CBPYA_TRIVH
ID CBPYA_TRIVH Reviewed; 543 AA.
AC D4DLI1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=cpyA; ORFNames=TRV_08055;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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; ACYE01000509; EFE37290.1; -; Genomic_DNA.
DR RefSeq; XP_003017935.1; XM_003017889.1.
DR AlphaFoldDB; D4DLI1; -.
DR SMR; D4DLI1; -.
DR ESTHER; triru-q5j6j0; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR EnsemblFungi; EFE37290; EFE37290; TRV_08055.
DR GeneID; 9579811; -.
DR KEGG; tve:TRV_08055; -.
DR HOGENOM; CLU_008523_10_4_1; -.
DR Proteomes; UP000008383; 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 Signal; Vacuole; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..124
FT /evidence="ECO:0000250"
FT /id="PRO_0000407488"
FT CHAIN 125..543
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407489"
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; 60657 MW; 8CFE0E24E4B01FA6 CRC64;
MKFLTTGLLA TAALAAAQEQ HVLQAEDGHG QAPQRDASIF DETLQKFQSS LEDGISHFWS
EMKTNFKDYL PLISLPKKHT RRPDSEWDHV VRGADIESVW VQGADGEKRR EIDGKLHNYD
LRVKAVDPSK LGVDPGVKQY SGYLDDNDAD KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
SLTGLFLELG PATIDKNLKV VSNPYSWNSN ASVIFLDQPV NVGFSYSGSS VSDTVAAGKD
VYALLTLFFK QFPEYASQDF HISGESYAGH YIPVFAAEIL SHKNTNINLK SALIGNGLTD
PLTQYPQYRP MACGEGGYPA VLDQGTCRSM DNSLERCLSL IETCYSSESA WVCVPAAMYC
NSAILAPYQQ TGMNPYDVRT KCEDMASLCY PQLNAITKWL NQESVMQALG VEVQSYESCN
SGINRDFLFH GDWMKPYHRL VPSVLEKIPV LIYAGDADFI CNWLGNLAWT DALEWPGHKK
FAEAKLEDLK IVNNKDKGKK IGQVKSSGNF TFMRIFGAGH MVPLNQPEAS LEFFNRWLGG
EWH