ID A0A6P8NXB3_GEOSA Unreviewed; 1580 AA.
AC A0A6P8NXB3;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=Probable global transcription activator SNF2L2 isoform X1 {ECO:0000313|RefSeq:XP_033781117.1, ECO:0000313|RefSeq:XP_033781126.1};
GN Name=SMARCA2 {ECO:0000313|RefSeq:XP_033781117.1,
GN ECO:0000313|RefSeq:XP_033781126.1, ECO:0000313|RefSeq:XP_033781136.1};
OS Geotrypetes seraphini (Gaboon caecilian) (Caecilia seraphini).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Gymnophiona; Geotrypetes.
OX NCBI_TaxID=260995 {ECO:0000313|Proteomes:UP000515159, ECO:0000313|RefSeq:XP_033781117.1};
RN [1] {ECO:0000313|RefSeq:XP_033781117.1, ECO:0000313|RefSeq:XP_033781126.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-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 RefSeq; XP_033781117.1; XM_033925226.1.
DR RefSeq; XP_033781126.1; XM_033925235.1.
DR RefSeq; XP_033781136.1; XM_033925245.1.
DR GeneID; 117350710; -.
DR KEGG; gsh:117350710; -.
DR CTD; 6595; -.
DR OrthoDB; 5857104at2759; -.
DR Proteomes; UP000515159; Chromosome 1.
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; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18063; DEXHc_SMARCA2; 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:UP000515159};
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 449..521
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 749..914
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1067..1229
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1432..1502
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..46
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..234
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..577
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1267
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1541
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1580 AA; 179882 MW; B900754F60E2FC75 CRC64;
MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVTHPMATL
AHSDYPQEGM HQMHKSLDGM HEKGIADEIH CASVKSTSMR PPHPGMGPPQ SPMDQHSQGY
MSPHPSPLGA PDHVSSPMST GGPTPPQIPP SQPGPLMPGD PQVMSQPTRG PSPFSPVQLH
QLRAQILAYK MLARGQPLPE NLQLAVQGKR TLPGIQQQQQ QQQQQQQQQQ QQQQIIPATY
NRPPGMGMHP MGVPPAGPGP TPGMPGHGTN MTPKTWTEGQ GSEMSVPSTP QKLAVPAPSG
RPSPAPPAVQ PPVAMPGPSV TQPTPGQPTS IVQLQQKQNR ISPIQKPQGL DPIEILQERE
YRLQARIAHR IQELENLPGS LPPDLRTKAT VELKALRLLN FQRQLRQEVV ACMRRDTTLE
TALNSKAYKR SKRQTLREAR MTEKLEKQQK IEQERKRRQK HQEYLNSILQ HAKDFKEYHR
SVTGKIQKLS KAVATWHANT EREQKKETER IEKERMRRLM AEDEEGYRKL IDQKKDRRLA
YLLQQTDEYV ANLTSLVWEH KQAQAAKEKK KRRRRKKKAE ENAEGMGSGL GPDGELIDES
SQMSDLPVKV IHTETGKVLL APEAPKASQL ETWLEMNPGY EVAPRSDSEE SGSEYEEEDE
DDESSRLESE EKIRINLNTD DVTENDAKQI IETAKQDVDD EYSMQADARE SQSYYAVAHA
ITERVEKQSS LLINGSLKHY QVQGLEWMVS LYNNNLNGIL ADEMGLGKTI QTIALITYLM
EHKRLNGPYL IIVPLSTLSN WQYEFDKWAP SVVKIAYKGT PAMRRSLVPQ LRSGKFNVLL
TTYEYIIKDK HILAKIRWKY MIVDEGHRMK NHHCKLTQVL NTHYVAPRRI LLTGTPLQNK
LPELWALLNF LLPTIFKSCS TFEQWFNAPF AMTGERVDLN EEETILIIRR LHKVLRPFLL
RRLKKEVESQ LPEKVEYVIK CDMSALQKIL YRHMQAKGIL LTDGSEKDKK GKGGAKTLMN
TIMQLRKICN HPYMFQHIEE SFAEHLGYSG GVINGADLYR ASGKFELLDR ILPKLRATNH
RVLLFCQMTS LMTIMEDYFA FRNLLYLRLD GTTKSEDRAA LLKKFNEEGS QYFIFLLSTR
AGGLGLNLQA ADTVVIFDSD WNPHQDLQAQ DRAHRIGQQN EVRVLRLCTV NSVEEKILAA
AKYKLNVDQK VIQAGMFDQK SSSHERRAFL QAILEHEEQN ESQKKDELSG DNSQEGASQE
EDEVPDDETL NQMIARNEEE FDLFMRMDMD RRREDARNPK RRPRLLEEDD LPSWIIKDDA
EVERLTCEDE EEKIFGRGSR QRRDVDYSDT LTEKQWLRAI EDGNLEEMEE EVRLKKRKRR
RNVDKDSSKD DGDKAKKRRG RPPAEKLSPN PPKLTKQMNA IIDTVINYKD SSGRQLSEVF
VQLPSRKELP EYYELIRKPV DFKKIKERIR NHKYRSVGDL EKDVMLLCHN AQTFNLEGSQ
IYEDSIVLQS VFKSARQKIA KEEESEEESN DDEEEEEDES ESESKSVKVK IRLNKKDEKS
RDKGKGKKRQ SRVKAKPCCE
//
