CBPYA_ARTOC
ID CBPYA_ARTOC Reviewed; 541 AA.
AC C5FWJ1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-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=MCYG_07094;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
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; DS995706; EEQ34275.1; -; Genomic_DNA.
DR RefSeq; XP_002845130.1; XM_002845084.1.
DR AlphaFoldDB; C5FWJ1; -.
DR SMR; C5FWJ1; -.
DR STRING; 63405.XP_002845130.1; -.
DR MEROPS; S10.001; -.
DR PRIDE; C5FWJ1; -.
DR EnsemblFungi; EEQ34275; EEQ34275; MCYG_07094.
DR GeneID; 9228162; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000002035; 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..122
FT /evidence="ECO:0000250"
FT /id="PRO_0000407428"
FT CHAIN 123..541
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407429"
FT ACT_SITE 264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..417
FT /evidence="ECO:0000250"
FT DISULFID 311..325
FT /evidence="ECO:0000250"
FT DISULFID 335..358
FT /evidence="ECO:0000250"
FT DISULFID 342..351
FT /evidence="ECO:0000250"
FT DISULFID 380..387
FT /evidence="ECO:0000250"
SQ SEQUENCE 541 AA; 60467 MW; 5AC030C02D6B5BE1 CRC64;
MKLLMTGLLA SAAVAAAQEQ QVLQAEGSAQ QQPAPSIFDE TLKQFESGLE EGITHFWSEM
KTNFKHYLPL ISVPKEHTRR ADSEWDHVVR GADVESVWVQ GANGEKHREI DGKLQSYDLR
VKAVDPAELG IDPGVKQYSG YLDDNETDKH LFYWFFESRN DPKNDPVVLW LNGGPGCSSL
TGLFLELGPA TIDKNLKIVP NPYSWNSNAS VIFLDQPVNV GFSYSGSSVS DTVAAGKDIY
ALLTLFFKQF PEYATQDFHI SGESYAGHYI PVFASEILSH KNTNINLKSV LIGNGLTDPL
TQYPQYRPMA CGDGGYPAVL DQGTCRSMDN SLERCLSLIE TCYSSESAWV CVPAAMYCNS
AIIGPYQQTG MNPYDVRSKC EDMSSLCYPQ LNTITEWLNQ KSVMKALGVE VESYESCNGG
INRDFLFHGD WMKPYHRLVP SLLEKIPVLI YAGDADFICN WLGNLAWTNA LEWPGHKKFA
DAKMNDLKIV DNKSKGKKIG QVKSSGNFTF MRIFGAGHMV PLNQPEASLE FFNRWLRGEW
R