CBPYA_PARBD
ID CBPYA_PARBD Reviewed; 550 AA.
AC C1GG77;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=CPYA; ORFNames=PADG_06314;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275964; EEH50235.1; -; Genomic_DNA.
DR RefSeq; XP_010761848.1; XM_010763546.1.
DR AlphaFoldDB; C1GG77; -.
DR SMR; C1GG77; -.
DR STRING; 121759.XP_010761848.1; -.
DR MEROPS; S10.001; -.
DR EnsemblFungi; EEH50235; EEH50235; PADG_06314.
DR GeneID; 22585067; -.
DR KEGG; pbn:PADG_06314; -.
DR VEuPathDB; FungiDB:PADG_06314; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR OMA; GDWMKPF; -.
DR Proteomes; UP000001628; 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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..131
FT /evidence="ECO:0000250"
FT /id="PRO_0000407463"
FT CHAIN 132..550
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407464"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 185..424
FT /evidence="ECO:0000250"
FT DISULFID 319..333
FT /evidence="ECO:0000250"
FT DISULFID 343..366
FT /evidence="ECO:0000250"
FT DISULFID 350..359
FT /evidence="ECO:0000250"
FT DISULFID 388..394
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 61910 MW; C9EBCE1DE53479AF CRC64;
MKSLVLGLLV GSAIASGPLQ HVLHAPPDPE PKPEPEPQVV KDPFEELRDT FDRLRNKAGD
IWDDVMDNIP NIMSNMRPLT IPAKKFTRRP DSEWTHIVRG ADLEALWVDD ESGYKHRKID
GKLSQYDLRI KAVDPSDLGI DKVKQYSGYL DDNANDKHLF FWFFESRNDP FGDPVVLWLN
GGPGCSSLTG MFFELGPASI DENITANYNP YSWNSNSSII FLDQPVNVGY SYSSQAVSDT
VTAAKDVYAL LTLFFTQFRQ YSAQDFHIAG ESYAGHYIPV FASEILHHNN TNINLQSVLI
GNGLTDPLSQ YPFYRPMACG DGGYPSVLDS QSCQSMDNAL PRCLSMIKSC YDIESTFTCL
PASIYCNNAL IGPYQKTGRN PYDVRTNCTG NDLCYPQLNY ITEYLNKPHV MRSLGVEVDS
YESCNMDINR NFLFHGDWMK PYHRLVPSLL ARIPVLIYAG DADFICNWLG NKAWTEALEY
PGHAKFAEAP MENLTMINSQ GKNEVFGEVK SHSNLTFMRI FKAGHMTPFD SPQASLEFAN
SWLSGEWSEV
