ID A0A165HDP5_9APHY Unreviewed; 1931 AA.
AC A0A165HDP5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=SNF2 chromatin remodeling protein {ECO:0000313|EMBL:KZT11597.1};
GN ORFNames=LAESUDRAFT_692620 {ECO:0000313|EMBL:KZT11597.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT11597.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT11597.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT11597.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV427607; KZT11597.1; -; Genomic_DNA.
DR STRING; 1314785.A0A165HDP5; -.
DR InParanoid; A0A165HDP5; -.
DR OrthoDB; 180798at2759; -.
DR Proteomes; UP000076871; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
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; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR Pfam; PF12054; DUF3535; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; ARM repeat; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000076871};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1354..1527
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1711..1864
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 204..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1884..1912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1931 AA; 213943 MW; F6C8D343EA58EBA5 CRC64;
MTSRLDRLLL LLDTGSSSSV RNTAAKQLAQ LAAKSVIGDV SLVEEDVKAT RQHVSVADQS
AWSELMAVVA RILPYLHSRS HETRSAASTA LSQIFTLVPL WQPCPDADSK DLEPPTSLPP
PEFPSFSVRE LMEKGTLLLA SSGKEFTKPT GILASSSEVK KARKEAMGRL GLGFLDSFGE
EDDMDIEKEL VADEVDQDAD MEAGTKVEEG SPVSDTVFVK KEPSPPTRSR TTTPAVAISD
TIDVAMTDDT SALSARERNR LKRKRKAGNG AYVAPPPQQA SGSKYTATTA GQSKARLVSS
EDQSGGQFRR GGPLSPRDNS PQEKVVIDPS KGGAVSPKAE KQSKALEVPQ GCWVWDGLAK
ILEVDLFSPA WEVRHGAAMA LRELLKLQGK YGGMHADMSW DDNKLAHERW CNDLAVKFLC
IFVLDRFGDF VSDQVVAPVR EMVSQTLASL LLHMPRRSVL HVHSVLLQMI RQDFPIPAKT
SKGKAQDGNE RGHVWEVRHA GLLGIKYEVA VRSDLVSCDI PVDQATSQDG KEVLRGVVDA
AVLGLGDRDD DVRSVAASCL LPVAGHLVER LPEELSRVLA VLWTCLSSMK DDLSSSVGAV
MDLLGKLVTY EEVIEIIADE SRSHPITVLA PTLFPFFRHT IVNVRLAVVK TLSTFMTVQS
LPKEWMDLHL LRLLYQNLVV EERSDIRDAT LAAWRLVLSI MSAVAGWLES LVTQQVLLEW
YAVIMTPLGL PLESSSFYDP TVTMEHDGAP ERHNVDKNML AQDLALVSVE TVLKARIAAA
SALAFIMAYW PNTGQGMTLE DMFKPILVHY IDSTSMLQKF LAAIVSEEWA KDYDARAGPS
APLLTKKSSL AAEVSGKTLS FLQADPPAAY HEMAFTLARI HGECYNLLQS FAHDCKLPQS
SIPPLGSEVD ITGTKPECFT IQTAQDAVGD MFTKLRDSLG RTKKRELAII KEKQAKVITS
IERYIEVKAQ YDTRVCAAFA AAFVAFKSTP DKVSPIVKGI MNSIKNEDNQ DLQARSAVAV
ATFVDFCTQR GLFMPPEKIV KNLCTFLCQD IDQTPTFAQA RKTLGGILSF SRGSGTNGSS
KPNIEKPELT PAEAAQARLS RRGAQLAFVE LSRKFGPRML DVVPKMWQSM AGGLLSACQT
DSVSKMDKAI EKQFGQDLID SFSVLDAIVP TFHEELWPKF GELFPMITLA LRSKFAIIRQ
SAARSFATIC DTMTVDAMRC VVEAVLPFLG DEVNLAYRQG AVELIYHIVQ KLDIKALPYV
IFMVVPVLGR MSDSDDDIRS TATNTFASLV KMVPLEAGLP DPPGFSAELM QRRDAERQFL
TQLLDGSKVQ QYNIPVTIKA ELRKYQQEGV NWLAFLAKYQ LHGILCDDMG LGKTLQSICI
LASKQYERAK RYEETKSPDS VHMPSLIICP PTLTGHWYYE ILKYTDNLKP VLYTGNSRER
SRLLGKVEKY DIVITSYEVV RNDIASLEDM NWHYCILDEG HIIKNAKTKL TKAVKCIRSH
HRLILSGTPI QNNVLELWSL FDFLMPGFLG TESHFNERFS KPILSNRDGK SKSGEAAALA
LEALHKQVLP FLLRRLKEDV LHDLPPKIIQ DYYCELSDLQ KYLYDDFSKS RAGATAEDVI
RSDKGDKHEQ QHVFQSLQYL RKLCNHPALV LKEKEAIIDA LSHAGKKANS ADLSDIHYAP
KLLALRQLLI ECGIGSTPVV ASDTVKTELA DAEPTTTGAF SQHRVLIFCQ MKQMLDIIEK
DLFKQHMPSV TYMRLDGGTE ANKRHAIVQT FNSDPSIDCL LLTTHVGGLG LTLTGADTVI
FVEHDWNPMK DLQAMDRAHR IGQKKVVNVY RLITKGTLEE KIMGLQRFKL NIANSIVTQQ
NTGLASMDTD LVLDLFRRTT ENEDSAVSKK REKESSGVMG QKNVLRGLED LPPEEEYEGL
DLSSFMSTLK H
//
