ID A0A1B8B8X5_FUSPO Unreviewed; 1594 AA.
AC A0A1B8B8X5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Chromatin remodeling factor mit1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPOA_03099 {ECO:0000313|EMBL:OBS29162.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS29162.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS29162.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS29162.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OBS29162.1}.
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DR EMBL; LYXU01000001; OBS29162.1; -; Genomic_DNA.
DR STRING; 36050.A0A1B8B8X5; -.
DR OMA; PLQNNAR; -.
DR Proteomes; UP000091967; Unassembled WGS sequence.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd15489; PHD_SF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR041684; Znf-PHD-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF15446; zf-PHD-like; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 792..964
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1097..1256
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 28..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1594 AA; 180385 MW; 82A68AE6B7650497 CRC64;
MDHDPLEGLM DQDENAIERS LELLRADLLE SEQQPPVDTA MDLEVEYPSP NQGSHAREED
QPDENEEDIL RIEGDIVDDV NPKPMSKPRV TTSYRVQVVV PEISWEERAQ YSFVHSEIVE
SILGEVHDKK TVDYRVEFTD GRKELKSFTQ LVTLENGRAA LARFNQGLGP LDIENMASTR
KRKYEPEDEW DSEHESIISD HMDIDDEEDE EPVQTKRMRS SRLRSRETTK QLSRSPSRMS
DEDELDDLQP EPSRPTRSLR VRQPRQSSNT SFKNGFGSQD QDELHGDIAP ASEEEDDDFM
PIVVSDINPK KGRPSKARQR MKRLQTMSMR QKALSQRPSR HKSDDSDIEF EAPRRSSRAT
RNTLNMQDDA LMDDESFYVA DDRTPGAPKI ISVREIFQPL PTESEFATMH MDTCHTCGGS
RQRGQIVYCQ GCTLSYHKSC IGYRSGREHM VTKVDEDSFV FQCRFCIGVP GKKDDKAPKH
DMCQVCKAPG GSCTSFSEKK TSRQEEKLRE ENGGVDPITP VSPELINNAG NVLFRCVACH
RGWHVEHLPG ARSGTVGTDL KSERLKDHSV DWHCKECATT RHKIHRLVAW RPTRKDLAKQ
VPRPTCAEVR EDDKEYLIKW DSRSYAHCVW KPGAWVYGVA ASAMRVSFGK RDATEDLLKL
DEQDAIPDEF LMADIIFNVK TDSSVRKSTR EQEMSNLAHV TKIFVKFQGL GYDDVVWDSP
PTEDDGEIYA SFAEAYYEYV EGKYFKSESQ PKIKERVKTY KAAPFEEINS QPAGLTRGKL
MGYQIEGVNW LLGNYHSGRS VVLADEMGLG KTVQVVGLVT SLVQDSPKCW PFLIVVPNAT
CPNWRREFKQ WVPELRVVAY HGGREPQALA YKYELFPNGS TDMKAHVVIM SYDSAQDPAT
KNLFKSINWA GLVVDEGQRL KNDENLLYGA LRSMRIPFRL LLTGTPLQNN KRELFNLLQF
IDDKQNAAEL DQEYEVLDKE TLPKLHNKIR PYFLRRTKAG VLKFLPPMTQ IILPVTMTVI
QEKLSKSIMA KNPELIKAMF SNSKMNKKER GSLNNILMQL RKCLCHPFMY SEAIEERHHD
PTVLQRNLVE ASAKLLLLQV MLPKLQERGH RVLIFSQFLQ QLDIIEDFLG GLGYDYRRLD
GSISSLEKQR RIDAFNAPDS PIFAFLLSTR AGGVGINLAT ADTVIILDPD FNPHQDIQAL
SRAHRIGQKK KVLCFQLMTT DSVEERIMQI GKKKMALDHA LIESMDDDDL AGDDLESILK
HGAQALFNDD YEKKSIHYDS AAVDALLDRT DEPETKADDG TSFSYAKVWS NDKSGFEAGL
ATEEMAEPEA INSSVWDRIL AQREAEAMRQ AEANREVLGR GGRRRQAINY KTEAVNNPVP
GDPEADSADS SDDFAGGDSG DESEDDPSVP KGAEADAILE LQNPKARDKK GQQLYRQQVE
NGSQPRQKPT VKQQQQKYWQ TWENGGSQNT NQQGRGQETG IAIPTPNPYQ KAGGQVIPGG
SIDLARYTVG NHIYQGNNAP PVPHQRVLVT QSHHPPLNQI ISFRSDGLKS EAEVRLALDF
VHHSNSDMGT KETQKALLMN RLKSLTPEKA SQHT
//
