ID L8FYC6_PSED2 Unreviewed; 1122 AA.
AC L8FYC6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GMDG_07464 {ECO:0000313|EMBL:ELR05544.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR05544.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; GL573395; ELR05544.1; -; Genomic_DNA.
DR RefSeq; XP_012745917.1; XM_012890463.1.
DR AlphaFoldDB; L8FYC6; -.
DR STRING; 658429.L8FYC6; -.
DR VEuPathDB; FungiDB:GMDG_07464; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; L8FYC6; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000011064; 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; 1.20.5.1190; iswi atpase; 1.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011064}.
FT DOMAIN 201..366
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 497..648
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 864..916
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 127819 MW; ABA083751002ECD2 CRC64;
MAPSRSGRLS GADTDSSMAD ASDLNIKLRV DAMDIDETPD YTEDSDTNPN TTASSVAGEP
VDGRRRRSEA TQLRRSVFGK KHDRLGQSQE DDSIRRFRYL LGLTDLFRHF IETNPNPHIK
QIMVEIDRQN EEAAEAKAKK ASRAGGAANE RRRRTEAEED AELLKDEKQG GSADTVFRES
PGFVKGGTMR DYQVAGLNWL ISLHENGISG ILADEMGLGK TLQTIAFLGY LRHIMDITGP
HLVIVPKSTL DNWKREFAKW TPEVNVLVLQ GAKDERNLLI NERLVDEKFD VCITSYEMIL
REKSHLKKFA WEYIIIDEAH RIKNEESSLA QVIRLFNSRN RLLITGTPLQ NNLHELWALL
NFLLPDVFGD SEAFDQWFSG QGADQDTVVQ QLHRVLRPFL LRRVKSDVEK SLLPKKEVNL
YIGMSDMQVK WYKKILEKDI DAVNGAGGKR ESKTRLLNIV MQLRKCCNHP YLFEGAEPGP
PYTTDEHLVV NAGKMVMLDR LLGRLQKQGS RVLIFSQMSR LLDILEDYCV FREFKYCRID
GSTAHEDRIA AIDDYNKPGS KKFVFLLTTR AGGLGINLTS ADIVVLYDSD WNPQADLQAM
DRAHRIGQTK QVVVYRFVTE NAIEEKVLER AAQKLRLDQL VIQQGRAQIA AKAAANKDEL
LNMIQHGAEK VFNTKGATGI LAQKGAEIGD DDIDEILKHG EKRTAELNAR YEKLGIDDLQ
KFTSESAYEW NGQDFTNKKK EIGISWINPA KRERKEQSYS MDQYYKQALS TGGRTADAKP
KAPRAPKQIV IHDYQFFPPM LQDLQDRETA YFRKEIGYKV PLPDGSEEDL SDREGERALD
QQEIDNATPL TEEEQAEKLR LSEQGFGDWN KRDFQQFING SAKYGRKNYD AIAEEVDNKT
TAEVKTYAQI FWKRYTDLND YSKYINLVEA GEEKTKKIEH QRQMLKRKMS QYRVPLQQLK
VNYSVSTTNK KVYTEEEDRF LLVLLDRFGI DSENIHERIR DEIRESPLFR FDWFFLSRTP
LEISRRCTTL LTTVAREYEE TQPKANGANG KTKREPEEED NDEESVHDTA PAKKKSKNVK
NKAIDSLKPG SKATSAAPSS RASSVGSPAP APSKSKAKGK KK
//