   GeneID; 8306581; -.
DR   KEGG; pcs:Pc22g00890; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g00890; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   BioCyc; PCHR:PC22G00890-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
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; IPR008442; Propeptide_carboxypepY.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 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..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..131
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407467"
FT   CHAIN           132..550
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_5000410069"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        465
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        527
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        516
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        186..426
FT                   /evidence="ECO:0000250"
FT   DISULFID        320..334
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..367
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        389..396
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  61428 MW;  8542765BCFB51BE1 CRC64;
     MRVLSATLLA GAASAAAPPF QQVLGAHKEY AENVIQQGAD AFKPLQHLQD QFKSLSGEAR
     QLWEEVSNYF PESMESAPLL SLPKKHTRRP DSHWDYHVSG AEVQDIWVSG AEGTKEREVD
     GRLEAYNLRA KKVDPSALGI DPGVKQYSGY LDDDENDKHL FYWFFESRND PKNDPVVLWL
     NGGPGCSSLT GLFMELGPSS IDSKIKPVYN DFSWNNNASV IFLDQPINVG YSYSGGSVSD
     TVAAGKDVYA LLTLFFKQFP EYATQDFHIA GESYAGHYIP VMASEILSHK KRNINLKSVL
     IGNGLTDGLT QYGYYRPMAC GEGGYPAVLD ESTCQSMDNS LSRCQSMIQA CYNSESPWVC
     VPASIYCNNA MLGPYQRTGQ NVYDIRGKCE DESNLCYKGM GYVSEYLGQE SVREAVGAEV
     DGYDSCNFDI NRNFLFNGDW FKPYHRLVPG LLEQIPVLIY AGDADFICNW LGNKAWSEAL
     EWPGQKEFAS AELEDLKIVQ NEHVGKKIGQ IKSHGNFTFM RIYGGGHMVP MDQPESGLEF
     FNRWIGGEWF