ID U4LFW0_PYROM Unreviewed; 545 AA.
AC U4LFW0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=PCON_08616 {ECO:0000313|EMBL:CCX30417.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX30417.1};
RN [1] {ECO:0000313|EMBL:CCX30417.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX30417.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX30417.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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.
CC {ECO:0000256|ARBA:ARBA00025622}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; HF935441; CCX30417.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LFW0; -.
DR STRING; 1076935.U4LFW0; -.
DR eggNOG; KOG1282; Eukaryota.
DR OMA; GDWMKPF; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000018144; Unassembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Signal {ECO:0000256|RuleBase:RU361156};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 18..545
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5006530804"
FT DOMAIN 1..109
FT /note="Propeptide carboxypeptidase Y"
FT /evidence="ECO:0000259|Pfam:PF05388"
SQ SEQUENCE 545 AA; 60641 MW; 57A10CF13DE8705B CRC64;
MKLSVASTLG LALAANAYFP NPAQEPLGIS TADSKLPSFL TNAMEKVKST LGALEMPAEA
AAAWAEIAKL YPEDTVSALQ AMASPQKPKE STKRRPDSHW DHIVKGEDMM SIMSSKIDGH
EKLKGTKLRI KQPNGLGIDE KVKQYSGYLD VEDDKHFFFW FFESRNDPKN DPVVLWLNGG
PGCSSLTGLF MELGPASIDN KVKVVQNPYS WNANASVIFL DQPVNVGYSY SDNAVSSTQA
AGKDVYAFLT MFFEKFPEYA SQDFHISGES YAGHYIPQFA AEILSHEKRN INLKSVAIGN
GLTDGLTQYE YYRPMACGEG GYPAVLSESE CKAMDQSLPR CTSLIESCYK SESVWSCVPA
SIYCNNAMIG PYQRTGINVY DIRGPCKDNN NLCYSELGWI SEYLNKKEVM EALGAEVSTY
ESCNFDINRN FLLHGDWMLP FHKFVVDLLA KIPVLIYAGD ADFICNWLGN HAWTEKLEWS
GKKDFNKVPL GPFTVNDKKV GQVKSAGNLT FLTVEQAGHM MPYNQPEASL EMLNRWIGGE
YWPHA
//