ID A0A2K5LU73_CERAT Unreviewed; 1573 AA.
AC A0A2K5LU73;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 {ECO:0000313|Ensembl:ENSCATP00000016496.1};
GN Name=SMARCA2 {ECO:0000313|Ensembl:ENSCATP00000016496.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000016496.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000016496.1}
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; ENSCATT00000040657.1; ENSCATP00000016496.1; ENSCATG00000031470.1.
DR GeneTree; ENSGT00940000154821; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000031470; Expressed in frontal cortex and 12 other cell types or tissues.
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; 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; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 173..208
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 419..491
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 719..884
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1037..1199
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1402..1472
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..69
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 211..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..636
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1573 AA; 179642 MW; F30578CDC5FA109C CRC64;
MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM
GSTDFPQESM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY
MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH
QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGMQQQQQ QQQQPQQQQQ QQQPQQQPPQ
PQTQQQQQPA LVNYNRPSGP GPELSGPSTP QKLPVPAAQP PAAAVPGPSV PQPAPGQPSP
ILQLQQKQSR ISPIQKPQGL DPVEILQERE YRLQARIAHR IQELENLPGS LPPDLRTKAT
VELKALRLLN FQRQLRQEVV ACMRRDTTLE TALNSKAYKR SKRQTLREAR MTEKLEKQQK
IEQERKRRQK HQEYLNSILQ HAKDFKEYHR SVAGKIQKLS KAVATWHANT EREQKKETER
IEKERMRRLM AEDEEGYRKL IDQKKDRRLA YLLQQTDEYV ANLTNLVWEH KQAQAAKEKK
KRRRRKKKAE ENAEGGESAL GPDGEPIDES SQMSDLPVKV THTETGKVLF GPEAPKASQL
DAWLEMNPGY EVAPRSDSEE SDSDYEEEDE EEESSRQETE EKILLDPNSE EVSEKDAKQI
IETAKQDVDD EYSMQYSARG SQSYYTVAHA ISERVEKQSA LLINGTLKHY QLQGLEWMVS
LYNNNLNGIL ADEMGLGKTI QTIALITYLM EHKRLNGPYL IIVPLSTLSN WTYEFDKWAP
SVVKISYKGT PAMRRSLVPQ LRSGKFNVLL TTYEYIIKDK HILAKIRWKY MIVDEGHRMK
NHHCKLTQVL NTHYVAPRRI LLTGTPLQNK LPELWALLNF LLPTIFKSCS TFEQWFNAPF
AMTGERVDLN EEETILIIRR LHKVLRPFLL RRLKKEVESQ LPEKVEYVIK CDMSALQKIL
YRHMQAKGIL LTDGSEKDKK GKGGAKTLMN TIMQLRKICN HPYMFQHIEE SFAEHLGYSN
GVINGAELYR 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 AIEDGNLEEM
EEEVRLKKRK RRRNVDKDPA KEDVEKAKKR RGRPPAEKLS PNPPKLTKQM NAIIDTVINY
KDRCNVEKVP SNSQLEIEGN SSGRQLSEVF IQLPSRKELP EYYELIRKPV DFKKIKERIR
NHKYRSLGDL EKDVMLLCHN AQTFNLEGSQ IYEDSIVLQS VFKSARQKIA KEEESEDESN
EEEEEEEEEE SESEAKSVKV KIKLNKKDEK GRDKGKGKKR PNRGKAKPVV SDFDSDEEQD
EREQSEGSGT DDE
//
