CBPYA_COCP7
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 03-AUG-2022, entry version 56.
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}.
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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 EnsemblFungi; EER28915; EER28915; CPC735_036210.
DR GeneID; 9696555; -.
DR KEGG; cpw:CPC735_036210; -.
DR VEuPathDB; FungiDB:CPC735_036210; -.
DR HOGENOM; CLU_008523_10_4_1; -.
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; 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 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