ID A0A135V6M6_9PEZI Unreviewed; 1119 AA.
AC A0A135V6M6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=SNF2 family domain-containing protein {ECO:0000313|EMBL:KXH68171.1};
GN ORFNames=CSAL01_02092 {ECO:0000313|EMBL:KXH68171.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH68171.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH68171.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH68171.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) 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:KXH68171.1}.
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DR EMBL; JFFI01000374; KXH68171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135V6M6; -.
DR STRING; 1209931.A0A135V6M6; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000070121; 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:UP000070121}.
FT DOMAIN 194..359
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 490..641
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 856..908
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 128327 MW; 2BFC5E3F705C634F CRC64;
MAPRSRAAAV DTDASMSDAA DAHPVEEMEV DETPDYTDSD TNANTTASSV VGEPLGDGRR
KRSEANQLRR SIFGKKHDRL GESKEEDSIR RFRYLLGLTD LFRHFIETNP NPKIREIMTE
IDRQNAEASK SKKKGSRQGG ASNERVRRTE AEEDAELLRD EKHGGSAETV FRDSPAFVQG
QMRDYQIAGL NWLISLHENG ISGILADEMG LGKTLQTISF LGYLRHIMDI TGPHIVIVPK
STLDNWKREF ERWTPEVNVL VLQGAKDERQ ALINDRLVNE DFDVCITSYE MVLREKNHLK
KFAWEYIIID EAHRIKNEES SLAQVIRLFN SRNRLLITGT PLQNNLHELW ALLNFLLPDV
FGDSEAFDQW FSGREQDQDT VVQQLHRVLR PFLLRRVKAD VEKSLLPKKE VNVYLGMSDM
QIKWYQKILE KDIDAVNGAN GKRESKTRLL NIVMQLRKCC NHPYLFEGAE PGPPYTTDEH
LVYNAGKMAV LDKLLARMQK QGSRVLIFSQ MSRLLDILED YCVFREYKYC RIDGGTAHED
RIAAIDEYNK PGSEKFIFLL TTRAGGLGIN LTTADIVVLY DSDWNPQADL QAMDRAHRIG
QTKQVVVYRF VTDNAIEEKV LERAAQKLRL DQLVIQQGRA QVAAKAANNK DELLSMIQHG
AEKVFQSKSA GGTLASKGTD LDDDDIDKIL SSGESRTKEL NAKYEKLGID DLQNFTSESA
YTWNGEDFKT NKKEIGMNWI NPAKRERKEQ SYSMDKYFRQ AMYPPKEKDT KPKAPRAPKQ
VPVHDYQFYP PRLRDLQDRE TAYYRKEIGY KVPLSDGDDE NLDEREAERA LDQQEIDEAT
PLNEEELEEK QRLSQQGFGE WNRRDFQQFI NASGRYGRND YANIAEDIDN KTASEVKQYA
KVFWQRYTEI ADYNKYIKVI EDGEERMRKI EHQRKLLRKK MSQYRVPLQQ LKINYSVSTT
NKKVYTEEED RFLLVLLDKY GIDSAGLYEK MRDDIAESPL FRFDWFFLSR TPVELSRRCT
TLLTTIVKEF EDVHPTKGAN GVNGKLKREA EDEENDEDSI LGMAPSKKKT KNGVKNKALD
NVKSEVGSKN TSAAPSRASS VASNKSATNA KSKTKGKKK
//