ID A0A4V6WK34_9PEZI Unreviewed; 1097 AA.
AC A0A4V6WK34;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A54_10760 {ECO:0000313|EMBL:TKA38469.1};
OS Friedmanniomyces endolithicus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Friedmanniomyces.
OX NCBI_TaxID=329885 {ECO:0000313|EMBL:TKA38469.1, ECO:0000313|Proteomes:UP000310066};
RN [1] {ECO:0000313|EMBL:TKA38469.1, ECO:0000313|Proteomes:UP000310066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5311 {ECO:0000313|EMBL:TKA38469.1,
RC ECO:0000313|Proteomes:UP000310066};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:TKA38469.1}.
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DR EMBL; NAJP01000045; TKA38469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V6WK34; -.
DR STRING; 329885.A0A4V6WK34; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000310066; 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; 3.40.50.300: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; 3.40.50.10810:FF:000002; ISWI chromatin-remodeling complex ATPase CHR11 isoform A; 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; 1.10.1040.30; 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:UP000310066};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 182..347
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 478..629
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..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 125220 MW; EF1ECEF1BFD01669 CRC64;
MSGATAVGAG DGAMADTHML DTPDYTDSES NPTGANSVAG DAHDGRKRRW EGNALRKSMF
GKKHDRLGEN KDDDTIKRFR YLLGLTDLFR HFIDRNPDPK IRDIMVEIDR QDRADEVKAA
GNKRKGGAAG GRRRTEKEED AELLRQGKQA GKEEHHVFHE SPSFIQGGEM RDYQVAGLNW
LISLHENGIS GILADEMGLG KTLQTISFLG YLRFVQGISG PHLIVVPKST LDNWARECAR
WIPELNILVL QGAKEERHEL IQDRLVDEKF DVCVTSYEMI LREKSHLKKF AWEYIIIDEA
HRIKNEESSL AQIIRVFNSR GRLLITGTPL QNNLHELWAL LNFLLPDVFG DAEAFDQWFS
AQNADQDAVV QQLHRVLRPF LLRRVKSDVE KSLLPKKEVN LYVGMSEMQI KWYKNILEKD
IDAVNGAGGK KESKTRLLNI VMQLRKCCNH PYLFDGAEPG PPYTTDEHLV DNAAKMVMLD
KLLKKMAAQG SRVLIFSQMS RVLDILEDYS VMRGFKYSRI DGSTAHEDRI AAIDEYNKPQ
SEKFLFLLTT RAGGLGINLT SADIVVLFDS DWNPQADLQA MDRAHRIGQT KQVYVYRFVT
ENAIEEKVLE RAAQKLRLDQ LVIQQGRAQQ QAKQAASKDE LLGMIQHGAE TIFESGEGYG
AFGKKGEDGE SELDELLRRG EERTKEMSKK YETLGLDDLQ KFSMEGASAY EWNGETFVSK
KKELGISWIN PSKRERKEQS YSMDKYYRNA LMTGGPRPDP KPKVPRAPKQ MAMHDYQFFD
PRLGLLQDKE TAWFRKENGL KAPLPDGEDD AMEQRLEDQA LEQRTIDEAE PLTEEETAEK
ERLSLLGFGD WNKRDFQQFV NGSGKFGRKA FEQIAVEVDS KTVKEVKDYS QVFWKRYKEI
HNWEKHYHAI VDGEQRTQRV IEQRSMLSRK MKMYRVPLQQ LKLSYTVSTT NKKVYTEEED
RFLLVMLHKH GIDTEGLYEK LRDEIRESPL FRFDWFFLSR TPQELSRRCA TLITTVTREM
EGGNGKENKR VAEEVDEEEE EVEKPAPKKG RVSGGAAKNK AVNGVKKGTP NGDSRAASED
TVASAGAAKP KSRSRKK
//
