CBPYA_ASPNC
ID CBPYA_ASPNC Reviewed; 557 AA.
AC A5AB21;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=cpyA; Synonyms=cpy; ORFNames=An08g08750;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270178; CAK96655.1; -; Genomic_DNA.
DR RefSeq; XP_001392987.1; XM_001392950.2.
DR AlphaFoldDB; A5AB21; -.
DR SMR; A5AB21; -.
DR MEROPS; S10.001; -.
DR PaxDb; A5AB21; -.
DR EnsemblFungi; CAK96655; CAK96655; An08g08750.
DR GeneID; 4983193; -.
DR KEGG; ang:ANI_1_1208074; -.
DR VEuPathDB; FungiDB:An08g08750; -.
DR HOGENOM; CLU_008523_10_4_1; -.
DR Proteomes; UP000006706; Chromosome 8R.
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_0000407436"
FT CHAIN 139..557
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_5000242373"
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; 62093 MW; 742FF0AE20371CEE CRC64;
MRVLPAAMLV GAATAAVPPF QQVLGGNGAK HGADHAAEVP ADHSADGFSK PLHAFQEELK
SLSDEARKLW DEVASFFPES MDQNPLFSLP KKHNRRPDSH WDHIVRGSDV QSVWVTGENG
EKEREVDGKL EAYDLRVKKT DPGSLGIDPG VKQYTGYLDD NENDKHLFYW FFESRNDPEN
DPVVLWLNGG PGCSSLTGLF MELGPSSINK KIQPVYNDYA WNSNASVIFL DQPVNVGYSY
SNSAVSDTVA AGKDVYALLT LFFKQFPEYA KQDFHIAGES YAGHYIPVFA SEILSHKKRN
INLQSVLIGN GLTDGYTQYE YYRPMACGDG GYPAVLDESS CQSMDNALPR CQSMIESCYS
SESAWVCVPA SIYCNNALLA PYQRTGQNVY DVRGKCEDSS NLCYSAMGYV SDYLNKPEVI
EAVGAEVNGY DSCNFDINRN FLFHGDWMKP YHRLVPGLLE QIPVLIYAGD ADFICNWLGN
KAWTEALEWP GQAEYASAEL EDLVIVDNEH TGKKIGQVKS HGNFTFMRLY GGGHMVPMDQ
PESSLEFFNR WLGGEWF
