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Database: UniProt
Entry: A0A150UZ40_9PEZI
LinkDB: A0A150UZ40_9PEZI
Original site: A0A150UZ40_9PEZI 
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
//
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