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Database: UniProt
Entry: J4H3T8_9APHY
LinkDB: J4H3T8_9APHY
Original site: J4H3T8_9APHY 
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
//
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