CBPYA_ASPFU
ID CBPYA_ASPFU Reviewed; 543 AA.
AC Q5VJG9; E9RBK4; Q4WLH2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE AltName: Full=Carboxypeptidase 3;
DE Flags: Precursor;
GN Name=cpyA; ORFNames=AFUA_6G13540;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jousson O., Monod M.;
RT "Genes encoding carboxypeptidases in Aspergillus fumigatus.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AY436353; AAR96055.1; -; Genomic_DNA.
DR EMBL; AAHF01000006; EAL89192.1; -; Genomic_DNA.
DR RefSeq; XP_751230.1; XM_746137.1.
DR AlphaFoldDB; Q5VJG9; -.
DR SMR; Q5VJG9; -.
DR STRING; 746128.CADAFUBP00000118; -.
DR ESTHER; aspfu-CBPYA; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR EnsemblFungi; EAL89192; EAL89192; AFUA_6G13540.
DR GeneID; 3508544; -.
DR KEGG; afm:AFUA_6G13540; -.
DR VEuPathDB; FungiDB:Afu6g13540; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; Q5VJG9; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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..124
FT /evidence="ECO:0000250"
FT /id="PRO_0000407434"
FT CHAIN 125..543
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407435"
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; 60917 MW; 0B5B0D6D9A2DC16E CRC64;
MRVLPATLLV GAATAAAPPF QQILGLPKKS ADTLAKPLHD LQEQLKTLSG EARHLWDEVA
SHFPNNMDHN PVFSLPKKHT RRPDSHWDHI VRGADVQSVW VAGASGEKER EIDGKLEAYD
LRVKKTDPSA LGIDPGVKQY TGYLDDNEND KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
SLTGLFLELG PSSINEKIKP IYNDFAWNSN ASVIFLDQPV NVGYSYSGAA VSDTVAAGKD
VYALLTLFFK QFPEYAKQDF HIAGESYAGH YIPVFASEIL SHKKRNINLK SVLIGNGLTD
GLTQYDYYRP MACGEGGYPA VLDESSCQSM DNALPRCKSM IESCYNTESS WICVPASIYC
NNALLGPYQR TGQNVYDIRG KCEDSSNLCY KGMGYVSEYL NKREVREAVG AEVDGYESCN
FDINRNFLFH GDWMKPYHRL VPGLLEQIPV LIYAGDADFI CNWLGNKAWT EALEWPGQKE
YAPLPLKDLV IEENEHKGKK IGQIKSHGNF TFMRLYGAGH MVPMDQPEAS LEFFNRWLGG
EWF
