ID A0A1A6A912_9TREE Unreviewed; 1123 AA.
AC A0A1A6A912;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Transcription activator snf2l1 {ECO:0000313|EMBL:OBR86550.1};
GN ORFNames=I303_02558 {ECO:0000313|EMBL:OBR86550.1};
OS Kwoniella dejecticola CBS 10117.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR86550.1, ECO:0000313|Proteomes:UP000078595};
RN [1] {ECO:0000313|EMBL:OBR86550.1, ECO:0000313|Proteomes:UP000078595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR86550.1,
RC ECO:0000313|Proteomes:UP000078595};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KI894029; OBR86550.1; -; Genomic_DNA.
DR RefSeq; XP_018264392.1; XM_018405898.1.
DR AlphaFoldDB; A0A1A6A912; -.
DR STRING; 1296121.A0A1A6A912; -.
DR GeneID; 28966257; -.
DR VEuPathDB; FungiDB:I303_02558; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000078595; 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; IPR001005; SANT/Myb.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 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.
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:UP000078595}.
FT DOMAIN 250..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 547..704
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 129105 MW; C591A52E0C3011B9 CRC64;
MSGTVLGTSN HPRLRVRSRQ HEQGDARLER NPLLAASNAT GAGADDDKLS DYVPNSRDLS
VSRAPSAVAS DEMNQRHINT APQTPEPESE DELDDEQLDE DDLMNGSSKA AKKAAQSSAR
KAANAERKAQ VAEIGAKRSA MEQAKFADSI KRFQYLLGQT ELFQHFIDLK KQREPEFAKM
LDEQMASQGG SKGKKKANDH RHRKSEKEED EELLKDEDAE DEAFVFEESP PYVKGGKMRD
YQVQGLNWMA SLHHNGINGI LADEMGLGKT LQTISFLGYL KFHKQIAGPH LIVVPKSTLD
NWRREVGKWV PGFNTLVLQG TKEERLDLIN KRILTQDFNI LITSYEMCLR EKSTLRKFSW
EYIIIDEAHR IKNVDSLLSQ IIRTFTSRGR LLITGTPLQN NLQELWALLN FILPDVFSSS
EDFDAWFKTK DDSDSDAVVK QLHKVLRPFL LRRVKADVEH SLLPKKEINL YVGMTEMQRK
WYRMLLEKDI DAVNGASGKK EGKTRLLNIV MQLRKCCNHP YLFDGAEPGP PFTTDEHLVD
NAGKMVILDK LLKSMKAKGS RVLIFSQMSR VLDILEDYCQ FRGHQYCRID GNTPHEDRIS
AIDDYNAPGS EKFVFLLTTR AGGLGINLVT ADIVVLFDSD WNPQADLQAM DRAHRIGQTK
QVYVFRFITQ DAVEERILER ATQKLKLDQM VIQEGRSQQA QKVGQNKDEL LDMIQHGAEK
IINNSTSMLI DDDIDEIIKR GEDKTAELNS KYAGLDLDAL NNFKSESMVN TWEGEDYANK
RGGKPLLWIE PAKRERKNNY NIDQYYRDSL NTSAPKSDKP KVSRPPKQIN INDFQFYPAR
LVELQDREWD AHRRAQNYVV PAREPEEGET AEQVEAERAE EQERINNSEP LTEEEVAEKD
ALVGEGFPDW QRRHYQAFVR GVEKYGREAL DKVAIEVNDH SEDAVRDYAE VFFERYKELK
DWEKAMERIR IGEDKIREQQ DRIDALHRKV KASRYPLQEL KIMYGQNKGK TYSDEEDRFL
LVRMHHHGIE RDDCYELIKR DIGEWPLFRF DWFFKSRTPD ELKRRAHTLL LCVMKEEEKG
GAAEEDKKPV KGKKRPIDEL KTAPGSRDTT PSVSGQKSKK KKV
//
