ID L2GC39_COLFN Unreviewed; 1121 AA.
AC L2GC39;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Chromatin remodelling complex atpase chain isw1 {ECO:0000313|EMBL:ELA35603.1};
DE SubName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0000313|EMBL:KAF4474911.1};
GN Name=ISW2 {ECO:0000313|EMBL:KAF4474911.1};
GN ORFNames=CGGC5_4687 {ECO:0000313|EMBL:ELA35603.1}, CGGC5_v015691
GN {ECO:0000313|EMBL:KAF4474911.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA35603.1};
RN [1] {ECO:0000313|EMBL:ELA35603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA35603.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF4474911.1, ECO:0000313|Proteomes:UP000011096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4474911.1,
RC ECO:0000313|Proteomes:UP000011096};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF4474911.1, ECO:0000313|Proteomes:UP000011096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:KAF4474911.1,
RC ECO:0000313|Proteomes:UP000011096};
RA Gan P., Shirasu K.;
RT "Genome sequencing and assembly of multiple isolates from the
RT Colletotrichum gloeosporioides species complex.";
RL Submitted (APR-2020) 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; KB020561; ELA35603.1; -; Genomic_DNA.
DR EMBL; ANPB02000010; KAF4474911.1; -; Genomic_DNA.
DR RefSeq; XP_007275337.1; XM_007275275.1.
DR AlphaFoldDB; L2GC39; -.
DR STRING; 1213859.L2GC39; -.
DR EnsemblFungi; ELA35603; ELA35603; CGGC5_4687.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; L2GC39; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000011096; 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:UP000011096}.
FT DOMAIN 195..360
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 491..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 857..909
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 128628 MW; 9B329FE0F2AD4645 CRC64;
MAPSRSRAAV VDTDASMSDA PEVNHAEEME VDETPDYTDS DTNPNTTASS VAGEPVGDGR
KRRSEANQLR RSIFGKKHDR LGESKEEDSI RRFRYLLGLT DLFRHFIETN PNPKIREIMT
EIDRQNAEAS KSKKGGARQG GANNERRRRT EAEEDAELLR DEKHGGSAET VFRESPAFIQ
GTMRDYQVAG LNWLISLHEN GISGILADEM GLGKTLQTIS FLGYLRHIMD ITGPHIVIVP
KSTLDNWKRE FEKWTPEVNV LVLQGAKEER HNLINDRLVS EDFDVCITSY EMVLREKAHL
RKFAWEYIII DEAHRIKNEE SSLAQVIRLF NSRNRLLITG TPLQNNLHEL WALLNFLLPD
VFGDSEAFDQ WFSGQDRDQD TVVQQLHRVL RPFLLRRVKS DVEKSLLPKK EVNVYLGMSE
MQIKWYQKIL EKDIDAVNGA NGKRESKTRL LNIVMQLRKC CNHPYLFEGA EPGPPYTTDE
HLVYNAGKMV VLDKLLNRMQ KQGSRVLIFS QMSRLLDILE DYCVFRQYKY CRIDGGTAHE
DRIAAIDEYN KPGSEKFIFL LTTRAGGLGI NLTTADIVVL YDSDWNPQAD LQAMDRAHRI
GQTKQVVVYR FVTDNAIEEK VLERAAQKLR LDQLVIQQGR AQTAAKAAAN KDELLSMIQH
GAEKVFQSKG ATGSLASKGA DVEEDDIDEI LASGETRTKE LNAKYEKLGI DDLQNFTSES
AYTWNGEDFK TNKKDIGMNW INPAKRERKE QSYSMDKYFR QTMYPPKEKD NKPKAPRAPK
QVPVHDYQFY PVRLRELQDR ETAYYRKEIG YKVPLPDGED DKLEEREQER ALDQQEIDDA
TPLNEEELEE KQRLSQQGFG EWNRRDFQQF INASGRYGRN DYESIAEDIN DKTAAEVKQY
AKVFWQRYTE IADYNKYIKV IEDGEERMRK IEHQRKLLRK KMSQYRVPLQ QLKINYSVST
TNKKVYTEEE DRFLLVLLDK FGIDSPGLYE KMRDEISVSP LFRFDWFFLS RTPVELSRRC
TTLLTTIVKE FEDVHPTKGA NGVNGKVKRE AADDEENDED SILGMAPAKK KAKNGVKNKA
LDNVKSEAGS KNTSAAPSRA SSVASTKSTT NAKSKTKGKK K
//
