ID A0A673VZG2_SALTR Unreviewed; 1032 AA.
AC A0A673VZG2;
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:ENSSTUP00000001622.1};
GN Name=SMARCA5 {ECO:0000313|Ensembl:ENSSTUP00000001622.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000001622.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000001622.1}
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; A0A673VZG2; -.
DR Ensembl; ENSSTUT00000001744.1; ENSSTUP00000001622.1; ENSSTUG00000000533.1.
DR GeneTree; ENSGT00940000156733; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000472277; 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; 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; 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:UP000472277}.
FT DOMAIN 170..335
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 465..616
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 817..869
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 786..817
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 120074 MW; 27231084FDE40E8A CRC64;
MSETGNGVEL REEQAVELEE TGGVEEKDDA SEASKEESSE AGQDAQDEDP SSSTAPAYEE
KVASDRTNRF EYLLKQTEVF AHFIQPAAQK TPTSPLKMKP GRPRVKKDEK QNLLSVGDNR
HRRTEQEEDE ELLSESSKTT NVCTRFDESP SFVKGGTMRD YQVRGLNWLI SLYENGINGI
LADEMGLGKT LQTISLLGYM KHYRSIPGPH MVLVPKSTLY NWMNEFKRWV PSLKAVCLIG
DREQRNALIR DVLLPGEWDV CVTSYEMLII EKAVFKKFNW RYLVIDEAHR IKNEKSKLSE
IVREFKTTNR LLLTGTPLQN NLHELWALLN FLLPDVFNSS EDFDSWFDTN NCLGDQKLVE
RLHTVLRPFL LRRIKNEVEK SLLPKKEIKM YVGLSKMQRE WYTKILMKDI DILNSAGKMD
KMRLLNVLMQ LRKCCNHPYL FDGAEPGPPY TTDLHLAVNS GKMAVLDKLL PKMKAQGSRV
LIFSQMTRML DILEDYCMWR NFGYCRLDGQ TPHEERQISI NAYNEENSPK FIFMLSTRAG
GLGINLATAD VVILYDSDWN PQVDLQAMDR AHRIGQKKQV RVFRFITENT VEERIVERAE
MKLQLDSIVI QQGRLVDPNA NKLGKDEMLS IIRHGATHVF ASKESDITDD DIDEILERGE
KKTMELKEKM NTMGESSLRN FTMESDNSVY TFEGEDYREK KKVVTNWIEP PKRERKANYA
VDAYFREALR VSEPKAPKAP RPPKQPNVQD FQFFPPRLFE LLEKEILFYR KTIGYKVPRN
PELPNAAQHQ KEEQAKIDEA EGLSEEELEE KENLLSQGFT IWNKRDFNQF IKANEKWGRD
DIENIAREVE GKTPEEVMEY SAVFWERCNE LQDIEKIMAQ IERGEARIQR RISIKKALDT
KIGRYKAPFH QLRISYGTNK GKNYTEEEDR FLICMLHKLG FEKESVYDEL RQCIRNSPQF
RFDWFLKSRT AMELQRRCNT LITLIERENM ELEEREKAEK KKKGPRSQSS AQKRKGEGTP
DQRGGRRKKL KL
//
