CBPYA_TRIEQ
ID CBPYA_TRIEQ Reviewed; 543 AA.
AC B8XGR4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=CPYA; Synonyms=CarbY;
OS Trichophyton equinum (Horse ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=63418;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Preuett B.L., Abdel-Rahman S.M.;
RT "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT and Trichophyton equinum.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ348246; ACL37336.1; -; Genomic_DNA.
DR AlphaFoldDB; B8XGR4; -.
DR SMR; B8XGR4; -.
DR ESTHER; triru-q5j6j0; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
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 Signal; Vacuole; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..124
FT /evidence="ECO:0000250"
FT /id="PRO_0000407482"
FT CHAIN 125..543
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407483"
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; 60711 MW; D7948DAE58A54235 CRC64;
MKFLTTGLLA TAALAAAQEQ QVLQAEDGMG QAPQRGSSIF DETLQKFQSS LEDGISHFWS
EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW VQGADGEKRR EIDGKLHNYD
LRVKAVDPSK LGVDAGVKQY SGYLDDNDAD KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
SLTGLFLELG PATIDKNLKV VSNPYSWNSN ASVIFLDQPV NVGFSYSGSS VSDTVAAGKD
VYALLTLFFK QFPEYATQDF HISGESYAGH YIPVFAAEIL SHKNTNINLK SALIGNGLTD
PLTQYPQYRP MACGEGGYPA VLDQGTCRSM DNSLERCLSL IETCYSSESA WVCVPAAMYC
NSAILAPYQQ TGMNPYDVRN KCEDMASLCY PQLNVITEWL NQKSVMQALG VEVESYESCN
SGINRDFLFH GDWMKPYHRL VPSVLEKIPV LIYAGDADFI CNWLGNQAWT DALEWPGHKK
FAEAKLEDLK IVDNKNKGKK IGQVKSSGNF TFMRIFGAGH MVPLNQPEAS LEFLNRWLRG
EWH