CBPYA_PODAN
ID CBPYA_PODAN Reviewed; 554 AA.
AC B2AWD5; A0A090CWP9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=CPYA; OrderedLocusNames=Pa_7_6790; ORFNames=PODANS_7_6790;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU633900; CAP68709.1; -; Genomic_DNA.
DR EMBL; FO904942; CDP32179.1; -; Genomic_DNA.
DR RefSeq; XP_001908036.1; XM_001908001.1.
DR AlphaFoldDB; B2AWD5; -.
DR SMR; B2AWD5; -.
DR STRING; 5145.XP_001908036.1; -.
DR MEROPS; S10.001; -.
DR PRIDE; B2AWD5; -.
DR EnsemblFungi; CAP68709; CAP68709; PODANS_7_6790.
DR GeneID; 6192366; -.
DR KEGG; pan:PODANSg5071; -.
DR VEuPathDB; FungiDB:PODANS_7_6790; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000001197; Chromosome 7.
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..137
FT /evidence="ECO:0000250"
FT /id="PRO_0000407472"
FT CHAIN 138..554
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407473"
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; 61984 MW; 7CD452763862547D CRC64;
MRVAASTVLL GVASAASFQQ QTQHVLSSGY ERAQAGMKPL AEQFVDAAGK PIANIEEAFH
GMTAEVKALW DEIKLLVPES AFNHSNWFTK PKPARRRHDW DHVVKGADVQ KLWVQGESGE
DHRQVDGKLA DFNLRVKAVD PSKLGVDKVK QYSGYLDDEA NDKHLFYWFF ESRNDPKNDP
VVLWLNGGPG CSSLTGLFLE LGPSSIDKKL KVVNNEFSWN NNASVIFLDQ PVNVGYSYSG
NSVSNTIAAG KDVYALLSLF FHQFPEYAKQ DFHIAGESYA GHYIPVFASE ILSHKNRNIN
LKSILIGNGL TDGLTQYEHY RPMACGKGGY PAVLDESECR SMDNALPRCQ SLIQNCYDSG
SVWSCVPASI YCNNALIGPY QRTGQNVYDI RGKCEDSSNL CYSALGWISD YLNQQDVMDA
LGVEVSGYES CNFDINRNFL FQGDWMQPFH RLVPNILKEI PVLIYAGDAD YICNWLGNQA
WTEALEWPGK KNFNKASIKD LKLAGAEKEY GKVKASGNFT FMQVYQAGHM VPMDQPENSL
DFLNRWLGGE WFAK
