ID A0A673KW45_9TELE Unreviewed; 1500 AA.
AC A0A673KW45;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE SubName: Full=Probable global transcription activator SNF2L2 {ECO:0000313|Ensembl:ENSSRHP00000067725.1};
GN Name=LOC107727446 {ECO:0000313|Ensembl:ENSSRHP00000067725.1};
OS Sinocyclocheilus rhinocerous.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=307959 {ECO:0000313|Ensembl:ENSSRHP00000067725.1, ECO:0000313|Proteomes:UP000472270};
RN [1] {ECO:0000313|Ensembl:ENSSRHP00000067725.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSRHP00000067725.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00048778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00048778};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR Ensembl; ENSSRHT00000069570.1; ENSSRHP00000067725.1; ENSSRHG00000027841.1.
DR Proteomes; UP000472270; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProtKB-ARBA.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.10810:FF:000008; Chromatin structure-remodeling complex subunit snf21; 1.
DR FunFam; 1.20.920.10:FF:000004; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 3.40.5.120:FF:000001; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 1.20.5.170:FF:000089; Putative global transcription activator SNF2L2; 1.
DR FunFam; 3.40.50.300:FF:003020; SNF2-related domain-containing protein; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472270};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 160..195
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 426..498
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 702..867
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1018..1180
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1365..1435
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..47
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..555
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1464
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1479
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1500 AA; 170330 MW; 37480C56AEF581FD CRC64;
MSTPNEPPVG IPHAGPSPGA ALSPGPILGP SPGPGPSPGS VHSMMGPSPG PPSVPHAMQG
QGPMEGMHEK GMGEDMHYGQ MKGVGMRSLH SGMGPPQSPM DQHSQGYMSP HPSPMGQVPE
HVPSPMSGGG PTPPQMSQGQ SPMMPMDPQG MVQQARGQSA FSPVQLQQLR AQILAYKILG
RGQPLPENLQ LAVQGKRSLP TMQQQPVNTG PYNRPLGMPM THGGPATGPC PSPVMQTHTQ
SSGPKPWPEG ECQGSETPGA QQKLLAPAPS GRPSPAPLLA PTGTQPVPST SLTSQPQPPP
GPGQPSLIIQ LQQKQNRITP IQKPQGLDPV ELLQEREYRL QARIAHRIQE LENLPGSLPP
DLRTKATVEL KALRLLNFQR QLRLDVVACM RRDTTLETAL NSKAYKRSKR QTLREARMTE
KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSIS GKIQKLSKAI ATWHTNTERE
QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDKRLAYLL QQTDEYVANL TELVYEHRAA
QAAKEKKRKR KKKKKETGDA EGMGAIGPDG EQLIDENSQM SELPVKVIQT ETGKVLQGTD
APKSSQLEAW LEMNPGYEVA PRSDSEESGS EFEEEVSVLL FLLIKSAKQD VDDEYSVQAG
QTSSQSYYGV AHTVIERVDK QSTLLINGTL KHYQVQGLEW MVSLYNNNLN GILADEMGLG
KTIQTIALIT YLMEHKRLNG PYLIIVPLST LSNWVNELDK WAPSIVKIAY KGTPSMRRSL
VPQLRSGKFN VLITTYEYII KDKHILAKIR WKYMIVDEGH RMKNHHCKLT QVLNTHYVAP
RRLLLTGTPL QNKLPELWAL LNFLLPTIFK SCSTFEQWFN APFAMTGERV DLNEEETILI
IRRLHKVLRP FLLRRLKKEV ESQLPEKVEY VIKCDMSAIQ KVLYRHMQGK GILLTDGSEK
DKKGKGGAKT LMNTIMQLKK ICNHPYMFQH IEVSQQCLST LKCTSGPDLY RASGKFELLD
RILPKLKATN HRVLLFCQMT TLMTIMEDYF AFRNFLYLRL DGTTKCEDRA MLLKKFNEEG
SQFFIFLLST RAGGLGLNLQ AADTVVIFDS DWNPHQDLQA QDRAHRIGQQ NEVRVLRLCT
VNSVEEKILA AAKYKLNVDQ KVIQAGMFDQ KSSSHERRAF LQAILEHEEQ NEEEDEIPDD
ETLNQMIARN EDEFELFMRM DLDRRREDAR NPKRKPRLME EDELPSWILK DDAEVERLTC
EEDDEKIFGR GSRHRRDVDY SDTLTEKQWL RAVEDGNLEE IEEEIRLKRR KRSRHVDKDL
RREDGDKAKK RRGRPPAEKF SPNPPKLMKQ MNAIIDTVIN YRDASGRQLS EVFVQLPSRK
ELPEYYELIR KPVDFKKIKE RVRSHKYRGV SDLEKDVMLL CHNAQTYNLE GSQVTKSVKV
KIRQSNRDER CQDKGKKRSS RGKAKPVVSD DDSEEEQEEN VGPPILSSNR PVIDTVCLAG
//
