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Database: UniProt
Entry: F9FSH9_FUSOF
LinkDB: F9FSH9_FUSOF
Original site: F9FSH9_FUSOF 
ID   F9FSH9_FUSOF            Unreviewed;       679 AA.
AC   F9FSH9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN   ORFNames=FOXB_09360 {ECO:0000313|EMBL:EGU80085.1};
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:EGU80085.1};
RN   [1] {ECO:0000313|EMBL:EGU80085.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU80085.1};
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:EGU80085.1}.
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DR   EMBL; AFQF01002556; EGU80085.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FSH9; -.
DR   STRING; 660025.F9FSH9; -.
DR   PaxDb; 5507-FOXG_11135P0; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   PANTHER; PTHR23025:SF3; HORMONE-SENSITIVE LIPASE; 1.
DR   PANTHER; PTHR23025; TRIACYLGLYCEROL LIPASE; 1.
DR   Pfam; PF07859; Abhydrolase_3; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}.
FT   DOMAIN          160..309
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   DOMAIN          391..486
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   REGION          300..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   679 AA;  76777 MW;  5C1ADEF205100839 CRC64;
     MIYLYAARNF STLVGLASPE PMANMYDATY YRATWVLTAL DAGFWTAMKI KTKWLRDMAS
     IVFSLFYLVA AEKADEKVRK VRGMITVEHL RVSWNKGTSP YLSFFQGLMR PRFMRWPPRQ
     IRIPRPADSD YKEPILAWLY YDGPLSDLHR HDRLILDIPG GGFVAMDPRC NDDKLFSWAA
     KSALPILSLD YKKAPEFPYP YALNECFDVY RTIVNTKGRC IGLPGTEVPR IIVTGDSAGG
     NLAVASTLMI METRHPAFRR PGQTELPAPD GLVCFYPALD MNIGNWMTDE QMSLIKDRKM
     RKTNRRIMRR KSMQYNELVG TPHHSDDEED GSPPPHTKLS ALTTKEALIA ASQGPRSPHP
     EFSHVGPRSL SLPKDASETN EKKSSHHPEP MKTRLATSSM ISYFNDRVLT PEMMRAMIIL
     YIGAHNRPDF SQDYLLSPVL APEALLVDFP KTYFMTGERD PLVDDTVIFA GRLRRAKEAA
     FVQEQSGRHQ NAEFNDRDAA EVMLIPGTSH GFMQFPTVYP PAWRHFERCI DWFDQLFDHA
     EVMRVRKDRQ ARAARSQTNG FGINGDGRHH MRTESSEEDR PLEISMTKMN QRRSSNQTTP
     QQSPDLNGGS ESGDTTPRAH TNGTSLSNGD KNAKKRKSVG LSKSKNRNKS LVKLKSSDDL
     LGRRMQGLAS GLTGMGDDD
//
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