ID   CBPYA_PHANO             Reviewed;         543 AA.
AC   Q0V1R1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=SNOG_02053;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445327; EAT90265.1; -; Genomic_DNA.
DR   RefSeq; XP_001792672.1; XM_001792620.1.
DR   AlphaFoldDB; Q0V1R1; -.
DR   SMR; Q0V1R1; -.
DR   STRING; 13684.SNOT_02053; -.
DR   MEROPS; S10.001; -.
DR   PRIDE; Q0V1R1; -.
DR   EnsemblFungi; SNOT_02053; SNOT_02053; SNOG_02053.
DR   GeneID; 5969522; -.
DR   KEGG; pno:SNOG_02053; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; Q0V1R1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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..128
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407470"
FT   CHAIN           129..543
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407471"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        519
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        182..421
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..330
FT                   /evidence="ECO:0000250"
FT   DISULFID        340..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..356
FT                   /evidence="ECO:0000250"
FT   DISULFID        385..391
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   543 AA;  61071 MW;  67C6C4D765B7D11B CRC64;
     MRVAASALLA GAASAAVAPQ QQILKFPSSF SELKEDLWSK PLHNLEESLK SLTGEAKATW
     DEVATMYPES FDKAAFFSTP KPHTRKHDSE WDHIVKGADV QSVWVENAQG EKEREIDGKL
     EQFDLRVKKV DPSVLGVDKV KQYSGYLDDN EEDKHLFYWF FESRNDPKND PVVLWLNGGP
     GCSSLMGLFM ELGPASVMKD GKLKHNDYSW NANASVIFLD QPVNVGYSYS SGSVSNTVAA
     GKDIYALLTL FFKQFPEYSK QPFHISGESY AGHYIPVFAS EILSHKKRNI NLQSVLIGNG
     LTDGLTQYEY YRPMACGEGG WPAVLDESSC QAMDNAYPRC ASLIENCYKS ESVWSCVPAS
     IYCNNAMIGP YQRTGQNVYD VRRPCGDNQL CYDEIDYISA FLNKKEVMKA VGAEVSSYDS
     CNFDINRNFL LQGDWMKPYH RVVPGLLEEI PVLVYAGDAD YICNWLGNKA WTEALEWKGH
     EEYKKAEMKD FKIDGDGKKV GEVKSSGNFT FMKIHAGGHM VPFDQPEASL EMVNRWLSGE
     FWE