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Database: UniProt
Entry: W5NBG1_LEPOC
LinkDB: W5NBG1_LEPOC
Original site: W5NBG1_LEPOC 
ID   W5NBG1_LEPOC            Unreviewed;      1038 AA.
AC   W5NBG1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 {ECO:0000313|Ensembl:ENSLOCP00000017970.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017970.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000017970.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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; AHAT01015616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NBG1; -.
DR   STRING; 7918.ENSLOCP00000017970; -.
DR   Ensembl; ENSLOCT00000018002.1; ENSLOCP00000017970.1; ENSLOCG00000014591.1.
DR   eggNOG; KOG0385; Eukaryota.
DR   GeneTree; ENSGT00940000157297; -.
DR   HOGENOM; CLU_000315_0_2_1; -.
DR   InParanoid; W5NBG1; -.
DR   OMA; VHDYQFF; -.
DR   Proteomes; UP000018468; Linkage group LG7.
DR   Bgee; ENSLOCG00000014591; Expressed in testis and 12 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:0021999; P:neural plate anterior/posterior regionalization; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          157..322
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          452..603
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          824..876
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1000..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1038
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1038 AA;  121491 MW;  648E20B35236876A CRC64;
     MSDEEIPSTS REPEPDSEEK EDPPFQLKPP PKLVTKVEAD VDPEYEEKRK TDRANRFEFL
     LKQTELFAHF IQPAAQKSPT SPLKVKLGRP RMKKDEKQNL LSVGDNRHRR TEQEEDEELL
     SESRKTSNVL VRFEESPSYV KNGALRDYQI RGLNWMISLY ENGINGILAD EMGLGKTLQT
     IALLGYLKHY RNIPGPHMVL VPKSTLHNWM NEFKRWVPTL RAVCLIGDKD ARAAFIRDVM
     MPGEWDVCVT SYEMVIREKS VFKKFNWRYL VIDEAHRIKN EKSKLSEIVR EFKTTNRLLL
     TGTPLQNNLH ELWSLLNFLL PDVFNSADDF DSWFDTNNCL GDQKLVERLH AVLRPFLLRR
     IKAEVEKSLP PKKEVKIYLG LSKMQREWYT KILMKDIDIL NSAGKMDKMR LLNILMQLRK
     CCNHPYLFDG AEPGPPYTTD THLVTNSGKM VVLDKLLPKV KEQGSRVLIF SQMTRVLDIL
     EDYCMWRGYE YCRLDGNTPH EEREEAIEAY NAPNSTKFIF MLSTRAGGLG INLATADVVI
     LYDSDWNPQV DLQAMDRAHR IGQTKTVRVF RLITDNTVEE RIVERAEMKL RLDSIVIQQG
     RLIDQQSNKL AKDEMLQMIR HGATHVFASK DSELTDEDIN TILERGAKKT AEMNERLEKL
     GESSLRNFTV DTETSLYNFE GEDYREKQKV FILFVLYNTN SLLIQFYNLS MMEWIEPPKR
     ERKANYAVDA YFREALRVSE PRAPKAPRPP KQPNIQDFQF FPPRLFELLE KEILYYRKTI
     GYKVPKNPEL SNATQVQKEE QRKIDEAGPL TAEETEEKEK LLTQGFTSWN KRDFNQFIKA
     NEKYGRDDID NIAREVEGKT PEEVIEYSAV FWERCNELQD IEKIMAQIER GEARIQRRIS
     IKKALDAKIA RYKAPFHQLR IQYGTNKGKN YTEEEDRFLI CMLHKMGFDK ENVYEELRQC
     VRNAPQFRFD WFIKSRTAME LQRRCNTLIS LIEKENMEIE EKERAEKKKR APKAQTAQKR
     KTDTLSDTAG RKDKKLKS
//
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