ID A0A316YMK4_9BASI Unreviewed; 1120 AA.
AC A0A316YMK4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ISW2-ATPase component of a two subunit chromatin remodeling complex {ECO:0008006|Google:ProtNLM};
GN ORFNames=FA10DRAFT_266909 {ECO:0000313|EMBL:PWN90431.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN90431.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN90431.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN90431.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KZ819636; PWN90431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YMK4; -.
DR STRING; 215250.A0A316YMK4; -.
DR InParanoid; A0A316YMK4; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000245768; 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:UP000245768}.
FT DOMAIN 243..408
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 540..691
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 897..950
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 41..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..89
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 127571 MW; 3644A64D78D196EC CRC64;
MASEGGNPPS APSVEISLAP TAAFAASAMA DDQDKLSDYI PASADLSRAP SASASASRMH
SKAPSEEGKS KDSEDEEEVD SDGEDGDDSR DATMDSPSKA ERLQAQRREK AERSEARKHE
KSARDAKLSS TRDGLNRSKL ADSMKRFSYL LGQTELFQHF IDIKKDRDPE FAKLLEQTQS
KAKKGKKGGA GEARRRKTEK EEDEELLGED EQEEEAFVFD ESPAYVKGGK MRDYQVQGLN
WMISLYQHGI NGILADEMGL GKTLQTISFL GWLKFYRDTP RFHLIVVPKS TLDNWKRELE
NWVPGFKVVS LQGDKEARQE LIQSHLLTQD FDILLTTYEM CLREKGALKR LSWEYIVIDE
AHRIKNVDSM LSQIVRMFNS RSRLLITGTP LQNNLMELWS LLNFLLPDVF SNSEDFESWF
KEKGEEAQDQ VVQQLHKVLR PFLLRRVKSD VEKSLLPKKE INVFVGLTEM QRKWYKSILE
KDIDAVNGVG SKKEGKTRLL NIVMQLRKCC NHPYLFDGAE PGPPFTTDEH LVYNSDKMII
LDKLLKSMKA KGSRVLIFSQ MSRVLDILED YCLFREYQYC RIDGSSAHED RISAIDEYNK
PGSEKFVFLL TTRAGGLGIN LTTADVVVLF DSDWNPQADL QAMDRAHRIG QTKQVYVFRF
VTEHAIEERI LERAAQKLRL DQLVIQQGRT QPKNAQQSKD ELVDMIQHGA EKIISSKESM
LIDDDIDKII ANGEERTKKL QEKYNDLNLD DLNNFKSEST LEWEGQDFRN RPGVKGLWIE
PSKRERKGAV SYSVDDYYRE AMSTKKPSAP KAPRAPRQVT IYDYQFYPLE LAELQRRETA
AYQRSIGYRV PSKQASTAEG ADPSTSEEER KKEQEFIDTA EPLTEEETQR KETLALQGLA
DWNRRDFQAF VRGCEKYGRN DFAAITEEVG EAKTERDVKA YSKVFWERIE ELNDHEKIIQ
RIEEGEKKRE KVAHLEEMLK KRVEACKMPQ HQLKINYGTG TAKGKGWSED EDRFLLIRLA
KHGLVDDAYD RIRQDIGQSD LFRFDWFIRS RTPLELNRRC NTLVSLLQKD DADAAANSGK
AGGAATKKRT ADALANGDGA GSSRGSTPAG GSKTSKKKKT
//
