ID F9FKT9_FUSOF Unreviewed; 491 AA.
AC F9FKT9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=FOXB_07018 {ECO:0000313|EMBL:EGU82432.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU82432.1};
RN [1] {ECO:0000313|EMBL:EGU82432.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU82432.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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}.
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:EGU82432.1}.
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DR EMBL; AFQF01002156; EGU82432.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FKT9; -.
DR STRING; 660025.F9FKT9; -.
DR PaxDb; 5507-FOXG_02417P0; -.
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 Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 20..491
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005130563"
FT DOMAIN 125..218
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 246..432
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 491 AA; 53670 MW; CD3DF602896A78DC CRC64;
MKLLSALICG ALLFSEVSAT KKLTPSQVEG DIKKSKLRKT LEDLNSIAKK NGGNRAFGFP
GYKASVDYIS KQLKGQYGKH LNTYIQPFNY TFEQTKDIWV RGPDGEDVYV ITLIYNVGTP
TPDGVTAPLV LVPIDDERGS GCFADQWEGV DAKDKLALVK RGSCAISDKL KLAKKAGARG
VLLVNNQPGE GITSATLSAE NLELIVPVGV IPLEVGTAWR TRIEGGEKLE VTLLVDSFHE
TRETWNIIAE TKQGDPNNVV MMGAHLDSVQ AGPGINDDGS GTAGILEIAK SFTKYTGYKN
KVRFAWWGAE ESGLAGSYYY GEQLTEEEAD RIRFYFNYDM IGSPKPKYWV QASKPADRVG
GDILAAWLRK KGKTVEWEEF GESSDYAAFV ELGIPSSGIF TGADAETDPC YHLECDTINN
IHWGALTLNT KTAGRAAAQF ALSLKGVPPR DKTSANPKSK RAVAARFEQW QKKKTLASNA
HKCNHKTKVV V
//
