ID A0A671V0S9_SPAAU Unreviewed; 1029 AA.
AC A0A671V0S9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 {ECO:0000313|Ensembl:ENSSAUP00010018430.1};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010018430.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010018430.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR AlphaFoldDB; A0A671V0S9; -.
DR Ensembl; ENSSAUT00010019473.1; ENSSAUP00010018430.1; ENSSAUG00010008122.1.
DR GeneTree; ENSGT00940000157297; -.
DR Proteomes; UP000472265; Unplaced.
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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000472265}.
FT DOMAIN 168..333
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 463..614
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 816..868
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 785..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 120124 MW; F2A397DD44ECAFD9 CRC64;
LREKTRENML VREQQPVQLS HPHSSDAGKE SSSDAGPDGQ DASPSSSKTK VEIPGYEEKV
QTDRTNRFEY LLKQTELFAH FIQPAAQKTP TSPLKMKPGR PRIKKDEKQN LLSAGDNRHR
RTEQEEDEEL LSESTKTTNV CTRFDDSPSY VKTGKMRDYQ VRGLNWLISL YENGINGILA
DEMGLGKTLQ TIALLGYMKH YRNIPGPHMV LVPKSTLYNW MNEFKRWVPS LRAVCLIGDR
EQRTALIRDV LLPGEWDVCV TSYEMLIIEK AVFKKFNWRY LVIDEAHRIK NEKSKLSEIV
REFKTTNRLL LTGTPLQNNL HELWALLNFL LPDVFNSAED FDSWFDTNNC LGDQKLVERL
HTVLRPFLLR RIKADVEKTL LPKKEIKMYV GLSKMQREWY TKILMKDIDI LNSAGKMDKM
RLLNVLMQLR KCCNHPYLFD GAEPGPPYTT DLHLVVNSGK MVVLDKLLPK MKQQGSRVLI
FSQMTRVLDI LEDYCMWRNY GYCRLDGQTP HEERQISINA YNEPNSSKFI FMLSTRAGGL
GINLATADVV ILYDSDWNPQ VDLQAMDRAH RIGQQKQVRV FRFITENTVE ERIVERAEMK
LRLDSIVIQQ GRLVDPSANK LGKDEMLSII RHGATHVFAS KESEITDDDI DAILERGERK
TMEMKEKLSS LGESTLRNFT MDTENSSVYT FEGEDYREKK KVITNWIEPP KRERKANYAV
DAYFREALRV SEPKAPKAPR PPKQPNVQDF QFFPPRLFEL LEKEILFYRK TIGYKVPRNP
DMPNSAQMQK EEQAKIDEAE ALTEEELEEK ENLLQQGFTI WNKRDFNQFI KANEKWGRDD
IENIAREVEG KTPEEVMEYS AVFWERCNEL QDIEKIMAQI ERGEARIQRR ISIKKALDSK
IGRYKAPFHQ LRISYGTNKG KNYTEEEDRF LICMLHKLGF DKESVYDELR QCIRNSPQFR
FDWFLKSRTA MELQRRCNTL ITLIERENME LEEREKAEKK KRGPKNASAQ KRKSEGTQDG
RGRRKKLKL
//