CBPYA_CHAGB
ID CBPYA_CHAGB Reviewed; 554 AA.
AC Q2H9G6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=CPYA; ORFNames=CHGG_03138;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ91203.1; -; Genomic_DNA.
DR RefSeq; XP_001229654.1; XM_001229653.1.
DR AlphaFoldDB; Q2H9G6; -.
DR SMR; Q2H9G6; -.
DR STRING; 38033.XP_001229654.1; -.
DR ESTHER; chagb-q2h9g6; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR EnsemblFungi; EAQ91203; EAQ91203; CHGG_03138.
DR GeneID; 4389770; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; Q2H9G6; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000001056; 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..137
FT /evidence="ECO:0000250"
FT /id="PRO_0000407443"
FT CHAIN 138..554
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407444"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 222
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 191..431
FT /evidence="ECO:0000250"
FT DISULFID 325..339
FT /evidence="ECO:0000250"
FT DISULFID 349..372
FT /evidence="ECO:0000250"
FT DISULFID 356..365
FT /evidence="ECO:0000250"
FT DISULFID 394..401
FT /evidence="ECO:0000250"
SQ SEQUENCE 554 AA; 61851 MW; 7D613BD299241E48 CRC64;
MRIAASTVLF GAASAASFQQ QAQHVLSGGF GKAQEAMKPI SDAFTDAAGR PFESFEDAFS
GMTAETKALW EEIKLLVPDS AFKDLSWLSK PKPHHRRDDW NHVVKGADVQ GMWVQDANGK
SHRQVDGRLE EYNLRVKAVD PSKLNVDSVK QYSGYLDDEA NDKHLFYWFF ESRNDPKNDP
VILWLNGGPG CSSLTGLFLE LGPSSIDKTL KVVNNDFSWN NNASVIFLDQ PVNVGYSYSG
SSVSNTVAAG KDVYALLTLF FHQFPEYAKQ DFHIAGESYA GHYIPVFASE ILAHKNRNIN
LKSVLIGNGL TDGLTQYEHY RPMACGEGGY PAVLGEAECR SMDNALPRCQ SLINNCYESG
SVWSCVPASI YCNNAMIGPY QRTGRNVYDI RGPCEDSSNL CYSGLGYISD YLNQQSVMDA
LGVEVSSYDS CNFDINRNFL FQGDWMQPFH RLVPKILEEI PVLIYAGDAD YICNWLGNRA
WTEALEWPGK KDFNAAKVKD LKLSGAEKEY GKVKASGNFT FMQVYQAGHM VPMDQPENSL
DFLNRWLNGE WFAK