ID A0A0D7BKV1_9AGAR Unreviewed; 1142 AA.
AC A0A0D7BKV1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=SNF2 family DNA-dependent ATPase {ECO:0000313|EMBL:KIY71173.1};
GN ORFNames=CYLTODRAFT_429579 {ECO:0000313|EMBL:KIY71173.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY71173.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY71173.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY71173.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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DR EMBL; KN880457; KIY71173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BKV1; -.
DR STRING; 1314674.A0A0D7BKV1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000054007; 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: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; 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; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 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 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.
PE 4: Predicted;
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:UP000054007}.
FT DOMAIN 250..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 554..705
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 86..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 130800 MW; D4565B69DF46263E CRC64;
MSKMVGYPVL IGNTCHTDHR SVASLILTVL DNVEKEPHGR EAYYFGESFG IEPRWIAATA
SKVVTGKVTD ERALTEEELR TFFPGRFTFT TTGPNDDDAL SDVVPSNIVS RQPSQGMDID
ADGESEREED ELLSDMTEPE DSEPEPEPEP VAPAAPKKNT AEERRQAKTK RKEDDAKLTE
RREDMGKAKA ADAIKRYSYL LGQTELFKHF VDIKVRKSSL MDAEQAKPKG RGLINGTMRP
YQLQGLNWMV SLHHNGLNGI LADEMGLGKT LQTISFLTYL KALRNVNGPH LVVVPKSTLQ
NWAREFANWS PDFSVALLTG SKEERAEIIR DRILTQDFEV CITSYEMCLI EKSSLKKLSF
EYIIIDEAHR IKNVDSILSQ IVRAFMSRGR LLITGTPLQN NLKELFALLN FICPEIFVEY
EDLDAFLHKD AKETQSTEEE SSKKVVEALH KILRPFLLRR VKADVEKSLL PKKEINIYVP
LTEMQRKWYR SVLEKDIEAV NGLTGKKEGK TRLMNMVMQL RKVTCHPYLF DGAEPGPPYT
TDEHIIENSG KMIILDKLLK SMKAKGSRVL IFTQMSRILD ILEDYCHFRE YQYCRIDGGT
AHEDRITAID EYNKPGSEKY IFLLTTRAGG LGINLTTADV VVLYDSDWNP QADLQAMDRA
HRIGQTKQVY VFRFITEGSV EERMLERAAQ KLRLDQLVIQ QGRTQQSKGQ SKDELLDMIT
AGAEKLISNT DAAEASFTDD IEDIISRGEA RTTELNSRYE DLNFEDLSNF KSEASVQQWE
GEDFRSGRKN LALNLLTMNK RERKSNYSVD SYFKDTLRAG PSKLDKPTKI PRAPKQVLAQ
DFQFYPQELL LLQERELAVH KRMNDIPALH REPTGPEDTE EVLEAERIIA QEYIDTAEAL
TDAELERKEQ LVEQGFTDWS RRDFQQFVRA LETFGWDQPM EMYANEVSDK NLQEVTAYYK
VFKQQWRTLP EAARIETRIT EGQAKRNKRE LHTRLLHKKM TSLKFPMHEL ELPYPTTKGK
VYTDDEDRYI LCQLHKYGLH KEDLYEQIRK DIMDSPLFRF DWFIRSRSTT ELQRRCTTLL
GLLEKDAESN MMPDGVLSLR GKKRANESVT AIPSRKGTTS GTATPTGSVS AGPERPTKKK
KT
//
