ID   A0A423WQQ1_9PEZI        Unreviewed;       357 AA.
AC   A0A423WQQ1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=VSDG_00246 {ECO:0000313|EMBL:ROW05545.1};
OS   Valsa sordida.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW05545.1, ECO:0000313|Proteomes:UP000284375};
RN   [1] {ECO:0000313|EMBL:ROW05545.1, ECO:0000313|Proteomes:UP000284375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSFL {ECO:0000313|EMBL:ROW05545.1,
RC   ECO:0000313|Proteomes:UP000284375};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular aminopeptidase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000256|ARBA:ARBA00043843}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28E subfamily.
CC       {ECO:0000256|ARBA:ARBA00043962}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ROW05545.1}.
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DR   EMBL; LJZO01000001; ROW05545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WQQ1; -.
DR   STRING; 252740.A0A423WQQ1; -.
DR   Proteomes; UP000284375; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284375};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..357
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019499351"
FT   DOMAIN          132..348
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   357 AA;  39406 MW;  1F52DE7C7D37122D CRC64;
     MRTLCLLTYA GLASALVVPC LPRLGPEFCP SSQILSNNND TFYDAFLKEH PAIFPNSTTQ
     NDILEKLFPQ LNKARMEKDL RELTDPDLFK NRYCFSKFGP WTQHWILDKL HNDTAPSVYV
     RLVGNQTPQN SVVVKVPGLS NNSISVGAHM DSISNRQSRN DSLSDLIAPG ADDNGSGTVV
     VLEVFRQLLS HVASVGALQN EVQFHWYGAE EIGLVGSKQV FSDMRSKSFP LKAMLNLDMV
     GYPGGGFDKI GVQQDHVDKN LTAFMTTLLE TYTTASAGRI TCGYPCSDHA SAHTYNYSSA
     MIGESAYIKG DPSNPSSNPF AHSANDTIEN DINFDYMMEF ARLALAFVVE LGQYTFE
//