ID   CBPYA_COCP7             Reviewed;         539 AA.
AC   C5P212; Q3HYC0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=CPC735_036210;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=16369008; DOI=10.1128/iai.74.1.516-527.2006;
RA   Tarcha E.J., Basrur V., Hung C.Y., Gardner M.J., Cole G.T.;
RT   "A recombinant aspartyl protease of Coccidioides posadasii induces
RT   protection against pulmonary coccidioidomycosis in mice.";
RL   Infect. Immun. 74:516-527(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; DQ176864; ABA54912.1; -; Genomic_DNA.
DR   EMBL; ACFW01000012; EER28915.1; -; Genomic_DNA.
DR   RefSeq; XP_003071060.1; XM_003071014.1.
DR   AlphaFoldDB; C5P212; -.
DR   SMR; C5P212; -.
DR   ESTHER; cocpo-q3hyc0; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; C5P212; 2 sites, No reported glycans.
DR   GeneID; 9696555; -.
DR   KEGG; cpw:CPC735_036210; -.
DR   VEuPathDB; FungiDB:CPC735_036210; -.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000009084; 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   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..122
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407445"
FT   CHAIN           123..539
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407446"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        455
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        517
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        176..416
FT                   /evidence="ECO:0000250"
FT   DISULFID        310..324
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..357
FT                   /evidence="ECO:0000250"
FT   DISULFID        341..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        379..386
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   539 AA;  60311 MW;  A801B5BA731EAE37 CRC64;
     MKALTATLLV GTALAAVPPQ QPIQVPTEDS AWAKPLENLK DTFKTLGNDA KQAWNELASA
     FPDAINEYTL FSAPKKHTRR PDTHWDHIVR GSDVQSIWVE GADGQKRREV DGKLEKYDLR
     VKAVDPSKLG IDKVKQYSGY LDDKENDKHL FYWFFESRND PKNDPVVLWL NGGPGCSSLT
     GLFLELGPAS IDKNLKVVHN PYSWNSNASV IFLDQPVNVG FSYSGGSVSD TIAAGKDVYA
     LLTLFFKQFP QYATQDFHIA GESYAGHYIP VFASEILSHK NRNINLQSVL IGNGLTDPLT
     QYPHYRPMAC GEGGYPAVLD ESTCRSMDNS LPRCLSMIES CYSSESAWLC VPASIYCNNA
     MIGPYQRTGQ NPYDVRAKCE DGGSLCYSQL GYITEWLNQK SVMDALGVEV SSYDSCNMDI
     NRNFLFHGDW MKPFHRVVPG LIDQIRVLIY AGDADFICNW LGNQAWTDAL EWSGREKFAK
     AELKDLTIVD NENKGKNIGK VKSYGNFTFM RLFGGGHMVP LDQPEASLEF FNRWLGGEW
//