ID A0A0F4ZG47_9PEZI Unreviewed; 1122 AA.
AC A0A0F4ZG47;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 40.
DE RecName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TD95_001584 {ECO:0000313|EMBL:KKA29502.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29502.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA29502.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29502.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-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:KKA29502.1}.
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DR EMBL; LAEV01000801; KKA29502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZG47; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000033483; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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; PS00690; DEAH_ATP_HELICASE; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000033483}.
FT DOMAIN 183..348
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 479..630
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 846..898
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 813..847
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 43..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 127330 MW; 6BBF24E16EE98A2A CRC64;
MPTRSSRPNE PGSDASMADA PEHSANDSMD VDDNSGSESQ STEATDGRKK RGEANQLRKS
VFGKKLDSLG ESKEDDTIRR FRYLLGLTDL FRHFIEANPD PKIREIMREI DRQNDEAAKS
KKASGRQGGA STDRRRRTEA EEDAELLKDE KDGTSAETIF RESPSFIQGT MRDYQVAGLN
WLVSLHENGI SGILADEMGL GKTLQTISFL GYLRHIMGVN GPHLILTPKS TLDNWKREFG
KWTPEVNVLV LQGSKEERQN LINGRLAEED FDVCIASYEI VLREKAHLRK FAWGYIIIDE
AHRIKNEESS LAQVVRLFNS RNRLLITGTP LQNNLHELWA LLNFLLPDVF GDSEAFDQWF
KGEDRDQDAV VKQLHRVLQP FLLRRVKADV EKSLLPKKEL NVYIGMSEMQ VKWYQKILEK
DIDAVNGAGG KRESKTRLLN IVMQLRKCCN HPYLFEGAEP GPPYTTDEHL VENSGKMVVL
DKLLERMRKQ DSRVLIFSQM SRQLDILEDY CVFRGYKYCR IDGGTAHEDR IAAIDEYNKP
GSEKFIFLLT TRAGGLGINL TTADIVVLYD SDWNPQADLQ AMDRAHRIGQ TKQVVVYRFV
TDKAIEEKVL ERAAQKLRLD QLVIQQGRSQ AAAKAAANKD ELLSMIQHGA QDLFNTKGAT
GVIGEKGGKI DDNDIDDILS RGEARTKELN AKYEKLGLDD LQNFTSESAY EWNGENFSKK
KNEEISMAWI EPAKRERKEQ SYSMDKYFKQ AMYPTAAKAE AKPKAPRAPK QVSAHDYQFY
PPRLRDLQER ETAFYRKEIG YKVPLSDGDA STLEEREKER VREQQEIDNA VALTAEEQEE
KQELAEQGFD WNRRDFQQFI NGSAKYGRHN IEGIAQEVDS KTPAEVRAYA KAFWQRHTEI
ADYAKYLKII EDGEERTRKI EHQRKLLRKK LNMYRVPLQQ LKINYSVSTT NKKVYTEEED
RFLLVLLDRF GIDREGIYEL MREEIRESPL FRFDWFFLSR TPVELSRRCT TLLTAVVKEF
EDAGSNKGNG ASANGANGKT KREDSDNDED SALELAPAKK KARSSGANGV KNKALDSIKS
TGGSSSKATS ATPSRASSVA STASTNAGSA STSKAKTKAK RK
//