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Database: UniProt
Entry: A0A671V0S9_SPAAU
LinkDB: A0A671V0S9_SPAAU
Original site: A0A671V0S9_SPAAU 
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
//
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