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Database: UniProt
Entry: A0A0G4L0W0_9PEZI
LinkDB: A0A0G4L0W0_9PEZI
Original site: A0A0G4L0W0_9PEZI 
ID   A0A0G4L0W0_9PEZI        Unreviewed;       491 AA.
AC   A0A0G4L0W0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=BN1708_011521 {ECO:0000313|EMBL:CRK15678.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK15678.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK15678.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK15678.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
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DR   EMBL; CVQH01006669; CRK15678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4L0W0; -.
DR   STRING; 100787.A0A0G4L0W0; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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   CDD; cd04816; PA_SaNapH_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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:UP000044602};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           19..491
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005118055"
FT   DOMAIN          124..211
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          244..433
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   491 AA;  52950 MW;  5329BCE6652E6813 CRC64;
     MKSVAALAAG LFAIGSFASN PLTPEKAVAD IETQKIQRNL WNLNKIARDN GGNRAYGYPG
     YKASSDFILE RVQTRFATTV DTRIQYFNHT FVQLNDISVT GPDGEDVVVI ALTYNPPTPA
     EGITAELIDT PVDDVRGSGC FADQWEGIDA TGKFALVKRG ACAISEKLKL AASKGAVGVI
     LYHNLPGNAI TGATLGFENI GLIPPVGTIP LEVGQAWKAR LAAGETLSVK LFVDAVYEER
     ETWNVIAETK EGDPNNVIVL GAHLDSVPAG PGVNDDGSGT SAILEIISSF KKYKGLKNKV
     RFIWWGAEEV GLIGSLYYTR TLSEEDADKI RFYFNYDMIG SINPMFAVYR GDNAGDAFGA
     DLLYDYLTKE GFPAEYAPFG TGSDYVGFVN IGVPSSGLFT GTPPYDPCYH LACDNIDNIN
     WEAITVNAKA AARAAAILAN SDLKDLPRRS KTSSAKRGVV AMRQEFQRWA AIAEEADHHH
     SCGAHGKENV V
//
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