ID A0A098DSH8_GIBZE Unreviewed; 943 AA.
AC A0A098DSH8; A0A0E0SEF3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblFungi:CEF84816};
GN Name=FG09828.1 {ECO:0000313|EnsemblFungi:CEF84816};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EnsemblFungi:CEF84816};
RN [1] {ECO:0000313|EnsemblFungi:CEF84816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF84816};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF84816}
RP GENOME REANNOTATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF84816};
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).
RN [3] {ECO:0000313|EnsemblFungi:CEF84816}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF84816};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; HG970335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A098DSH8; -.
DR EnsemblFungi; CEF84816; CEF84816; FGRRES_09828_M.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 383..547
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 704..742
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 775..931
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 105969 MW; 7057C8EB638822B4 CRC64;
MIHYRRKEAI SVVRLPRQAR SIPSSPCNKK EENKERETTS SFLLACFLSP PVFCNICVII
RMSKSTKRAH DFVDLTSDDE SETRQKRPAL NGPASQHQHQ DRGSSSQNAP SSTAEPDYLD
LTQDDECPPL ELYGTFHGKI VGVRYYAGYA SPGEAVLCRR EPNNSYDRNA IRVDNVVGDQ
IGHLPRKVVE KIAPYVDRGD IVLEAQLIGE KAYYDCPIKL FFYGSSDPQE RSRIEESLKK
DRLVKAMELK NTRKEAEARR KAALGLVNGS STHGVGSELA VPQKPEITMD NVLQKSEAVE
MRKGGDAIKS LAIGEDELEK IPMAEQPEDL KAQLLPYQLQ GLAWMTSKEK PQLPAEGSQD
SVQLWLHQSK KKFFNVASGF VTSIAPKLLS GGILADDMGL GKTLQIISLI LTGGKGPTLI
VAPVSVMSNW SQQIKRHVRG DKQPSIITYH GSEKATAKQL QGYDVVITSY GRLARERDQG
VKRALTSEDI KWRRVVLDEG HTIRNSSTKV AQAACEINAE SRWVLTGTPI VNSVKDLHSL
VKFLHITGGI EQSEIFNAQI TRRLAVGDKT GEKLLQALMH DLCLRRKKDM KFVDLKLPAK
KEYVHRISFR KDEKRKYDAL LDEARGELEQ WQASSQVGQK GRFQNVLERL LRLRQICNHW
SLCKERVSDI LKLLDEHEVV PLNEKNRGLL QEALRLYIES QEECAICYDN PNDPVITTCK
HVFCRGCIIR AIQIQHKCPM CRNKLDESSL LEPAPEDAGD EEDFDAESQS SKTEAMMQIL
KATMRKEGSK VVVFSQWTSF LNIIEAQLKA DGMGYTRIDG SMKADKRDKA IEALDSDPET
RVMLASLAVC SVGLNLVAAD TVILSDSWWA PAIEDQAIDR VHRLGQTRET TIFRLVMEGS
VEERVLDVQS EKRELVTKAF QEKNSRNKKR QNTRAADISK LLG
//