CBPYA_TALSN
ID CBPYA_TALSN Reviewed; 553 AA.
AC B8M044;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=cpyA; ORFNames=TSTA_083730;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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; EQ962653; EED21141.1; -; Genomic_DNA.
DR RefSeq; XP_002478104.1; XM_002478059.1.
DR AlphaFoldDB; B8M044; -.
DR SMR; B8M044; -.
DR STRING; 441959.B8M044; -.
DR ESTHER; penmq-cbpya; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR PRIDE; B8M044; -.
DR EnsemblFungi; EED21141; EED21141; TSTA_083730.
DR GeneID; 8101466; -.
DR VEuPathDB; FungiDB:TSTA_083730; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; B8M044; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
DR PhylomeDB; B8M044; -.
DR Proteomes; UP000001745; 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..134
FT /evidence="ECO:0000250"
FT /id="PRO_0000407480"
FT CHAIN 135..553
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407481"
FT ACT_SITE 276
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 220
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 189..428
FT /evidence="ECO:0000250"
FT DISULFID 323..337
FT /evidence="ECO:0000250"
FT DISULFID 347..370
FT /evidence="ECO:0000250"
FT DISULFID 354..363
FT /evidence="ECO:0000250"
FT DISULFID 392..398
FT /evidence="ECO:0000250"
SQ SEQUENCE 553 AA; 61898 MW; A1EB9702FD8701F4 CRC64;
MRVLSTTLLI GAAAAAVSPP QQVLQAPEEA VENTHKSSPS LAESLSQPLR ELKEELKLLT
NEVEEVWEEV SNIFPGALDN IFFSSAKKHT RRPDSHWDHI IRGSDVQNIW VENENGEKER
EVGGRLEAFD LRVKAVDPSS LGIDPDVKQY SGYLDDNEND KHLFYWFFES RNDPKTDPVV
LWLNGGPGCS SLTGLFFELG PSSIGKNIKP IYNPYSWNSN TSVIFLDQPV NVGFSYSGNS
VSETSAAAKD VYALLTLFFK QFPEYSSQDF HIAGESYAGH YIPSFASEIL SHKKRNINLK
SVLIGNGLTD GLTQYEYYRP MACGDGGYPA VLDETTCRSM DNALGRCQSM IQSCYDSESA
WTCVPASIYC NNALLGPYQR TGQNVYDVRK PCEDSSLCYA DLEYVSTYLN QAEVMKALGA
EVDSFDSCNF DINRNFLFKG DWMKPFHKLV PGLLEEIPVL IYAGDADFIC NWLGNKAWTD
ALEWAGHEEY AATELEDLEI VDNKHKGKKI GQVKSSGNLT FMRLFGGGHM VPYDQPEASL
EFFNRWIGGE WTK