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Database: UniProt
Entry: A0A3M7QFJ8_BRAPC
LinkDB: A0A3M7QFJ8_BRAPC
Original site: A0A3M7QFJ8_BRAPC 
ID   A0A3M7QFJ8_BRAPC        Unreviewed;      1254 AA.
AC   A0A3M7QFJ8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Putative global transcription activator SNF2L2 isoform X1 {ECO:0000313|EMBL:RNA10217.1};
DE            EC=3.6.1.15 {ECO:0000313|EMBL:RNA10217.1};
DE            EC=3.6.1.3 {ECO:0000313|EMBL:RNA10217.1};
DE   Flags: Fragment;
GN   ORFNames=BpHYR1_002745 {ECO:0000313|EMBL:RNA10217.1};
OS   Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OC   Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC   Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX   NCBI_TaxID=10195 {ECO:0000313|EMBL:RNA10217.1, ECO:0000313|Proteomes:UP000276133};
RN   [1] {ECO:0000313|EMBL:RNA10217.1, ECO:0000313|Proteomes:UP000276133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYR1 {ECO:0000313|EMBL:RNA10217.1};
RX   PubMed=30375419; DOI=10.1038/s41598-018-34188-y;
RA   Franch-Gras L., Hahn C., Garcia-Roger E.M., Carmona M.J., Serra M.,
RA   Gomez A.;
RT   "Genomic signatures of local adaptation to the degree of environmental
RT   predictability in rotifers.";
RL   Sci. Rep. 8:16051-16051(2018).
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:RNA10217.1}.
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DR   EMBL; REGN01006258; RNA10217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7QFJ8; -.
DR   STRING; 10195.A0A3M7QFJ8; -.
DR   Proteomes; UP000276133; Unassembled WGS sequence.
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:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
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; 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:SF973; ATP-DEPENDENT HELICASE BRM; 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; 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; 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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RNA10217.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276133}.
FT   DOMAIN          151..223
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          414..579
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          728..895
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1056..1126
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1202..1220
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1221..1243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RNA10217.1"
SQ   SEQUENCE   1254 AA;  144699 MW;  D99179E4034787F5 CRC64;
     SKPQPAPAAL PQAGTARQMT PMTSRPSHNA IPMAAYKHMN KVAPCAKPVG LDPAQLLKER
     ENFIVHKIKY RIGELERLPL KQLGDHLQTK VAIELKALRL LDFQKQLRHE IVSCMRADST
     LETGLNAKAY KRCKRQTLRE ARITEKMERQ QKQEAERKRR QKHLEYLNAV IEHSKTFKEQ
     HRANLAKVNK MAKGVINWHT NTERIQKKEQ ERLEKERIKL LMAEDEEGYR KLVNEKKDKR
     LQYLLQQTDD YIESLTKLVR EHQDDLMKQK SSVKTKSSAK TTKTDTAHTD DAEDRRVKVA
     NSMTGEVIEG GDAPRSSELD AWLEAHPDWH AVPRELDHDN DNDSVPDDDD DDEHQDKADT
     SLTTAEDDEY NSASSKNSYY GVAHRLREKV TEQASILVGG TLKPYQVRGL EWLVSLYNNN
     LNGILADEMG LGKTIQTISL ITYLMEKKKV NGPFLIIVPL STLSNWVNEF ARWAPSVISV
     VYKGDPNQRK AISGLLKTGK FNVLVTTYEY IIKDKSILAK IKWKYMIIDE GHRMKNHHCK
     LTQILNTFYI APHRLLLTGT PLQNKLPELW ALLNFLLPSI FKSCSSFEQW FNAPFNTSGE
     KVELNNEETL LIIRRLHKVL RPFLLRRLKK EVESQLPDKV EYIIKCDMSA LQRVIYHSMK
     TNGVMLTEDK NGKNTTKTLM NTIMQLRKIC NHPFIFQEIE EKLAQHLKYP GGIINGPEIY
     RASGKFELLD RILPKLKQTG HRVLMFCQMT SLMTVMEDYF NYRNFRYLRL DGGTKAEERG
     DLLKVFNEPG SEYFIFILST RAGGLGLNLQ VADTVIIFDS DWNPQQDLQA QDRAHRIGQK
     NEVRVLRLMT VNSVEEKIVA AAKHKLNVDS KVIQAGMFDA KSTGQERRQY LQTILSQESN
     EVDDDPEVPD DETVNQMIAR SEDEYELFQR MDIERRRVEA REQNRKPRLM EDSELPAWLI
     KDDSQLEQMR LEAQGHIDES IYGRGTRVRK EEDEDGDDAE QGEDTAESPQ PQVKRKRGRP
     AASTKKISKH DQKEAHRLHK KIKFLLDCLL NYADNDGRLL SEPFVQLPTR RELPDYYEII
     KRPIDIKKIQ AKIKDNKYAS LDQLADDVEL MFRNAQEYNV ESSLIYEDSV VLLSVFKTAK
     ARLMEREAAS ASEKEEESDD DGDENEDGKK SKRARLDESK RSKKSAKKTD EYEPMDDSVN
     VAVGADDDEE EDDVDINFDF NDDEEAKIAT ERRNERKQQA GFRQIQDEIK TGND
//
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