ID A0A2P5I3W4_9PEZI Unreviewed; 1679 AA.
AC A0A2P5I3W4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Chromatin remodeling factor 6-1 {ECO:0000313|EMBL:POS77180.1};
GN ORFNames=DHEL01_v204424 {ECO:0000313|EMBL:POS77180.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS77180.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS77180.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS77180.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-2017) 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:POS77180.1}.
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DR EMBL; MAVT02000293; POS77180.1; -; Genomic_DNA.
DR STRING; 158607.A0A2P5I3W4; -.
DR InParanoid; A0A2P5I3W4; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000094444; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
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 PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000094444};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 267..338
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 367..427
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 465..636
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 783..947
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1679 AA; 192380 MW; FBB8A38C7D12C7C7 CRC64;
MSASPESSPA NGHVSPVATS VAVQLLDPEP SDSDLSDVQA PDVASPSSDS ANNFNSTARD
GRVDDSDGAS SPSDNGASDD ADFDEVVDSP ASPRSDGPAE GAASASDDSR TAPKRKAGGS
LEEDYMRENP ELYGLRRSSR PQQRKTIVGA DDDDSESDSV VVHRRAAKKR RTERSLPSSK
RETPLRHTPA DDSDSDTYGG ARARAIQKKA RRQAMAQPAL AFAEKRWNSR RAAQVTAGAY
QESDAELDDD SDVTPAHWAG EEEDNSPYIE KIIRHELKEG AEWSPDLTRH DFKYYIKWQG
MSHLHDTWET TASVAGFRGF RRLENYYRKF VEFELSMRYD EDAITPEERE QYILDREREN
EALEDYTNVE RVVAMRDGEE DTEYLIKWKG LQYDECTWET SADVSERAQD KIDQFIDRSQ
RNWQSDRKES NPDTRGRMTK LEHQPSYITN GELREFQMRG LNFLALNWTR GNNVILADEM
GLGKTVQSVS FLSWLRNDRD QEGPFLVVAP LSVIPAWCDT FNNWAPDLNY VVYLGPEAAR
STIREHELMI NNNPKKTKFN VLVTSYDYIL LDADFLRTIK WQVLAVDEAH RLKNRESQLY
AKLVSFNIPC KVLITGTPIQ NNLAELSALL DFLNPGKVLI DEELELLGQS EKPGVIDEQK
DEEQRQQTQE KLSQLHKAIS PFILRRTKET VESDLPPKTE KIIRVELSDV QLDYYKNILT
RNYAALRDAS GQKQSLLNIM MELKKISNHP YMFQGAEERV LNGSSRREDH IKGLITSSGK
MMLLDQLLTK LKKDNHRVLI FSQMVKMLDI LGDYLRIRGY PFQRLDGTIP AGPRRLAINH
FNADGSDDFC FLLSTRAGGL GINLMTADTV IIYDSDWNPQ ADLQAMARAH RIGQKRPVSV
YRLVAKQTIE EEVVKRARNK LFLEYLTIQA GVTDEGKALK EKFQERGVQV DEARTSEDIQ
MILKMRSQNL FEQSGNQEKL EKLDIDAILE QAEETKTAVD DKLNLSSGGI DWDNWMQVTD
VKVDEMALDW DQIIPADQLA VIKAEEEKKE NDAYLAKAME ENAPRKATLK GVKKGSDADR
ADRLAKKRER ERQELQELEE QRALLSDPRR PLNEKETRNL IRAFFRYGSM DDRGDEVVFE
ARLSDRDRDF LHEIIDDLIR DSQAAVDISN EKVREEEERT GKSLAKKDKK AVLVDFGEVR
KVNAETVVER PPQLKLLRNV LAEQANPLNF RLPEAAKAAH YSCDWGARED GMLLIGIDRY
GFGAWTQIRD DPELQMQDKF FLEEHRVDKK EERKKGDDKS IQSPGAVHLV RRSEYLLSVL
MAKYSDDAAA KKAVENHHRS KKNLVLNGHR RSDVHSASGS PAPQLLKKSG HNRDRNRERL
HSDHHRSRSI ADERGTPRPE HKRKHTDDYD DRHSKHRRTD HAHGDNRHGS LDKHAKDDKN
RAKLDSDALD RLNRRREEAV QRFNRLMELD DNKLDVQDNE QLIWSLLKPV RGNFKRIMYT
TQDHIASAKE RAKIMGTELR HIGNHLTGLK DAGLPAEQLD GLMPQFWDFL STVWPIGEIE
VTGDKLAKMY RTLTDKDKGK DKKEGGEKKS AKKRDDLEDG EIDDEDEAHR HARREARRDL
SEESRRDYRR DDYRHRAYEN GDRLSFRKDR DRPLTDRGLA DRGRPSWSPP NNQHRPSPY
//
