CBPYA_ARTGP
ID CBPYA_ARTGP Reviewed; 543 AA.
AC E4USS9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=CPYA; ORFNames=MGYG_03599;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989824; EFR00594.1; -; Genomic_DNA.
DR RefSeq; XP_003173424.1; XM_003173376.1.
DR AlphaFoldDB; E4USS9; -.
DR SMR; E4USS9; -.
DR STRING; 63402.XP_003173424.1; -.
DR ESTHER; triru-q5j6j0; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR EnsemblFungi; EFR00594; EFR00594; MGYG_03599.
DR GeneID; 10028703; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; E4USS9; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000002669; 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; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 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..124
FT /evidence="ECO:0000250"
FT /id="PRO_0000407426"
FT CHAIN 125..543
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407427"
FT ACT_SITE 266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 179..419
FT /evidence="ECO:0000250"
FT DISULFID 313..327
FT /evidence="ECO:0000250"
FT DISULFID 337..360
FT /evidence="ECO:0000250"
FT DISULFID 344..353
FT /evidence="ECO:0000250"
FT DISULFID 382..389
FT /evidence="ECO:0000250"
SQ SEQUENCE 543 AA; 60846 MW; 01C8974ABAEC31F3 CRC64;
MKLLTTGLLA SAALVAAQEQ QVLRADEVFG KAPLPDASIF DETIKQFQSS IEDGISHFWS
EMKTNFKDYL PMISLPKKHN RRPDSEWDHV VRGADVESVW VQGADGEKRR EIDGKLKNYD
LRVKSVDPSQ LGIDPGVKQY SGYLDDNDAD KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
SLTGLFLELG PATIDKNLKV VHNPYSWNSN ASVIFLDQPV NVGFSYSGSS VSDTVAAGKD
VYALLTLFFK QFPEYATQDF HISGESYAGH YIPVFAAEIL SHKNTNINLK SALIGNGLTD
PLTQYPHYRP MACGDGGYPA VLDQGTCRSM DNSLERCLSL IETCYSSESA WVCVPAAMYC
NSAILAPYQQ TGMNPYDVRS KCEDMGSLCY PQLNAITEWL NQKSVMKALG VEVESYESCN
SGINRDFLFH GDWMKPFHRL VPSVLEKIPV LIYAGDADFI CNWLGNQAWT EALEWPGHKK
FTEAKLQDLK IVDNKNKGKK IGQVKSSGNF TFMRIFGAGH MVPLNQPEAS LEFFNRWLRG
EWH