ID   CBPYA_EMENI             Reviewed;         552 AA.
AC   Q96VC4; C8VGH8; Q5B1Y8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=AN5442.2;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=A26;
RX   PubMed=11440134; DOI=10.1271/bbb.65.1175;
RA   Ohsumi K., Matsuda Y., Nakajima H., Kitamoto K.;
RT   "Cloning and characterization of the cpyA gene encoding intracellular
RT   carboxypeptidase from Aspergillus nidulans.";
RL   Biosci. Biotechnol. Biochem. 65:1175-1180(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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:0000269|PubMed:11440134}.
CC   -!- DISRUPTION PHENOTYPE: Decreases strongly intracellular carboxypeptidase
CC       activity. {ECO:0000269|PubMed:11440134}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; AB051820; BAB56108.1; -; Genomic_DNA.
DR   EMBL; AACD01000094; EAA62602.1; -; Genomic_DNA.
DR   EMBL; BN001305; CBF81902.1; -; Genomic_DNA.
DR   PIR; JC7666; JC7666.
DR   RefSeq; XP_663046.1; XM_657954.1.
DR   AlphaFoldDB; Q96VC4; -.
DR   SMR; Q96VC4; -.
DR   STRING; 227321.Q96VC4; -.
DR   ESTHER; emeni-CBPYA; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; Q96VC4; 2 sites, No reported glycans.
DR   EnsemblFungi; CBF81902; CBF81902; ANIA_05442.
DR   GeneID; 2871736; -.
DR   KEGG; ani:AN5442.2; -.
DR   VEuPathDB; FungiDB:AN5442; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; Q96VC4; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; TAS:UniProtKB.
DR   GO; GO:0004180; F:carboxypeptidase activity; IDA:AspGD.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IMP:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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:SF113; CARBOXYPEPTIDASE Y; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..133
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407449"
FT   CHAIN           134..552
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407450"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        467
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        529
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        188..428
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..336
FT                   /evidence="ECO:0000250"
FT   DISULFID        346..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        353..362
FT                   /evidence="ECO:0000250"
FT   DISULFID        391..398
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  62066 MW;  F67CF39FDBF7D761 CRC64;
     MRVLPATLLV GAATAATPAQ QVLGGLQDFG NAVQDAMHEN LPKINKPLEA FQEQLKSLYE
     AREFWEEVAN AFPQNLDHNP VFSLPKKHTR RPDSHWDHIV RGADVQSVWV TGENGEKERE
     IEGKLEAYDL RIKKTDPSSL GIDPDVKQYT GYLDDNENDK HLFYWFFESR NDPKNDPVVL
     WLNGGPGCSS LTGLFMELGP SSIDENIKPV YNPYAWNSNA SVIFLDQPVN VGYSYSGSTV
     SDTVAAGKDV YALLTLFFKQ FPEYAEQDFH IAGESYAGHY IPVFTSEILS HQKRNINLKS
     VLIGNGLTDG LTQYEYYRPM ACGEGGYPAV LDESSCRSMD NALGRCQSMI ESCYNSESAW
     VCVPASIYCN NALLAPYQRT GQNVYDVRGK CEDESNLCYK GMGYVSEYLN KPEVRAAVGA
     EVDGYDSCNF DINRNFLFHG DWMKPYHRLV PGILEQIPVL IYAGDADFIC NWLGNKAWTE
     ALEWPGHKEF AAAPMEDLKI VDNEHTGKKI GQIKTHGNFT FMRLYGGGHM VPMDQPEASL
     EFFNRWLGGE WF
//