ID   CBPYA_PYRTR             Reviewed;         541 AA.
AC   B2WKF1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=PTRG_10461;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231628; EDU43511.1; -; Genomic_DNA.
DR   RefSeq; XP_001940792.1; XM_001940757.1.
DR   AlphaFoldDB; B2WKF1; -.
DR   SMR; B2WKF1; -.
DR   STRING; 45151.EDU43511; -.
DR   ESTHER; pyrtr-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EDU43511; EDU43511; PTRG_10461.
DR   GeneID; 6348766; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; B2WKF1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000001471; Unassembled 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; 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..125
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407474"
FT   CHAIN           126..541
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407475"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        179..418
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..388
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   541 AA;  60888 MW;  C6380578F2E78391 CRC64;
     MKVATSALLI GAAAAQQQQI LKFPDSFSEL KESSWTKPLQ NLEESLKSLT GEARATWDEI
     AMMFPESFEK AAFFSEPKPH TRKQDSEWDH IIKGADIQSV WVENEKGEKE REIDGKLEQY
     SLRAKKVDPS VLGVDKVKQY SGYLDDEEED KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
     SLTGLFMELG PASITKDQKI KHNPYSWNSN ASVIFLDQPV NVGYSYSSGS VSNTVAAGKD
     IYALLTLFFK QFPEYSHQSF HISGESYAGH YIPVFASEIL SHKNRNINLQ SVLIGNGLTD
     GLTQYEYYRP MACGEGGWPA VLDESQCKAM DNAYPRCASL IENCYNSESV WSCVPASIYC
     NNAMIGPYQR TGQNVYDVRK PCGSNSLCYD ELDWIQGYLN KKEVMKAVGA EVSNYESCNF
     DINRNFLLQG DWMKPFHRVV PGILEKIPVL IYAGDADYIC NWLGNKAWTE ALEWPGAKAY
     NQAKMEDFKI DGDGKTVGQV KSSGNFTFMR LHAGGHMVPY DQPEASLEML NRWLGGGFWK
     A