ID A0A673KM75_9TELE Unreviewed; 1536 AA.
AC A0A673KM75;
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:ENSSRHP00000067531.1};
GN Name=LOC107727446 {ECO:0000313|Ensembl:ENSSRHP00000067531.1};
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:ENSSRHP00000067531.1, ECO:0000313|Proteomes:UP000472270};
RN [1] {ECO:0000313|Ensembl:ENSSRHP00000067531.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSRHP00000067531.1}
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; ENSSRHT00000069374.1; ENSSRHP00000067531.1; 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; 3.40.50.300:FF:000116; probable global transcription activator SNF2L2 isoform X1; 1.
DR FunFam; 1.20.5.170:FF:000089; Putative global transcription activator SNF2L2; 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 173..208
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 448..520
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 723..888
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1041..1203
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1401..1471
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1479..1525
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 71..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..158
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..576
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1500
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1515
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1536 AA; 174454 MW; 90D3AC173ACB4845 CRC64;
MSTPNEPPVG IPHAGPSPGA ALSPGPILGP SPGPGPSPGS VHSMMGPSPG PPSVPHAMQG
QGAGDYSQDI HPMHKPMEGM HEKGMGEDMH YGQMKGVGMR SLHSGMGPPQ SPMDQHSQGY
MSPHPSPMGQ VPEHVPSPMS GGGPTPPQMS QGQSPMMPMD PQGMVQQARG QSAFSPVQLQ
QLRAQILAYK ILGRGQPLPE NLQLAVQGKR SLPTMQQQPV NTGPYNRPLG DYTYGHFRCM
PMTHGGPATG PCPSPVMQTH TQSSGPKPWP EGECQGSETP GAQQKLLAPA PSGRPSPAPL
LAPTGTQPVP STSLTSQPQP PPGPGQPSLI IQLQQKQNRI TPIQKPQGLD PVELLQEREY
RLQARIAHRI QELENLPGSL PPDLRTKATV ELKALRLLNF QRQLRLDVVA CMRRDTTLET
ALNSKAYKRS KRQTLREARM TEKLEKQQKI EQERKRRQKH QEYLNSILQH AKDFKEYHRS
ISGKIQKLSK AIATWHTNTE REQKKETERI EKERMRRLMA EDEEGYRKLI DQKKDKRLAY
LLQQTDEYVA NLTELVYEHR AAQAAKEKKR KRKKKKETGD AEGMGAIGPD GEQLIDENSQ
MSELPVKVIQ TETGKVLQGT DAPKSSQLEA WLEMNPGYEV APRSDSEESG SEFEEEVSVL
LFLLIKSAKQ DVDDEYSVQA GQTSSQSYYG VAHTVIERVD KQSTLLINGT LKHYQVQGLE
WMVSLYNNNL NGILADEMGL GKTIQTIALI TYLMEHKRLN GPYLIIVPLS TLSNWVNELD
KWAPSIVKIA YKGTPSMRRS LVPQLRSGKF NVLITTYEYI IKDKHILAKI RWKYMIVDEG
HRMKNHHCKL TQVLNTHYVA PRRLLLTGTP LQNKLPELWA LLNFLLPTIF KSCSTFEQWF
NAPFAMTGER VDLNEEETIL IIRRLHKVLR PFLLRRLKKE VESQLPEKVE YVIKCDMSAI
QKVLYRHMQG KGILLTDGSE KDKKGKGGAK TLMNTIMQLK KICNHPYMFQ HIEESFAEHL
GYPNGIISGP DLYRASGKFE LLDRILPKLK ATNHRVLLFC QMTTLMTIME DYFAFRNFLY
LRLDGTTKCE DRAMLLKKFN EEGSQFFIFL LSTRAGGLGL NLQAADTVVI FDSDWNPHQD
LQAQDRAHRI GQQNEVRVLR LCTVNSVEEK ILAAAKYKLN VDQKVIQAGM FDQKSSSHER
RAFLQAILEH EEQNEVSHFN SSSCLKTTEE DEIPDDETLN QMIARNEDEF ELFMRMDLDR
RREDARNPKR KPRLMEEDEL PSWILKDDAE VERLTCEEDD EKIFGRGSRH RRDVDYSDTL
TEKQWLRAVE DGNLEEIEEE IRLKRRKRSR HVDKDLRRED GDKAKKRRGR PPAEKFSPNP
PKLMKQMNAI IDTVINYRDA SGRQLSEVFV QLPSRKELPE YYELIRKPVD FKKIKERVRS
HKYRGVSDLE KDVMLLCHNA QTYNLEGSQV TKSVKVKIRQ SNRDERCQDK GKKRSSRGKA
KPVVSDDDSE EEQEENVGPP ILSSNRPVID TVCLAG
//
