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Database: UniProt
Entry: A0A452SL89_URSAM
LinkDB: A0A452SL89_URSAM
Original site: A0A452SL89_URSAM 
ID   A0A452SL89_URSAM        Unreviewed;      1416 AA.
AC   A0A452SL89;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 {ECO:0000313|Ensembl:ENSUAMP00000033405.1};
GN   Name=SMARCA2 {ECO:0000313|Ensembl:ENSUAMP00000033405.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000033405.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000033405.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   Ensembl; ENSUAMT00000037213.1; ENSUAMP00000033405.1; ENSUAMG00000024701.1.
DR   GeneTree; ENSGT00940000154821; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:UniProt.
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: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; cd18063; DEXHc_SMARCA2; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.40.5.120; -; 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; 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; 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   SMART; SM00592; BRK; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022}.
FT   DOMAIN          171..206
FT                   /note="QLQ"
FT                   /evidence="ECO:0000259|PROSITE:PS51666"
FT   DOMAIN          425..497
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          755..920
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   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1360..1402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..32
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..154
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..305
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1360..1389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1416 AA;  160987 MW;  D56A34C54092C8BD CRC64;
     MSTPTDPGAM PHPGPSPGPG PSPGPILGPR PGPSPGSVHS MMGPSPGPPS VSHPMPTMGS
     ADFPQESTHQ MHKPIDGLHD KGIVEDMHCG SMKGSGMRPP HPGMGPPQSP MDQHSQGYMS
     PHPSPLGAPE HVSSPMSGGG PTPPQMPPSQ PGPLISGDPQ AMSQPSRGPS PFSPVQLHQL
     RAQILAYKML ARGQPLPETL QLAVQGKRTL PGMQQPQDAW FCLLTFSSFP LPALPPSSSP
     FLPSSSLVWR WSVVPVAGAV GRPGGGCRAP ACPSCPCRSC PAGPGPELSG PSTPQKLPPA
     PGQPSPILQL QQKQSRISPI QKPQGLDPVE ILQEREYRLQ ARIAHRIQEL ENLPGSLPPD
     LRTKATVELK ALRLLNFQRQ LRQEVVACMR RDTTLETALN SKAYKRSKRQ TLREARMTEK
     LEKQQKIEQE RKRRQKHQEY LNSILQHAKD FKEYHRSVAG KIQKLSKAVA TWHANTEREQ
     KKETERIEKE RMRRLMAIHG SLPWCCYFLM GVDKYRRNWF TSLAWVSGFI GHSFLEWDLR
     AEDEEGYRKL IDQKKDRRLA YLLQQTDEYV ANLTNLVWEH KQAQAAKEKK KRRRRKKAEE
     IAEGGESALG PDGEPIDESS QMSDLPVKVT HTETGKVLFG PEAPKASQLD AWLEMNPGYE
     VAPRSDSEES DSDYEEEVCG HLCWCGVRGK PLCLAVTTTA KQDVDDEYSM QYSARGSQSY
     YTVAHAISER VEKQSALLIN GTLKHYQLQG LEWMVSLYNN NLNGILADEM GLGKTIQTIA
     LITYLMEHKR LNGPYLIIVP LSTLSNWTYE FDKWAPSVVK ISYKGTPAMR RSLVPQLRSG
     KFNVLLTTYE YIIKDKHILA KIRWKYMIVD EGHRMKNHHC KLTQVLNTHY VAPRRILLTG
     TPLQNKLPEL WALLNFLLPT IFKSCSTFEQ WFNAPFAMTG ERVDLNEEET ILIIRRLHKV
     LRPFLLRRLK KEVESQLPEK VEYVIKCDMS ALQKILYRHM QAKGILLTDG SEKDKKGKGG
     AKTLMNTIMQ LRKICNHPYM FQHIEESFAE HLGYSNGLYR ASGKFELLDR ILPKLRATNH
     RVLLFCQMTS LMTIMEDYFA FRNFLYLRLD GTTKSEDRAA LLKKFNEPGS QYFIFLLSTR
     AGGLGLNLQA ADTVVIFDSD WNPHQDLQAQ DRAHRIGQQN EVRVLRLCTV NSVEEKILAA
     AKYKLNVDQK VIQAGMFDQK SSSHERRAFL QAILEHEEEN EEEDEVPDDE TLNQMIARRE
     EEFDLFMRMD MDRRREDARN PKRKPRLMEE DELPSWIIKD DAEVERLTCE EEEEKIFGRG
     SRQRRDVDYS DALTEKQWLR VGVAIEDGNL EEMEEEVRLK KRKRRRNVDK DPAKEDVEKA
     KKRRGRPPAE KLSPNPPKLT KQMNAIIDTV INYKDR
//
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