CBPYA_EMENI
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 03-AUG-2022, entry version 114.
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; 162425.CADANIAP00003647; -.
DR ESTHER; emeni-CBPYA; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR EnsemblFungi; CBF81902; CBF81902; ANIA_05442.
DR EnsemblFungi; EAA62602; EAA62602; AN5442.2.
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; 625787at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; 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..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
