ID A0A161Y0A6_9PEZI Unreviewed; 1120 AA.
AC A0A161Y0A6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 43.
DE SubName: Full=Chromatin remodelling complex atpase chain isw1 {ECO:0000313|EMBL:KZL82892.1};
GN ORFNames=CI238_05348 {ECO:0000313|EMBL:KZL82892.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL82892.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL82892.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL82892.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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}.
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:KZL82892.1}.
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DR EMBL; LFIW01001266; KZL82892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161Y0A6; -.
DR STRING; 1573173.A0A161Y0A6; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:TreeGrafter.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0034728; P:nucleosome organization; IEA:TreeGrafter.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.10810:FF:000036; Chromatin remodelling complex ATPase chain; 1.
DR FunFam; 3.40.50.300:FF:000082; ISWI chromatin remodeling complex ATPase ISW1; 1.
DR FunFam; 1.10.10.60:FF:000022; ISWI chromatin-remodeling complex ATPase CHR11 isoform A; 1.
DR FunFam; 1.20.5.1190:FF:000005; ISWI chromatin-remodeling complex ATPase ISW1; 1.
DR FunFam; 1.10.10.60:FF:000234; ISWI chromatin-remodeling complex ATPase ISW2; 1.
DR FunFam; 1.10.1040.30:FF:000003; ISWI chromatin-remodeling complex ATPase ISW2; 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-like.
DR InterPro; IPR009057; Homeodomain-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 5; 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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1060
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1112
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 128254 MW; 1ACA12ACB7CF9A83 CRC64;
MAPRSRAAAV DTDASMSDVA DTRPVEGMEV DETPDYTDSD TNANTTASSV AGEPLGDGRK
RRSEANQLRR SIFGKKHDRL GESKEEDSIR RFRYLLGLTD LFRHFIETNP NPKIREIMTE
IDRQNAEASK SKKKGSRQGG ASNERVRRTE AEEDAELLQD EKHGGSAETV FRESPAFIKG
QMRDYQVAGL NWLISLHENG ISGILADEMG LGKTLQTIAF LGYLRHIMDI TGPHIVIVPK
STLDNWKREF EKWTPEVNVL VLQGAKEERN ALINDRLVNE DFDVCITSYE MVLREKSHLK
KFAWEYIIID EAHRIKNEES SLAQVIRVFN SRNRLLITGT PLQNNLHELW ALLNFLLPDV
FGDSEAFDQW FSGREQDQDT VVQQLHRVLR PFLLRRVKSD VEKSLLPKKE VNVYLGMSDM
QVKWYQKILE KDIDAVNGAN GKRESKTRLL NIVMQLRKCC NHPYLFEGAE PGPPYTTDEH
LIFNAGKMVV LDKLLARMRK QGSRVLIFSQ MSRLLDILED YCVFREYKYC RIDGGTAHED
RIAAIDEYNK PGSEKFIFLL TTRAGGLGIN LTTADIVVLY DSDWNPQADL QAMDRAHRIG
QTKQVVVYRF VTDNAIEEKV LERAAQKLRL DQLVIQQGRA QVAAKAAANK DELLSMIQHG
AEKVFQNKGA SGVLADKGAD LDDDDIDKIL ASGESRTKEL NAKYEKLGID DLQNFTSESA
YTWNGEDFKT NKKDIGMNWI NPAKRERKEQ SYSMDKYFRQ TMYPPKEKDT KPKAPRAPKQ
VPVHDYQFYP PRLRDLQDRE TAYYRKEIGY KVPLADGDDE NLDEREAERA LDQQEIDNAT
PLTEEEQEEK QRLSQQGFGE WNRRDFQQFI NASGRYGRTD YESIAEDIDN KTAAEVKQYA
KVFWQRYTEI ADYNKYIKVI EDGEERMRKI EHQRKLLRKK MSQYRVPLQQ LKINYSVSTT
NKKVYTEEED RFLLVLLDKY GIDSPGLYEK MRDEIAESPL FRFDWFFLSR TPVELSRRCT
TLLTTIVKEF EDVHPTKGAN GVNGKVKREA ADDEENDEDS ILGMAPAKKK SKNGVKNKAL
DNVKSEVGSK NTSAAPSRAS SVASTKSATN AKSKTKGKKK
//
