ID A0A401P1V3_SCYTO Unreviewed; 1498 AA.
AC A0A401P1V3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Global transcription activator SNF2L2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=scyTo_0013657 {ECO:0000313|EMBL:GCB67112.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB67112.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB67112.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB67112.1}.
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DR EMBL; BFAA01007076; GCB67112.1; -; Genomic_DNA.
DR STRING; 75743.A0A401P1V3; -.
DR OMA; XDEEEES; -.
DR Proteomes; UP000288216; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216}.
FT DOMAIN 94..129
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 349..421
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 650..815
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 968..1130
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1328..1398
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 18..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1435
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1498
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1498 AA; 171687 MW; 3101FDC84D7FCB2A CRC64;
MHDKGMADEM HYGQMKGMGM RTSHAGMGPP QSPMDQHSQG YLSPHPSPMS VPEHVPSPMS
AGGPTPPQIP PAQATPMLQG DPQVISQQNR GPSPFNPVQL HQLRAQILAY KMLARGQPLP
DNLQLAVQGK RSLPSMQQQV APIAYNRPPN MGMHSMAGQA VGPSQIMPGH VPNVPKPWTE
GQVNEMGIPN TPQKMPTQAT CGRPSPIPAV QATPGPGAPL SQQPIVQPSP TIQLHQKQNR
ITPIQKPQGL DPVEILQERE YRLQARIAHR IQELENLPGS LPPDLRNKAT VELKALRLLN
FQRQLRQEVV ACMRRDTTLE TALNAKAYKR SKRQSLREAR ITEKLEKQQK IEQERKRRQK
HQEYLNSILQ HAKDFKEYHR SVTGKIQKLS RAIGTWHANT EREQKKETER IEKERMRRLM
AEDEEGYRKL IDQKKDKRLA YLLQQTDEYV ASLTKLVYEH KAAQAAKEKK KKKKKKKKTE
EVSEAASSSL APDGELLDES SQMSDLPVKV IHVETGKVLQ GADAPKAIQL DTWLEMNPGY
EVAPRSDTEE SGSEYEEEEE DEEAPVAPGS EEKKIIVPNI EDVSDFFAKQ IIECAKQDVD
DEYSMRAGMK GSQSYYAVAH AVTERVEKQS TLLINGSLKH YQLQGLEWLV SLYNNNLNGI
LADEMGLGKT IQTIGLITYL MEHKRLNGPY LIIVPLSTLS NWVYEFDKWA PSVVKISYKG
TPALRRSFIP QMRSGKFNVL LTTYEYIIKD KHVLAKLRWK YMIVDEGHRM KNHHCKLTQV
LNTHYVAPRR VLLTGTPLQN KLPELWALLN FLLPTIFKSC STFEQWFNAP FAMTGERVDL
NEEETILIIR RLHKVLRPFL LRRLKKEVES QLPEKVEYVI KCDMSSLQKI LYRHMQAKGI
LLTDGSEKDK KGKGGAKTLM NTIMQLRKIC NHPFMFQHIE ESFAEHLGYN GGIITGPDLY
RASGKFELLD RILPKLRVTN HRVLLFCQMT SLMTIMEDYF AFRSFSYLRL DGTTKAEDRG
ALLKMFNEEG AKYFIFLLST RAGGLGLNLQ AADTVVIFDS DWNPHQDLQA QDRAHRIGQQ
NEVRVLRLCT VNSVEEKILA AAKYKLNVDQ KVIQAGMFDQ KSSSHERRAF LQALLEHEEQ
NEGDTNASPS CSTTWEEDEV PDDETLNQMI ARHEEEFELF MRMDLERRRE DARNPKRKPR
LMEEDDLPSW IVKDDAEVER LTCEEEEEKM FGRGSRMRRD VDYSDALTEK QWLRAIEDGN
LEEMEEEIRQ KKARKRRRNV DKDPSKDDGK KKKKRGRPPA EKLSPNPPRI TKQMNAIIDT
VINYRDSLSR QLSEVFIQLP SRKELPEYYE LIRKPVDFKK IKDRIRSHKY RSLGDLEKDV
MLLCHNAQTF NLEGSQIYED SIVLQSVFKS ARQKIAKEEE SEEESNEDDD DEEESGSESK
SVKVKIKLGR KDSDKSREKG KSKKRLSRTK IKPVISDDDS DDDQDDNDQS DISGSEDE
//
