CBPYA_ASPTN
ID CBPYA_ASPTN Reviewed; 557 AA.
AC Q0CSD3;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=cpyA; ORFNames=ATEG_03401;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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; CH476597; EAU36675.1; -; Genomic_DNA.
DR RefSeq; XP_001212579.1; XM_001212579.1.
DR AlphaFoldDB; Q0CSD3; -.
DR SMR; Q0CSD3; -.
DR STRING; 341663.Q0CSD3; -.
DR MEROPS; S10.001; -.
DR PRIDE; Q0CSD3; -.
DR EnsemblFungi; EAU36675; EAU36675; ATEG_03401.
DR GeneID; 4317774; -.
DR VEuPathDB; FungiDB:ATEG_03401; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000007963; 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 Reference proteome; Signal; Vacuole; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..138
FT /evidence="ECO:0000250"
FT /id="PRO_0000407439"
FT CHAIN 139..557
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407440"
FT ACT_SITE 280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 193..433
FT /evidence="ECO:0000250"
FT DISULFID 327..341
FT /evidence="ECO:0000250"
FT DISULFID 351..374
FT /evidence="ECO:0000250"
FT DISULFID 358..367
FT /evidence="ECO:0000250"
FT DISULFID 396..403
FT /evidence="ECO:0000250"
SQ SEQUENCE 557 AA; 62443 MW; 5789C84F886F2EB9 CRC64;
MRVLPATLLV GAATAAVPPF QQQFQQVLGI PQEEVEQAAP VAPSAPTTPK PLQIFQDQLK
SLSDEARKLW DEVSNFFPDS MDHNPVFSLP KKHTRRPDSH WDHIVRGSDV QGVWVTGADG
EKQREVDGKL EAYDLRVKKT DPSALGIDPG VKQYTGYLDD NENDKHLFYW FFESRNDPEN
DPVVLWLNGG PGCSSLTGLF MELGPSSINE KIKPVYNEYS WNSNASVIFL DQPVNVGYSY
SGSAVSDTVA AGKDVYALLT LFFKQFPEYA KQDFHIAGES YAGHYIPVFA SEILSHKKRN
INLQSVLIGN GLTDGYTQYE YYRPMGCGEG GYPAVLDKGT CQSMDNALPR CQSMIKSCYE
SESSWVCIPA SIYCNNALIG PYQRTGQNVY DVRGKCEDES NLCYKGMGYV SEYLNKAEVR
QAVGAEVDGY DSCNFDINRN FLFHGDWMKP YHRLVPGLLE QIPVLIYAGD ADYICNWLGN
KAWTEALEWP GQKEYASAEM EDLVIEQNAN TGKKIGQVKS HGNFTFMRIY GGGHMVPMDQ
PESGLEFFNR WLGGEWF