ID A0A0L6WRL1_9AGAR Unreviewed; 1397 AA.
AC A0A0L6WRL1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Chromatin structure-remodeling complex subunit snf21 {ECO:0000313|EMBL:KNZ78207.1};
DE Flags: Fragment;
GN ORFNames=J132_01732 {ECO:0000313|EMBL:KNZ78207.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ78207.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KQ412487; KNZ78207.1; -; Genomic_DNA.
DR STRING; 1306850.A0A0L6WRL1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000053712; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-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; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT DOMAIN 89..124
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 374..455
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 569..734
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 880..1034
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1249..1319
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 33..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KNZ78207.1"
SQ SEQUENCE 1397 AA; 158914 MW; EEB903BAC2AC0BDC CRC64;
RANFLKKNPH EQKNPGELEQ LLKYIHAVSQ VQGRPQGQIS NMAQQQQQLQ QPPMTNGHTQ
SLPNGSATTS ITSGPIPQNI PPQSSTPVSF TQEQIGALRA QIHAFKCISR GMPIPEHVQQ
ALRVPNTAIP DLEKLLQGPD VSSRVVTAAV NVAKGEPTSS ASVIAAIPEE TAKVEEELAV
AYNAADMPKG PFLEDDTKSG IYPYNAYRHP FTHLKRTGDT DPSLFATRLQ RLLVPSIMPA
GLDAHQILSE RDRYIEARVQ QRIRELEAMP STMGDGSFDD TFDPDENMKE EKGVDATILK
LQNGNTNHLS ALIHPSASAH GKLRAVIELK SLRLLEKQRS MRAQVAERLN HSAMLPLNRL
DFRRIRKPNI RDARKTEQAE RKQRVEREHR AKRKHVEQIT VICTHGREVL NANRAAQDRV
TRLGRSVLAF HQMTEKEEQK RIERISKERL RALKADDEEA YMKLIDTAKD TRITHLLRQT
DAYLDSLAQA VVTQQNESGL EMMPFEQEDG PTSEATFGAQ VNADEGDDKK KVDYYAIAHR
ISEKVSKQPS LLVGGTLKEY QLKGLQWMVS LYNNRLNGIL ADEMGLGKTI QTISLITFLI
EVKRQHGPYL VIVPLSTMTN WSGEFAKWAP TVKTISYKGN PSQRRALQGE LRVGHFQVLL
TTYEYIIKDR PFLSKVKWVH MIIDEGHRMK NTQSKLSQTL TTYYHSRYRL ILTGTPLQNN
LPELWALLNF ALPKVFNSVQ SFDEWFNTPF ANSGTGDKIE LNEEEALLII RRLHKVLRPF
LLRRLKKDVE SELPDKVEKV IKVRMSALQS QLYKQMKKHK MIADGTSKGK PAGIKGLSNE
LMQLRKICQH PFLFESVEDR VSPSGFIDEK LVRTSGKLEL LNRILPKFFA TGHRVLIFFQ
MTKVMDIMED FLKMMKWAYL RLDGGTKTEE RASFVQLFNA VNSEYKVFIL STRAGGLGLN
LQTADTVIIF DSDWNPHADL QAQDRAHRIG QTRAVLILRF ITEKSDARYK LDIDDKVIQA
GRFDNKSTQE EQEEFLRSIL EADQEEENEE AGDMNDDELN ELIARTEEEA AIFREMDMKR
ERDVIEHWRN SGGRGKPPPP LMQLEELPEC YQTDEPFEAK EIEDVLEGRG QRRRNVVSYN
DGLSDEQWAL ALEEGEDIQE LSERARDRKD RRAANKLLRE ADASNRGTPA SDVDSRGRKN
KKGKAKALDY EPSTGSKRKR GQKSMSVTPS LNGDDDDEHE MKRPCEDETG RKRCDLFREL
PDKRDYPDYY HLITRPIALS HLRKRANSTY YKTVQAFKDD WKLMFDNART YNQEGSWVYV
DAEEMEKVFN ATFDQVMTGS GLPGAPAATG NGSASGSYDS ALTPMDEDER PIPSRSRSAG
RKQVISDEEY LTPSDDD
//
