ID F9F7U7_FUSOF Unreviewed; 1116 AA.
AC F9F7U7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_02472 {ECO:0000313|EMBL:EGU87078.1};
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:EGU87078.1};
RN [1] {ECO:0000313|EMBL:EGU87078.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU87078.1};
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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:EGU87078.1}.
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DR EMBL; AFQF01000749; EGU87078.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F7U7; -.
DR STRING; 660025.F9F7U7; -.
DR PaxDb; 5507-FOXG_05187P0; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 193..358
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 489..640
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 855..907
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 127873 MW; C8587326565A70CA CRC64;
MAPRSRAKAV DTDASMSDAQ EHRQEEEMEV DETPDYTDTE NPSTTASSVA GEPTGDGRRR
RTEVNQLRRS IFGKKHDRLG ESKEDDTIRR FRYLLGLTDL FRHFIETNPD PKIRDIMTEI
DRQNAESARG KKGAGRQGGA TSERRRRTEA EEDAELLKDE KHGGSAETVF RESPPFVHGT
MRDYQVAGLN WLISLHENGI SGILADEMGL GKTLQTISFL GYLRHILDIT GPHLVIVPKS
TLDNWKREFA KWTPEVDVLV LQGAKDERQN LINDRLVDEK FDVCITSYEM VLREKAHLKK
FAWEYIIIDE AHRIKNEESS LSQVIRLFSS RNRLLITGTP LQNNLHELWA LLNFLLPDVF
GDAEAFDQWF SGQDRDQDTV VQQLHKVLRP FLLRRVKSDV EKSLLPKKEV NVYLGMSEMQ
IKWYQKILEK DIDAVNGAGG KRESKTRLLN IVMQLRKCCN HPYLFEGAEP GPPYTTDEHL
VYNAGKMAVL DKLLKRLQKQ GSRVLIFSQM SRLLDILEDY CVFREYKYCR IDGGTAHEDR
IAAIDEYNKP GSEKFVFLLT TRAGGLGINL TTADIVILYD SDWNPQADLQ AMDRAHRIGQ
TKQVVVYRFV TDNAIEEKVL ERAAQKLRLD QLVIQQGRAQ QAAKAAANKD ELLSMIQHGA
EKVFQSKGPT GNMASKDGEV GDDDIDEILA KGENRTKELN AKYEKLGIDD LQKFTSESAY
EWNGENFANT KKNINMTWIN PAKRERKEQS YSMDKYFRQT MYPNPKADAK PKAPRAPKQV
PVHDYQFYPP RLRDLQDRET AYYRKEIGYK VPLPDGDEEN LEEREAERAL DQQEIDNATP
LTEEEREEKE RLSLQGFGDW NKRDFQQFVN GSGKYGRTDY EGISNEIDSK SAPEIKAYAK
VFWQRYTEIA DYPKYIKTIE DGEERTRRIG HHQKLLRKKM QQYRVPLQQL KINYSVSTTN
KKVYTEEEDR FLLVLLDRYG IDSEGLYEKM RDDIRESPLF RFDWFFLSRT PIELSRRCTT
LITTIVKEFE DVPARGSNGV NGKSKREPDD ENDEDSILGM APAKKKAKNG VKNKALDNVK
SVKSSKNSSA TPSRASSVAS TVSAGGSAKG KKGKKK
//
