ID   CBPYA_CHAGB             Reviewed;         554 AA.
AC   Q2H9G6;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=CHGG_03138;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ91203.1; -; Genomic_DNA.
DR   RefSeq; XP_001229654.1; XM_001229653.1.
DR   AlphaFoldDB; Q2H9G6; -.
DR   SMR; Q2H9G6; -.
DR   STRING; 306901.Q2H9G6; -.
DR   ESTHER; chagb-q2h9g6; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; Q2H9G6; 2 sites, No reported glycans.
DR   GeneID; 4389770; -.
DR   VEuPathDB; FungiDB:CHGG_03138; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; Q2H9G6; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000001056; 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; 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; IPR008442; Propeptide_carboxypepY.
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; PF05388; Carbpep_Y_N; 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   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..137
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407443"
FT   CHAIN           138..554
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407444"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        529
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        191..431
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..339
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..372
FT                   /evidence="ECO:0000250"
FT   DISULFID        356..365
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..401
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  61851 MW;  7D613BD299241E48 CRC64;
     MRIAASTVLF GAASAASFQQ QAQHVLSGGF GKAQEAMKPI SDAFTDAAGR PFESFEDAFS
     GMTAETKALW EEIKLLVPDS AFKDLSWLSK PKPHHRRDDW NHVVKGADVQ GMWVQDANGK
     SHRQVDGRLE EYNLRVKAVD PSKLNVDSVK QYSGYLDDEA NDKHLFYWFF ESRNDPKNDP
     VILWLNGGPG CSSLTGLFLE LGPSSIDKTL KVVNNDFSWN NNASVIFLDQ PVNVGYSYSG
     SSVSNTVAAG KDVYALLTLF FHQFPEYAKQ DFHIAGESYA GHYIPVFASE ILAHKNRNIN
     LKSVLIGNGL TDGLTQYEHY RPMACGEGGY PAVLGEAECR SMDNALPRCQ SLINNCYESG
     SVWSCVPASI YCNNAMIGPY QRTGRNVYDI RGPCEDSSNL CYSGLGYISD YLNQQSVMDA
     LGVEVSSYDS CNFDINRNFL FQGDWMQPFH RLVPKILEEI PVLIYAGDAD YICNWLGNRA
     WTEALEWPGK KDFNAAKVKD LKLSGAEKEY GKVKASGNFT FMQVYQAGHM VPMDQPENSL
     DFLNRWLNGE WFAK
//