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Database: UniProt
Entry: W7LQ22_GIBM7
LinkDB: W7LQ22_GIBM7
Original site: W7LQ22_GIBM7 
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
//
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