ID W7LQ22_GIBM7 Unreviewed; 1116 AA.
AC W7LQ22;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Adenosinetriphosphatase {ECO:0000313|EMBL:EWG40621.1};
GN ORFNames=FVEG_02946 {ECO:0000313|EMBL:EWG40621.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG40621.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG40621.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; DS022244; EWG40621.1; -; Genomic_DNA.
DR RefSeq; XP_018746812.1; XM_018890489.1.
DR AlphaFoldDB; W7LQ22; -.
DR STRING; 334819.W7LQ22; -.
DR EnsemblFungi; FVEG_02946T0; FVEG_02946T0; FVEG_02946.
DR GeneID; 30061119; -.
DR KEGG; fvr:FVEG_02946; -.
DR VEuPathDB; FungiDB:FVEG_02946; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OMA; VHDYQFF; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000009096; Chromosome 5.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
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..156
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..156
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; 127903 MW; 63BE6136222B2294 CRC64;
MAPRSRAKAV DTDASMSDAQ EHRQEEEMEV DETPDYTDTE NPSTTASSVA GEPTGDGRRR
RTEVNQLRRS IFGKKHDRLG ESKEDDTIRR FRYLLGLTDL FRHFIETNPD PKIRDIMTEI
DRQNAESARG KKGAGRQGGA TSERRRRTEA EEDAELLKDE KHGGSAETVF RESPPFIHGT
MRDYQVAGLN WLISLHENGI SGILADEMGL GKTLQTISFL GYLRHILDIT GPHLVIVPKS
TLDNWKREFA KWTPEVDVLV LQGAKDERQT LINNRLVDEK FDVCITSYEM VLREKAHLKK
FAWEYIIIDE AHRIKNEESS LSQVIRLFSS RNRLLITGTP LQNNLHELWA LLNFLLPDVF
GDSEAFDQWF SGQDRDQDTV VQQLHRVLRP FLLRRVKSDV EKSLLPKKEV NVYLGMSEMQ
IKWYQKILEK DIDAVNGAGG KRESKTRLLN IVMQLRKCCN HPYLFEGAEP GPPYTTDEHL
IYNAGKMAVL 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 KLSLQGFGDW 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
//