ID A0A376B5B2_9ASCO Unreviewed; 1170 AA.
AC A0A376B5B2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Related to ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0000313|EMBL:SSD59831.1};
GN ORFNames=SCODWIG_01592 {ECO:0000313|EMBL:SSD59831.1};
OS Saccharomycodes ludwigii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Saccharomycodes.
OX NCBI_TaxID=36035 {ECO:0000313|EMBL:SSD59831.1, ECO:0000313|Proteomes:UP000262825};
RN [1] {ECO:0000313|Proteomes:UP000262825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTAD17 {ECO:0000313|Proteomes:UP000262825};
RA Guldener U.;
RL Submitted (JUN-2018) 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; UFAJ01000213; SSD59831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A376B5B2; -.
DR VEuPathDB; FungiDB:SCODWIG_01592; -.
DR Proteomes; UP000262825; 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; 1.10.1040.30; 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; 2.
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; PS50090; MYB_LIKE; 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:UP000262825}.
FT DOMAIN 153..318
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 451..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 958..1010
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 961..1010
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 736..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..855
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 135137 MW; 7C509F454DD8D8CA CRC64;
MNTQENKETL AERKKRYILE HDAKFEKLKD KNDTVGRFKY LLDLTDLFRH FITVRAKNDK
NIQLLLKSLD STSKKTSDNN FRMKKKGIDH TKGRHRKTEK EEDQEILMME EDSELEDNDD
VIPHEYEFFN ESPTYIKDGK LRDYQVQGLN WLISLHKNKL SGILADEMGL GKTLQTISFL
GYLRYVNKID GPFLIIAPKS TLDNWKREFA KWTPDINVVV LQGDKDERHA LISNVIMQAN
FDVVIASFEI VLREKNALKK ICWQYLVVDE AHRIKNEQSA LSQIIRLFYS KSRLLITGTP
LQNNLHELWA LLNFLLPDVF GDSALFDEWF NNSESEQDQD LIVQQLHTIL SPFLLRRIKA
DVEKSLLPKI ETNVYVGMTD MQLKWYKMLL EKDIDAVNGA VGKREGKTKL LNIVMQLRKC
CNHPYLFEGA EPGPPYTNDE HLVFNSGKMI ILDKLLEKKM EQGSRVLIFS QMSRLLDILE
DYCYLRGYEY CRIDGSTAHE DRIKAIDDYN APNSKKFIFL LTTRAGGLGI NLVTADTVIL
YDSDWNPQAD LQAMDRAHRI GQKKQVHVFR FVTEHAIEEK VIERAAQKLR LDQLVIQQGS
ANNGVGAASS KNSLANSKDD LLDMIQYGAR DVFDNKAVKI SSDADIDKIL KKGEQKTKEL
NAKYQALGLD DLQKFNGLSE HSAYEWNGTN FQKKKVASPL ETWINPSKRE RKRRNDIQSY
SVDDYYREVM HKASNSYNKS KDDNDAEHGG SNNNNNGDHS FSQGRAPRAP KGTLMTDYQF
FPQEIKELDE KELLYFKRKS KYKVTKYDIM DDVNITNDDE DDEEDDEEDE DEDDVDDDEA
DGGEVDDDET AVDETNDGTD IAAELGDDSK GGNRSITATE TPCSALNGSN EGGNKNEEQG
KNVEGDAGEK EKNNKIGSRT EEVELSLDDK IKLEQEKIDN ASEFTEDDNK KRQELIQQGF
SNWSKREFTT LVNAMAKFGK DQYKSIASML TNKTEDDVRN YCKVFWERYK EINGYEKYIS
LINKNEKKLK LLRHQELLLK QKMENCKSPI HDFNIQYPPN NARRTYNTLE DRFILMHVVK
YGLFSENVFE IIRQDILSSS LFQFDWFIKT RTAHELSKRV YTLLTIITRE IEGPESNNAT
KRKKAKTKEN ISSLNNSNKQ QYSNKKVKTE
//
