ID W6MQZ7_9ASCO Unreviewed; 993 AA.
AC W6MQZ7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 13-SEP-2023, entry version 50.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=KUCA_T00005103001 {ECO:0000313|EMBL:CDK29116.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK29116.1};
RN [1] {ECO:0000313|EMBL:CDK29116.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29116.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK29116.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29116.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
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}.
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DR EMBL; HG793130; CDK29116.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MQZ7; -.
DR STRING; 1382522.W6MQZ7; -.
DR HOGENOM; CLU_000315_0_0_1; -.
DR OrthoDB; 5482994at2759; -.
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; 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; 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}.
FT DOMAIN 66..231
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 362..513
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 743..795
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 114874 MW; 758FF52B07044394 CRC64;
MKKSNAASAK KSKKQTGRRR KTEREEDEEL MHDEEFEEET TVITESPSYI HGTLREYQVQ
GLNWLISLYE NRLSGILADE MGLGKTLQTI SFLGHLRYNK QIDGPFLVLV PKSTLDNWRR
EFAKWTPDVN VLVLQGTKEE RAELIANRLL QADFDVCITS FEMVLREKSK LGKIRWEYVV
IDEAHRIKNE ESSLSQIIRL FYSRNRLLIT GTPLQNNLHE LWALLNFILP DVFGDSEAFD
QWFETQDQDQ DQVVQQLHKV LAPFLLRRVK ADVEKSLLPK KEVNVYVGMS DMQVKWYKNL
LEKDIDAVNG IVGKREGKTR LLNIVMQLRK CCNHPYLFEG AEPGPPYTTD EHLVFNSGKM
VVLDKLLKRL KEQGSRVLIF SQMSRLLDIL EDYCFFREYE YSRIDGSTSH EDRIQAIDDY
NDPDSKKFIF LLTTRAGGLG INLTSADCVV LYDSDWNPQA DLQAMDRAHR IGQKKQVKVF
RFVTENAIEE KVLERAAQKL RLDQLVIQQG RSNNAKSGAT IGNNKDDLLG MIQHGAQKVF
ESNGSTMQED DIDKILSKGE EKTATLNAKY SKLGLDDLQN FTSDSAYEWN GENFAKKQHG
PLLPWMNPTK RERKEHQYSV DGYYKDVMQS FKGTPGARGQ RNPRAPKQVL TLDFQFYPPE
LAKLLEKEQL WYKKKIGYKV PSPESDSDDD EFLVSEDEAE KLPKTKESKN SKAERRKREQ
KKIDSAEEFT EEDGELKEKL LLQGFGDWSK RDFTNFVHVC ARYGRGNIGA IASEMKGKSV
ADVKRYAETF KERFKEIEGY DRYISQIEQG EQKLNKLQHQ EQLLAVKIKQ YEAPLQELTI
QYPPNNSKRV YSDLEDRFLL VTVNKYGLSR HNLYELVKEE IVDSGLFRFD WFFLSRTPQE
LGRRCTTLLL AITREIEGPD AFKRRKNGSS LLATNANSNE PSRQQSMEVD DESLDVESTF
DEKENEDSKQ KPSRKRLIVR SNTSTPVSKR IKV
//