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Database: UniProt
Entry: L8FYC6_PSED2
LinkDB: L8FYC6_PSED2
Original site: L8FYC6_PSED2 
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
//
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