ID F9FUF4_FUSOF Unreviewed; 1074 AA.
AC F9FUF4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 08-NOV-2023, entry version 52.
DE RecName: Full=Endocytosis protein end4 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_10035 {ECO:0000313|EMBL:EGU79450.1};
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:EGU79450.1};
RN [1] {ECO:0000313|EMBL:EGU79450.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU79450.1};
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 SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
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:EGU79450.1}.
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DR EMBL; AFQF01002678; EGU79450.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FUF4; -.
DR STRING; 660025.F9FUF4; -.
DR PaxDb; 5507-FOXG_03618P0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR10407:SF15; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF89009; GAT-like domain; 1.
DR SUPFAM; SSF109885; I/LWEQ domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT DOMAIN 9..153
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 825..1074
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 322..621
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 120613 MW; 4E363300F57A37A2 CRC64;
MAAAVRGTEH TKSATPSRFM TAKLTPSSCA EPIKSSLSTS RRLQTSRRSL QSESMSEHVS
SIHGTIGPPP PSGPASRSDE VQTFKALITI HKVLQEGHPS ALKEAMANRA WIDSLNRGMG
GGEGMRGYAP LIREYVYYLL AKLSFHHQHP EFNGTFEYEE YLSLKAINDP NEGYETISDL
MVLQDKIEQF QKLIFSHFRN VGNNECRIAA LVPLVQESYG IYKFITSMLR AMHSTTGDDE
ALEPLRERYN AQHYRLVKFY YECSNLRYLT SLITIPKLPQ DPPNLLAEDD DAPALPARPK
QEIERKPSPP PEPKNDAPDE MNEFWKSELD RQNREYEEQQ RILEQQQQQA LLAQQQAQLQ
AQREFEQQQQ QLMEQQQREQ EALMAQQAQW QTQGRLAELE RENLNARAQY ERDQLMLQQY
DQRVKALEGE LSHIQNSLGQ QMNSKDDQIR ALQEQVNTWR TKYEALAKLY SQLRHEHLDL
LQKFKAVQLK AASAQEAIDR REKLEREIKT KNLELADMIR ERDRALHDKD RATGSSKDEV
EKLKRELRLA QDKADNLERS KGNELSTMLA KYNREMADLE EALRNKTRQL EDAQMNLRDG
SSDLEQLLRD KEEELEVYKA GMDQTLIELN ELKMNQGDTD HALDGQIDAL IMSNLDKIND
IIDSVLQAGV ARVDDALYEL DSSMQAGNQN ASPSYVLSQI EKASASAMEF ATSFNNFIAD
GPNATHADLI KAINVFSGAI ADVCSNTKGL TRLATDDKKT DALMNGTRQP AISAVQFLRG
LQSFRLEGMD PLQKTDVVIN SNNDVQMNLQ KLNKLVESFA PGFGKLANKK GDLGDLVDQE
LSKAADAIAA AAARLAKLKN KPRDGYSTYE LKVNDSILDA ATAITNAITQ LIQAATVTQQ
EIVQAGRGST SRTAFYKKNN RWTEGLISAA KAVASSTNTL IETADGVISG RNSPEQLIVA
SNDVAASTAQ LVAASRVKAG FMSKSQEKLE QASKAVGAAC RALVRQVQSL IKERSQEEDQ
VDYSKLGAHE FKVREMEQQV QLIPGPVEIL QLENALASAR HRLGEMRKIS YQEE
//
