ID A0A0G4MHQ9_9PEZI Unreviewed; 353 AA.
AC A0A0G4MHQ9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=BN1708_006107 {ECO:0000313|EMBL:CRK33732.1}, BN1723_003769
GN {ECO:0000313|EMBL:CRK31043.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK33732.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|Proteomes:UP000044602, ECO:0000313|Proteomes:UP000045706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK33732.1}, and VL2
RC {ECO:0000313|EMBL:CRK31043.1};
RA Fogelqvist Johan;
RL Submitted (MAY-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}.
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DR EMBL; CVQI01023335; CRK31043.1; -; Genomic_DNA.
DR EMBL; CVQH01022639; CRK33732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4MHQ9; -.
DR STRING; 100787.A0A0G4MHQ9; -.
DR OrthoDB; 2443150at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR Proteomes; UP000045706; 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:UP000044602};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 17..353
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5010893759"
FT DOMAIN 158..346
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 38255 MW; 641319C8ACC7A67F CRC64;
MRVAVVLAVF AAITKGLLPM PSEPIFTLEL GPGSIRTVTE AGKKRLEAAG YDYADLTHSS
IRVARANGGS SGNGPKSSMP PQNNALDQIV TLNATALEEN LLGLTEFHTR YYKSQTGIQS
SKWLLGRIQA YISGATSRGV ERASFRIVDH NWEGQKSIIV SLEGKGKGVV VLGAHSDSIN
GLDPTKGHAP GADDNGTGSI TILEALRAIL ESDLAVKDSE HTLEFHWYAG EEAGLLGSNA
IFNEYARDHV NVIAMLNFDM TGYVKPNTKP TMGVITDNVD PKLTQRLREI IKKCSDHASA
TLNGFPSAFI FESTFENSNE YIHTPEDTIE KVDFGHVYEF AKLAVAAAYE LAW
//
