ID A0A2A9NGF9_9AGAR Unreviewed; 1043 AA.
AC A0A2A9NGF9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PFH46856.1};
GN ORFNames=AMATHDRAFT_68955 {ECO:0000313|EMBL:PFH46856.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH46856.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH46856.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH46856.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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; KZ302154; PFH46856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9NGF9; -.
DR STRING; 703135.A0A2A9NGF9; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000242287; 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; 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.
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:UP000242287}.
FT DOMAIN 154..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 457..621
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 818..871
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 120456 MW; 488FC9FFF03B4FDF CRC64;
MNVKGVASSV AMTKSQAQAE RRERKQKRKA AEGQLQVKRQ EMDKAKVADA VKRYSYLLGQ
TELFKHFVDI KRTRDPEYAS MLDAQPKPKG RGRKKPTDTS ARHRKSEKEE DEELLKDGEM
AADGNDQPVV FEESPKFING IMRAYQLQGL NWMISLHHNG LNGILADEMG LGKTLQTISF
LAFLKHYRGI LGPHLIVVPK STLQNWNREF DRWTPDFNVV LLTGTKEERS DLIANRLITQ
DFEVCITSYE ICLIEKSALK KFSFEYIVID EAHRIKNVDS ILSQIVRSFT SRGRMLITGT
PLQNNLKELF ALLNFICPEI FVHYEDLDSF LHKDDSGAEG EEEKSKKVVE ALHKILRPFL
LRRVKSDVEK NLLPKKEINL YVGLTEMQRK WYRSVLEKDI DAVNGLTGKK EGKTRLMNMV
MQLRKVTCHP YLFDGAEPGP PYTTDEHLIQ NSGKMMILDK LLGLMKAKGS RVLIFSQMSR
VLDILEDYCL FRGYRYCRID GSTPHDERIV AIDEYNKPGS EKFIFLLTTR AGGLGINLTT
ADIVVLYDSD WNPQADLQAM DRAHRIGQTK QVYVFRLVTE GSVEERMLER AAQKLRLDQL
VIQQGHQQQA KTVAANKEEL LEMITHGADQ IISASDELLI DDDIEAIIQR GEERTHQLNS
KYEGLNLEDL SNFKSDSSVQ QWEGEDFRTG QRKALGLNLL SLSKRERKSN YSVDNYFKDT
LRAGPAKPEK APKMPRAPKQ ISIQDFQFFP PGLAQLQERE LAVHKRLNGI VATLRESQGP
EDTPDKLEEE RRVAQEFIDT AEPLSDEEAA LKEAYIEEGF PDWSRRDFQQ FVRALEAYGW
GESYDVYAAE IQEKTPEDVE RYYRTFEKKW KSLAEYPRIA VRIQEGEAKR NKRDNLEILL
SQKIQSVRYP MQELELNYPT TKGKVYSEEE DRYLLCRLHY YGMQTEDVYE RIKKDITEFP
VFRFDWFFKS RSPQELQRRC NTLLTMIEKE AEVKQQEEAK AKSTSKGKKR GIEEVHKTEK
KESKPPTPAT STTTKKSAKK RKT
//
