ID F9F210_FUSOF Unreviewed; 1778 AA.
AC F9F210;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Vacuolar protein sorting-associated protein 33A {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_00434 {ECO:0000313|EMBL:EGU89022.1};
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:EGU89022.1};
RN [1] {ECO:0000313|EMBL:EGU89022.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU89022.1};
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 STXBP/unc-18/SEC1 family.
CC {ECO:0000256|ARBA:ARBA00009884}.
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:EGU89022.1}.
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DR EMBL; AFQF01000131; EGU89022.1; -; Genomic_DNA.
DR STRING; 660025.F9F210; -.
DR PaxDb; 5507-FOXG_01950P0; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 1.25.40.850; -; 1.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR043155; VPS33_dom3b.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR11679:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 33B; 1.
DR PANTHER; PTHR11679; VESICLE PROTEIN SORTING-ASSOCIATED; 1.
DR Pfam; PF01593; Amino_oxidase; 2.
DR Pfam; PF09011; HMG_box_2; 1.
DR Pfam; PF00995; Sec1; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267}.
FT DOMAIN 901..995
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 1646..1723
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1646..1723
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 709..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1778 AA; 197554 MW; 50797186720F6B40 CRC64;
MAPRIEFNVE QIRNKARKDL LYLLEGVRGK KNVVLDQSLV GPIGTIVKVA VLQEYGVDKF
FILENDNADT SQRNVVFISR GECGRHAEAI AAQIKRIQRE SQTGHDFHIF WVPRRTLVSD
KLLEEAGVLG DVNIAELPLS FFPLEKDVLS LELDDSFRNL YLSKDVTPDF LMAKALMEIQ
RNHGLFPRVI GKGDNAKRVA DLLSRMRQEL LAGEDTSEAN KIGLTPSTTN ESVIIIDREV
DFVTPLLTQL TYEGLIDEVF EIHNNQTKVD TTVVGAPAQA SAATSQSRKR TIQLDSSDKL
YEQLRDANFA IVGSLLNKVA RRLQKVQSDY ESKHKTKTIA ELKDFVSQLP GYQQEQQSAR
IHTGLAEEII KHTRTDQFKG LLEVQQNLAA GADPSSQFDG IEELIARDAP IAQTLRLLCI
YSCISGGIRP KEFDQFRRLI LEGYGYQHLL TLSNLEKLQL FLSKSSPLAG MIPIPGNNAG
PTGSKTNYTY LRKQLRLIVD EVQEDDPNDI SYVYSGYAPL SIRLVQCILQ KQYLLSVTKG
NSANAAGAPP GVGTQGWQGF DEAVKHVRGQ TFYEHQKGED KAVKARALLS GSGNKQTVFV
VFVGGITFTE IAALRFIAKQ EEEIVQRVDI EKKHVAVTSL STQIFSLPTY LSTILINPRH
RTSLKDQYPR KTFETNAAMG SDFGQSFRKG IGIRKRDLDD KDAIDSLTPS DTIVMSNPPG
RISPPITPDV VSVPQSRQTS TEIASEIAPE IVVWTEDMDI DNASHVESDD ELSSIKSYAE
AFQTQQFLTV RREEPPQNDD DPTPFRVSTI EDAIGSLPSN LTELSDLSSI PSTVSSKATT
PTPVDTDGAQ EEDQDQDLSI DEQPQSHQQS PSHDAERYNF NIRPKASVPT DMSAYQYASE
CVLAAESSRL NPYALHPEEY HLLRHHISYT QVTTYLNIRN GIIRLWFQHP WIGVTRLEAV
GCANARWFDA ASVCYDWLVR RGYINYGCVR LSEAETDDTV APVVKRQKTI AVIGAGISGL
GCARQLEGLF RQFADRFHER GEPAPRVVVL EGRARVGGRV YSREFQTKPK EKSPAFEGKR
HTAEMGGMII TGFDRGNPIN ILLRGQLGLP YHALTADTTI YDNSGRAVDP VRDQLVEKLY
NDCLDRVSEY KHKNQLAKLI EGRRDLIEEG RDSPGDGSKT MFQEEEAAAA QQDAPPVAQQ
NIPAKVNLIP ISSDKLTGRV HMEPGTPATT KASDKAKLMG WTIRDSADGE NIDLTSAVNE
EGATLGSVLD NAISQYKQII GLNAQDHRLI NWHIANLEYS NATSLHNLSL PLWDIDAGNE
WEGSHTMVVG GYQSVARGLV HCPSSLDLKT KFPVKSISYH TGEGMASAAI ECEDGSVVDA
DAVVCTIPLG VLKQNNIVFN PPLPSWKTDV VERLGFGILN KVVLVYDKIF WDHDRHIFGV
LRESSNRLST SQKDYAANRG RFFQWFNVSN TTGLPCLIAL MAGEAGFETE HSSNDSLVAE
ATEVLRSVFG QDVPYPVEAM VTRWGSDRFA RGSYSSAAPG MQPEDYDVMA RPVGNLFFAG
EHTIGTHPAT VHGAYLSGLR AASEVLETLI GPIEVPTPLI LPRDSVLLRK RKEPAQDQQP
ARLQAYENEI QTYIQSKLGD RPSRPAKVAG NAYILYSKDL FDVARKKCEE NRKPGKGGRA
VPNEVRIMTS KMWKDASSEE RKPYEDQATE QKRGYAEAVQ AWTRATERWD QEAAALRTAY
EKENPFGTAK IAEVPHESSS KHRRTRHISY AEDSDIGF
//
