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Database: UniProt
Entry: F9FD68_FUSOF
LinkDB: F9FD68_FUSOF
Original site: F9FD68_FUSOF 
ID   F9FD68_FUSOF            Unreviewed;       546 AA.
AC   F9FD68;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=FOXB_04346 {ECO:0000313|EMBL:EGU85124.1};
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:EGU85124.1};
RN   [1] {ECO:0000313|EMBL:EGU85124.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU85124.1};
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   -!- 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:EGU85124.1}.
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DR   EMBL; AFQF01001379; EGU85124.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FD68; -.
DR   STRING; 660025.F9FD68; -.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          62..506
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   546 AA;  60677 MW;  1D6D510EC960BDB0 CRC64;
     MEPLSSATWA NSVAYYNGRV YTVNEMQEWT EGFIVNETGV FEAVGSSQDI LAIADKRRLV
     RFDLRQKFSM PGIHDAHAHM YFAGLAQMSE ATLELEPNDA KIAEKIQKGH CMCSHTGERH
     DWILGNSYLL IHFPDNVPDR RYLDEIFPDR PVLIRELSVH SMLLNTKALE RLSINDATPD
     PPGGRYVRRA DGTLSGGLYE SAMEKVWNAV PFPPMSHYKR ALSRAVSICH SYGITSAQEA
     TASTMELDAF RELEAENRLD FDIYTHIVSA PGSAVGESED SLAAQISIDE GFRTKHIHPH
     FIKFILDGLY DAKGYTCKVH AAGEGSARLA LDILEQVRAL NPNGPRHEVA HCNSVHADDV
     KRFAPLRVTA EMSPAIFHNE DMIKANPKFF DWDFVGMHKT GALTTIGSDW VVVPTPNVLP
     SVAYLTEPIG AGIETDVDDG LTDLQRGSRV TIRMLTLGGA EAVDSKRSAG SIEVGKKANF
     IALDSDLSEG EFANATCLQT WFEGRRCIAE LRLFVQRTVR LDLNNKSDKD KGINIFFFPF
     SSPRTL
//
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