ID A0A150UZ40_9PEZI Unreviewed; 1099 AA.
AC A0A150UZ40;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_156602 {ECO:0000313|EMBL:KYG43538.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG43538.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG43538.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG43538.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYG43538.1}.
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DR EMBL; JPDO01000306; KYG43538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150UZ40; -.
DR STRING; 766039.A0A150UZ40; -.
DR Proteomes; UP000075602; 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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT DOMAIN 185..350
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 481..632
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 849..901
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 126502 MW; 1E833653533404A8 CRC64;
MSGVNALGAG DGTVPDLNML DTPDYTDSES NPTGANSVAG DVVHSDGRKR RWEGNQLRKS
MFGKKHDRLG ESKDDDSIRR FRYLLGLTDL FRHFIDTNPN PRIREIMAEI DRQDTEQQTQ
AAGNKRKGGA SGDRRRRTEK EEDAELLRQG KKDGKEEQTI FRESPSFIQG GKMRDYQIAG
LNWLISLHEN GISGILADEM GLGKTLQTIS FLGYLRFVQG ITGPHLIAVP KSTLDNWRRE
FEKWIPEINV LVLQGAKDER HELINDRLID EKFDVCITSY EMILREKSHL KKFAWEYIII
DEAHRIKNEE SSLAQIIRIF NSRNRLLITG TPLQNNLHEL WALLNFLLPD VFGDSEVFDN
WFSSQSEDQD TVIQQLHRVL RPFVLRRVKS DVEKSLLPKK EINLYVGMSE MQIKWYKNIL
EKDIDAVNGA GGKKESKTRL LNIVMQLRKC CNHPYLFDGA EPGPPYTTDE HLVDNAAKMV
MLDKLLKRLK SQGSRVLIFS QMSRVLDILE DYSVMRGYQY CRIDGSTAHE DRIAAIDEYN
KPGSEKFLFL LTTRAGGLGI NLTSADIVIL FDSDWNPQAD LQAMDRAHRI GQTKQVVVFR
FVTEKAIEEK VLERAAQKLR LDQLVIQQGR AQQQAKQAAS KDELLGMIQH GAEKIFEQKE
GMGIFGKGGD ITETELDEIL RQGEERTKEM NAKYEKLGLD DLQKFTTEAA GAYEWNGESF
VNRKKEIGLS WINPSKRERK EQSYSMDKYY RNALATGGPR PEPKPKVPRA PKQMAMHDYQ
FFDRRLEDLQ EKETAWFRKE NGIKAPLNDG DEESLQQRLE DQEIEQKMID EAEPLTEEEI
AEKEQLSQEG FGDWNKRDFQ QFINGSAKYG RYNYEDIALE VDSKSPKEIK EYAKVFWKRY
KEIQNWEKHI AAIKEGEDRK QRVLEQREML HKKIKMYRVP LQQLKLNYTV STTNKKVYTE
EEDRFLLVML DKYGLDTEGL YERIRDEIRE SPLFRFDWFF LSRTPQELSR RCATLITTVT
REMEGGVTGK ENKRHVEEVD DEDDEDKPMP KKGRASGGAA KNKVVNGVKG TPNGASRAAS
EDTVASGNVT KSKGRGRKK
//