ID A0A3B5R540_XIPMA Unreviewed; 1605 AA.
AC A0A3B5R540;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Probable global transcription activator SNF2L2 {ECO:0000313|Ensembl:ENSXMAP00000038773.1};
GN Name=SMARCA2 {ECO:0000313|Ensembl:ENSXMAP00000038773.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000038773.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000038773.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000038773.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 STRING; 8083.ENSXMAP00000038773; -.
DR Ensembl; ENSXMAT00000035184.1; ENSXMAP00000038773.1; ENSXMAG00000015611.2.
DR GeneTree; ENSGT00940000154821; -.
DR InParanoid; A0A3B5R540; -.
DR OMA; XDEEEES; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0070603; C:SWI/SNF superfamily-type complex; IEA:UniProt.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 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.
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:SF541; GLOBAL TRANSCRIPTION ACTIVATOR SNF2L2-RELATED; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 186..221
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 475..547
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 773..938
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1090..1252
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1439..1509
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 528..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 181636 MW; 82407043428BCF18 CRC64;
MSTPSDTSGG MSHPGPSPGA GLSPGPILGP SPGPDPSPGS VHSMMGPSPG PGTPNAPHGM
QAQGQSDYSQ DSMYPMHKPM EAAMNDKTMA EAMHFGHMKG VGMRSLHSGM GPPQSPMDQH
SQGYMSPHPS PLGIHEHASS PMSGGGGGPT PPHMPPAQPS PMMSMDPQGG MASMSGMGQP
GRGPSSFSPI QLQQLRAQIL AYKILARGQP LPENLQLAVQ GKRSLPTMQQ QQPQAALPPQ
QQPQQPQQQQ PQQQQQQQQQ QASGASPYRP SGMSMAPMSG PQSSPCPTPA LQGHNQSTGP
KPWTDGQASD NQAQKHLTPV PSGRPSPAPP QAPVGAPGPV PGSSGAVHPP GQQVSPMLQM
QQKQNRITPV QKPQGLDPVG ILQEREFRLQ ARIAHRIQEL ESLPGSLPPD LRTKATVELK
ALRLLNFQRQ LRQDVVACMR RDTTLETALN SKAYRRSKRQ TLREARMTEK LEKQQKLEQE
KKRRQKHQEY LNSILQHAKD FKEYHRSVSG KIQKLTRAVA NWHTNTEREQ KKETERLEKE
RMKKLLEEDE EGYRKLIDQK KDKRLAYLLQ QTDEYVANLT TLVYEHKAAQ AAKEKKRRKT
KKKKVEGDGE GTSAIGPDGE PMDESSQMSE LPVKVIQTET GKVLQGTDAP KSSQLEAWLE
MNPGYEVAPR SDSEESGSEF EEEDEEEMGK AETEEKKKVD PNGDKVAEND TKNIIESAKQ
DVDDEYSVPT GQTSSQSYYG VAHAVIERVE KQSSLLINGM LKQYQVQGLE WMVSLYNNDL
NGILADEMGL GKTIQTIALI TYLMEHKRLN GPYLIIVPLS TLSNWVYELD KWAPSVVKIA
YKGTPGLRRG LVPQLRSGKF NVLITTYEYI IKDKHILAKI RWKYMIVDEG HRMKNHHCKL
TQVLNTHYVA PRRLLLTGTP LQNKLPELWA LLNFLLPTIF KSCSTFEQWF NAPFAMTGER
VDLNEEETIL IIRRLHKVLR PFLLRRLKKE VESQLPEKVE YVIKCDMSAI QRVLYRHMQK
GILLTDGSEK DKKGKGGAKT LMNTIMQLKK ICNHPYMFQH IEESFAEHLG YPNGIINGHE
LYRASGKFEL LDRILPKLQA TGHRVLLFCQ MTSLMTIMED YFGYRNFQYL RLDGTTKSED
RAALLKKFNE EGSQYFIFLL STRAGGLGLN LQAADTVVIF DSDWNPHQDL QAQDRAHRIG
QQNEVRVLRL CTVNSVEEKI LAAAKYKLNV DQKVIQAGMF DQKSSSHERR AFLQAILEHE
EQNEDEDEVP DDETLNQMIA RNEDEFDLFM RMDMDRRRED ARNPKRKPRL MEEDELPSWI
IKDDAEVERL TYEEEEEKMF GRGSRCRRDV DYSDTLTEKQ WLRAIEDGNL EEIEEEIRLK
KRKRKRRQDK DSSSRDDGGM KAKKRRGRPP AEKLSPNPPK LTKQMNTIID TVINYRDGSG
RQLSEVFVQL PSRKELPEYY ELIRKPVDFK KIKERVRNHK YRSLGDLEKD VMLLCQNAQT
FNLEGSQIYE DSIVLQSVFK SARQKIAKDE DSEDDSDEDD DDDYDSEAEA KSVRVKIKLG
RDGRSHDKGK KRQSRGKAKP VVSDDDSDDD QDDNDLSDKS KSDDD
//
