ID Q6DFM0_XENLA Unreviewed; 1046 AA.
AC Q6DFM0;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=ISWI protein {ECO:0000313|EMBL:AAH76715.1};
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 S homeolog {ECO:0000313|RefSeq:NP_001083868.1};
GN Name=smarca5.S {ECO:0000313|RefSeq:NP_001083868.1,
GN ECO:0000313|Xenbase:XB-GENE-866389};
GN Synonyms=ISWI {ECO:0000313|EMBL:AAH76715.1}, iswi
GN {ECO:0000313|RefSeq:NP_001083868.1}, smarca5
GN {ECO:0000313|RefSeq:NP_001083868.1,
GN ECO:0000313|Xenbase:XB-GENE-866389}, SNF2H
GN {ECO:0000313|RefSeq:NP_001083868.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH76715.1, ECO:0000313|Proteomes:UP000186698};
RN [1] {ECO:0000313|RefSeq:NP_001083868.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10942776; DOI=10.1074/jbc.M006041200;
RA Guschin D., Geiman T.M., Kikyo N., Tremethick D.J., Wolffe A.P., Wade P.A.;
RT "Multiple ISWI ATPase complexes from xenopus laevis. Functional
RT conservation of an ACF/CHRAC homolog.";
RL J. Biol. Chem. 275:35248-35255(2000).
RN [2] {ECO:0000313|RefSeq:NP_001083868.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [3] {ECO:0000313|EMBL:AAH76715.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000313|EMBL:AAH76715.1};
RA Tajne S.S.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001083868.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16169710;
RA Dirscherl S.S., Henry J.J., Krebs J.E.;
RT "Neural and eye-specific defects associated with loss of the imitation
RT switch (ISWI) chromatin remodeler in Xenopus laevis.";
RL Mech. Dev. 122:1157-1170(2005).
RN [5] {ECO:0000313|RefSeq:NP_001083868.1, ECO:0007829|PDB:2NOG}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 747-909 IN COMPLEX WITH
RP MAGNESIUM.
RX PubMed=17377988; DOI=10.1002/prot.21352;
RA Horton J.R., Elgar S.J., Khan S.I., Zhang X., Wade P.A., Cheng X.;
RT "Structure of the SANT domain from the Xenopus chromatin remodeling factor
RT ISWI.";
RL Proteins 67:1198-1202(2007).
RN [6] {ECO:0000313|RefSeq:NP_001083868.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20008562;
RA Yokoyama H., Rybina S., Santarella-Mellwig R., Mattaj I.W., Karsenti E.;
RT "ISWI is a RanGTP-dependent MAP required for chromosome segregation.";
RL J. Cell Biol. 187:813-829(2009).
RN [7] {ECO:0000313|RefSeq:NP_001083868.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26116984;
RA Eastlund A., Al-Ani G., Fischer C.J.;
RT "Low processivity for DNA translocation by the ISWI molecular motor.";
RL Biochim. Biophys. Acta 1854:1487-1493(2015).
RN [8] {ECO:0000313|RefSeq:NP_001083868.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; BC076715; AAH76715.1; -; mRNA.
DR RefSeq; NP_001083868.1; NM_001090399.1.
DR PDB; 2NOG; X-ray; 2.00 A; A/B=747-910.
DR PDBsum; 2NOG; -.
DR IntAct; Q6DFM0; 2.
DR DNASU; 399165; -.
DR GeneID; 399165; -.
DR KEGG; xla:399165; -.
DR AGR; Xenbase:XB-GENE-866389; -.
DR CTD; 399165; -.
DR Xenbase; XB-GENE-866389; smarca5.S.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 399165; Expressed in blastula and 19 other cell types or tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd00167; SANT; 2.
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; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2NOG};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0007829|PDB:2NOG};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT DOMAIN 185..350
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 480..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 833..885
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 806..833
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 862
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:2NOG"
FT BINDING 865
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:2NOG"
FT BINDING 868
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:2NOG"
SQ SEQUENCE 1046 AA; 122078 MW; 43AE9E81FAD06B26 CRC64;
MSAESTEQQP DTVVKEEKEG KDPMEVDSGD GKKQEQDGEA VKEEAMEDGE PDDDDDDDDS
LKSKEGNEMD PAYEKKRKTD RSNRFDYLLK QTELFAHFIQ PAAQKTPTSP LKMKPGRPRL
KKDEKQDLLS AGDNRHRRTE QEEDEELLTE SSKTTNVCTR FEDSPAYVKS GKLRDYQVRG
LNWLISLYEN GINGILADEM GLGKTLQTIS LLGYMKHYRS IPGPHMVLVP KSTLHNWMAE
FKRWVPSLCA VCLIGDKDHR AAFVRDVLLP GEWDVCVTSY EMLIREKSVF KKFNWRYLVI
DEAHRIKNEK SKLSEIVREF KTTNRLLLTG TPLQNNLHEL WALLNFLLPD VFNSSEDFDS
WFDTNNCLGD QKLVERLHMV LKPFLLRRIK ADVEKSLKPK KEIKIYVGLS KMQREWYTKI
LMKDIDILNS SGKTDKMRLL NILMQLRKCC NHPYLFDGAE PGPPYTTDLH LATNSGKMMV
LDKLLPKLKE QDSRVLIFSQ MTRVLDILED YCMWRNYEYC RLDGQTPHEE RQESIIAYNA
PGSTKFIFML STRAGGLGIN LATADVVIIY DSDWNPQVDL QAMDRAHRIG QTKTVRVFRF
ITDNTVEERI VERAEMKLRL DSIVIQQGRL VDQNLNKLGK DEMLQMIRHG ATHVFASKDS
EITDEDINAI LERGEKKTAE MNEKLSNMGE SSLRNFTMDT ESSVYNFEGE DYREKQKMAF
TQWIEPPKRE RKANYAVDAY FREALRVSEP KVPKAPRPPK QPNVQDFQFF PPRLFELLEK
EILYYRKTIG YKVPRNPDLP NSAQVQKEEQ LKIDEAESLN DEELEEKEKL LTQGFTNWNK
RDFNQFIKAN EKWGRDDIEN IAREVEGKTP EEVIEYSAVF WERCNELQDI EKTMAQIERG
EARIQRRISI KKALDTKIGR YKAPFHQLRI SYGTNKGKNY TEEEDRFLIC MLHKLGFDKE
NVYDELRQCI RNSPQFRFDW FLKSRTAMEL QRRCNTLITL IERENLELEE KEKAEKKKRG
PRPSSAQKRK VDGTPDGRGR KKKLKL
//
