ID J4H3T8_9APHY Unreviewed; 1096 AA.
AC J4H3T8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCM03819.1};
GN ORFNames=FIBRA_05968 {ECO:0000313|EMBL:CCM03819.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM03819.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM03819.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM03819.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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; HE797130; CCM03819.1; -; Genomic_DNA.
DR RefSeq; XP_012183102.1; XM_012327712.1.
DR AlphaFoldDB; J4H3T8; -.
DR STRING; 599839.J4H3T8; -.
DR GeneID; 24098730; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; J4H3T8; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000006352; 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: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; 1.10.1040.30; 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 Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT DOMAIN 204..369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 507..658
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 866..919
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1096 AA; 125886 MW; E37C96A433EB8B7F CRC64;
MEEDVLSDVV PSNIVSRQQS EGVESEYADE ILSEQDELQS EEEDDNKGER SSAASPQKLA
QIQASADRAQ KKQKRKAEEG KLQVKRQEMD KAKASIVTDA VKRYSYLLGQ TELFKHFVDI
KKARDPEYAA MLDAQPKPKG RGRKKAVDNS ARHRKSEKEE DEEMLKDGEM AVDGNDQPFV
FEESPSFVNG TMRSYQLQGL NWMVSLHHNG LNGILADEMG LGKTLQTIAF LSYLKHYRSI
SGPHLIVVPK STLQNWAREF ERWTPDVNTV LLTGTKEERG ALIANRLIPQ DFDVLITSYE
ICLIEKSALK KFSFEYIAID EAHRIKNVDS ILSQIVRSFM SRGRLLITGT PLQNNMKELF
ALLNFICPEI FSDYADLDSF LHKDEAEGEG DDEKSKKVVE ALHKILRPFL LRRVKSDVEK
NLLPKKEINI YVGLTEMQRK WYRSVLEKDI DAVNGLTGKK EGKTRLMNMV MQLRKVTCHP
YLFDGAEPGP PYTTDEHLVE NSGKMVILDK LLQSMKAKGS RVLIFSQMSR MLDILEDYCL
FRGYKYCRID GGTAHDDRIV AIDEYNKPDS EKFIFLLTTR AGGLGINLTT ADIVVLYDSD
WNPQADLQAM DRAHRIGQTK QVYVFRFITE GSVEERMLER AAQKLRLDQL VIQQGRTQNT
KAANKEELLE MIAHGAENIV NSNADLMIND DIEAIIQRGE VRTVELNSKY EGLTFEDLSN
FKSEASVQQW EGEDFRTGQR KPLQLNPLAL SKRERKLNYS VDSYFKETMR AGPSKTEKAP
KVPRAPKQIQ LQDFQFFPAR LAELQEQELA AHKRQNDIPA TLRESAGPED TPEKLEAERQ
AAQEYIDNAE PLTEEQLQDK EELIAQGFET WSRRDFQQFV RALETYGWTD DYELLASEIQ
DKNADDVADY YPVFRKKWKE LAEYPRIKAR IEEGEAKRNK RSNLEALLSK KIASVRYPMQ
ELELNYPTTK GKVYSEEEDR YLLCRLNHYG MRAEDVYERI KKDITEFPVF RFDWFFKSRS
PQELQRRCNT LLGMIEKEAE VKQAEEVKTK GTKGKKRGID AVEKSEKLDK PSRSATPAST
TPAAAPAKRQ YKKRKT
//