ID F9G522_FUSOF Unreviewed; 723 AA.
AC F9G522;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Partial AB-hydrolase lipase domain-containing protein {ECO:0000259|Pfam:PF04083};
GN ORFNames=FOXB_13754 {ECO:0000313|EMBL:EGU75735.1};
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:EGU75735.1};
RN [1] {ECO:0000313|EMBL:EGU75735.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU75735.1};
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:EGU75735.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFQF01003431; EGU75735.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G522; -.
DR STRING; 660025.F9G522; -.
DR PaxDb; 5507-FOXG_09291P0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF160; STEROL ESTERASE 1-RELATED; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 273..358
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 82830 MW; 71EDECD53DB73EB0 CRC64;
MTQQQHGSST ATQEHHPKVF GKKLAETAVQ FTQQAEKLSH QHPTGEDPGV AIEAQFVTPH
DPVIITSDGK RLPGVPLQEA HKLNVLREEL QGEPESVEIK AGNETKEKIS NVENANPEQK
KVVQLPSEQN GASLQKSNSN STLRKQTPPS HTNPLFPPLP LYGPPNMLRN LQCMFFRISA
FFLSLAFLGV IVLGSLFTTI PMIWKNIWYR LTFRDPDSDR PFYEEEKRRA QARREQEKSW
KQKSPNGRTL DRMENAEEFP PTEGGPDPII CDVAYYARRV GLDVETFEVQ TEDGFLIDLW
HVYDPKEYTE LEESLRSDRG PEVFQSQRKK LKDPSQKPKF PVLLMHGLLQ SSGAYCCNDD
DSLAFWLCKS GYDVWLGNNR CGFKPKHALL EYNDPRMWCW NIRQMGVFDL PALTSRVITE
TGFEKIGLIC HSQGTTQTFV ALAKEQRPEL GEKLTVFCAL APAAYAGPLI GKMYFKFMRI
ISPGLFRLMF GIHAFIPFMM QMHKLLDPRL YGWLGYKVFS FLFDWTDARW DRGLRNRMFQ
FAPVYVSAES MRWWLGRECF AKHKCILSTK EIVRAEEHMD SKGDGRPVTP RTSSALEAHR
KHPKGSTAWY NKQAPPMAMW VCGNDDLVDG RKLLRRFEKG REPHVNLVHS KVIPEYEHLD
VIWAMDAVDQ VFKEVREVLW KTCNARDICR VPEGCEAVLL EKEKLSVKED VVEECQSSSS
GET
//