ID F9G291_FUSOF Unreviewed; 964 AA.
AC F9G291;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Pep3/Vps18/deep orange beta-propeller domain-containing protein {ECO:0000259|Pfam:PF05131};
GN ORFNames=FOXB_12773 {ECO:0000313|EMBL:EGU76752.1};
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:EGU76752.1};
RN [1] {ECO:0000313|EMBL:EGU76752.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU76752.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the VPS18 family.
CC {ECO:0000256|ARBA:ARBA00010454}.
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:EGU76752.1}.
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DR EMBL; AFQF01003186; EGU76752.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G291; -.
DR STRING; 660025.F9G291; -.
DR PaxDb; 5507-FOXG_09431P0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16462; RING-H2_Pep3p-like; 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR007810; Pep3_Vps18.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF26; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 18 HOMOLOG; 1.
DR Pfam; PF05131; Pep3_Vps18; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR PROSITE; PS50236; CHCR; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 21..433
FT /note="Pep3/Vps18/deep orange beta-propeller"
FT /evidence="ECO:0000259|Pfam:PF05131"
FT REGION 236..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 812..846
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 108886 MW; 4434EFF7814AF94F CRC64;
MALDLQDGFV AANGVPDLEE PIFTIERVQL QFSVAADFVA AQVANNVIVL ALSNGRILRI
DLERPEDIDD IDLPKKPSEI GMIRRMFLDP TASHLIVCTA LGENYYLHSQ SKHPRPLGRL
RGVSIESVAW NPSLPTASTR EILIGASDGN IYEAFIETSK EFYKKEVKHL KNLHKLPDGP
ITGLWVDNLQ NNKSDLRRVV IATQTRLFHL VGRIGFGHDG SGSVYTRLFE SEQPVVHELS
RTTSGAPSSL AVSPDPPDSG PYDDDIPDRA YAWLSYQGVF HGKLLNQPVD SNLGTKVFSE
SHMLSRAQIL SPENSERRVP TTEAIDAIAL TQWHIVHLVG GRVITTNRLT GKMVSEHDVI
GQGQKPLGFS VDIQKNTFWL FTSDEIFEIV VRDEERNIWE IMTKLKEFEP ALQHARTPLQ
KETVAAAYGD HLAKNGHWLE AATVYGRSNK PFEDIALSII DNNQPDALRK FLLTKLASLK
KSAVMQRMMI AGWLIEVFMS KLNTLDDTIN TQAEPSEHLN STESRKLLES VRKEFRDFVD
KYKNDLDRKM VYDVISSHGR EGELLYFANA VNDYNYVLSY WVQRERWNEV LNVLKKQTDP
EVFYRYSSVL MTYVAPELVE ILMRHADLKP RNLIPAFLEY NRTFSGGPNA QNQAIRYLNY
AVYQLNSKDA AVHNTLVSIY ASHSSKDESG LLSYLQAQGD EPRYDPDFAL RLCIQHHRTL
SCVHIYTSMG QYLQAVDLAL SHGEVELAAV IADRPMSNPQ LRKRLWLAVA RKVISQSNGI
KTAIEFLKRC DLLKIEDLIP FFPDFVVIDD FKEEICAALE DYSRNIDNLK KEMDESSQTA
TNIKVDIAAL DHRYAIVEPG EKCYTCGLPL LSRQFFVFPC QHSFHSDCLG RKVLEQAGVG
KSTRIRELQT QIQKGLVSGT QRETVVAELD ALVASACILC SDLAIKRIDE PFITHNDNVN
EWAL
//