ID A0A2H3TUL8_FUSOX Unreviewed; 406 AA.
AC A0A2H3TUL8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Related to extracellular metalloproteinase {ECO:0000313|EMBL:SCO92308.1};
GN ORFNames=FRV6_16436 {ECO:0000313|EMBL:SCO92308.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO92308.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388}.
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DR EMBL; FMJY01000010; SCO92308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3TUL8; -.
DR VEuPathDB; FungiDB:FOC1_g10011973; -.
DR VEuPathDB; FungiDB:FOIG_06178; -.
DR VEuPathDB; FungiDB:FOMG_08876; -.
DR VEuPathDB; FungiDB:FOXG_05949; -.
DR VEuPathDB; FungiDB:FOZG_07649; -.
DR VEuPathDB; FungiDB:HZS61_013531; -.
DR OrthoDB; 2679274at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR032475; Protealysin_N_PP.
DR PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF16485; PLN_propep; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 60..99
FT /note="Protealysin N-terminal propeptide"
FT /evidence="ECO:0000259|Pfam:PF16485"
FT DOMAIN 97..232
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 236..402
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT REGION 98..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 45235 MW; 37C088AA907E04F6 CRC64;
MACRHFIVPP HLLRAIADSE ANADKIRHAA RRTLAARDTY TKVRAERMVA LTVPRGYQRQ
QIIPPHILRS LSQSEESEEN VRDRAKRDLQ HVEGLMQQKL ASSESSGTAE LAKKPSPKRS
VYDANHTTDE ADLPGKLVRK EGGDKVKDEA VNEAYDNVGI VLGFYKEQFN WNSIDNKNVD
VSSSVHFGEG YENAFWDPER LQMVYGDGGE FLNNFTGCID VIGHELTHAV TEHTSPLEYT
GQSGALNEHV SDVFGIMIKQ KVQNEKAHGA DWLIGEDCIL PGVKGVALRS MKAPGTAYDD
ARFGKDPQPD NMKDYEIIVE DNGGVHIYSG IPNKAFYLAS VAFGGYSWEK AGKIWWETMR
SGKIAPKCQF KHFADITVEI AEELFGEEAA KIVRKAWTDV GITRGI
//