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Database: UniProt
Entry: F9GFH6_FUSOF
LinkDB: F9GFH6_FUSOF
Original site: F9GFH6_FUSOF 
ID   F9GFH6_FUSOF            Unreviewed;       523 AA.
AC   F9GFH6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Oxidoreductase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=FOXB_17410 {ECO:0000313|EMBL:EGU72080.1};
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:EGU72080.1};
RN   [1] {ECO:0000313|EMBL:EGU72080.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU72080.1};
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   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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:EGU72080.1}.
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DR   EMBL; AFQF01006955; EGU72080.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9GFH6; -.
DR   STRING; 660025.F9GFH6; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR021833; DUF3425.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR24320; RETINOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR24320:SF291; SHORT-CHAIN DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF11905; DUF3425; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   REGION          84..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGU72080.1"
SQ   SEQUENCE   523 AA;  57622 MW;  4657807E2479FFCA CRC64;
     LKSGSATYLC LMTVKEILGL TVHRSVHFLK MESNWEPFMK TIADDWTAVP DPAQRKRIQN
     RLAQRARRAR LAGKRGQAIV QCESDKMDAS APSRGDAELG PGHQQSSTDV SALAVIAQRL
     DLDCQIRPGF HIRASTQNLP SPIAPTQLQR SLPHRSYLDM LPWASLRDRL LKSLSVINED
     EFMLEMRNGN LRIWGTVPWE PMGWELFPQK PTYTEESIPS LKGKVFLVTG GTSGVGLALV
     DMLYAKGGTV YLPCRSTTKA AGTIKAIQAA HPESTGDLQT LGLDLNDLDS VAACASTFLA
     RESRLDVLWN NAGISYAPPD ELTAQEYEPH MGINCLGPFL LTKLLLPVLK QTASISPGPS
     TRVIFIASPM VDMAAPLGGV PLSELLPGNQ SVDPSRNYAI SKTGNWFLAS EFDRRTRADG
     ILFIAQNPGN LVTNIWDRVP WIIKAPVKIL LHPPKRGAYS ELWAGPSTEI KLEDGGRYGV
     PWGRWHPSPR RDLLSSLKPK DDGGTGLAAD FWDWCDDQTK KFL
//
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