ID A0A096MA15_POEFO Unreviewed; 1648 AA.
AC A0A096MA15;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 {ECO:0000313|Ensembl:ENSPFOP00000028256.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000028256.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000028256.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYCK01008250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPFOT00000024933.1; ENSPFOP00000028256.1; ENSPFOG00000007892.2.
DR GeneTree; ENSGT00940000156887; -.
DR OMA; YGPGHKL; -.
DR Proteomes; UP000028760; 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; cd18062; DEXHc_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; IPR030100; BRG1_ATP-bd.
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; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF76; TRANSCRIPTION ACTIVATOR BRG1; 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:UP000028760}.
FT DOMAIN 167..202
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 455..527
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 751..916
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1069..1234
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1484..1554
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..331
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..662
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1648
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1648 AA; 184687 MW; 0DBF397588DC37CF CRC64;
MSTPDPPMGG TPRPGPSPGP GPSPGGMMGP SPGPSPGSAH SMMGPSPGPP SSGHPHPPQG
PSGYPQDNMH QMHKPMDPMH DKGMPDDPRY GQMKGMGMRP GGHSGMGPPP SPMDQHSQGY
PSPLGGSEHA PSPVPANGTP SGPGASPGPG GPPGPGVGPG AAGGPTPFNQ NQLHQLRAQI
MAYKMLARNH PIPEHLQLAV QGKRPMPGTP PPMPNMPPSA GPGGGQAAGP GPGPGPGPGP
AQTNYNRPHG MVGPNMAPPG PAGVPPAMQG QPANGPPKSW PEGPMVNAAA PSNPPQKLIP
PQPTGRPSPA PPSVPPAASP VMPPQTQSPG QPAQLPPMML HQKQNRITPI QKPHGLDPVE
ILQEREYRLQ ARIVHRIQEL EHLPGSLAGD LRTKATIELK ALRLLTFQRQ LRQEVVACMR
RDTALETALN AKAYKRSKRQ SLREARITEK LEKQQKIEQE RKRRQKHQEY LNSILQHAKD
FKEYHRSITA KIQKATKAVA TYHANTEREQ KKENERIEKE RMRRLMAEDE EGYRKLIDQK
KDKRLAYLLQ QTDEYVANLT ELVRAHKAAQ ALKKPDAVEG GAPAMGPDGE PLDETSQMSD
LPVKVIHVDS GKILTGVDAP KAGQLEAWLE MNPGYEVAPR SDSEDSGSED EDEEDEDDAE
DQPQPTTATS EEKKKIPDPD SEDVSEVDVQ HIIEHAKQDV DDEYGSASFN RGLQSYYAVA
HAVTEKVDKQ SSLMVNGMLK QYQIKGLEWL VSLYNNNLNG ILADEMGLGK TIQTIALITY
LMELKRINGP FLIIVPLSTL SNWVYEFDKW APSVVKVSYK GSPQARRSFV PILRSGKFNV
LLTTYEYIIK DKQVLAKIRW KYMIVDEGHR MKNHHCKLTQ VLNTHYLAPR RLLLTGTPLQ
NKLPELWALL NFLLPTIFKS CSTFEQWFNA PFAMTGEKVD LNEEETILII RRLHKVLRPF
LLRRLKKEVE AQLPEKVEYV IKCDMSALQR VLYRHMQAKG VLLTDGSEKD KKGKGGTKTL
MNTIMQLRKI CNHPYMFQHI EESFSEHLGF SGGIVTGPDL YRASGKFELL DRILPKLRAT
KHKVLLFCQM TSLMTIMEDY FAYRNFKYLR LDGGPSGTTK AEDRGMLLKT FNDPASEYFV
FLLSTRAGGL GLNLQSADTV IIFDSDWNPH QDLQAQDRAH RIGQQNEVRV LRLCTVNSVE
EKILAAAKYK LNVDQKVIQA GMFDQKSSGY ERRAFLQAIL EHEEQDEVRS WSYREASVHT
LPPPWGAIPY DSILQEEDEV PDDETVNQMI ARSEEEFELF MRMDLDRRRE DARNPKRKPR
LMEEDDMPGW ILKDDAEVER LTCEEEEEKM FGRGSRQRKE VDYSDSLTEK QWLKVGQRKP
PRVHNGFGDD LLTHRAIEEG NLEDIEEEVR HKKTTRKRKR ERDHDGSPAT PSSSHRGRDK
DDSGKKAKKR GRPPAEKLSP NPPTLTKKMK KIVDAVVKYK DGHNGRQLSE VFIQLPSRKE
LPEYYELIRK PVDFKKIKER IRSHKYRNLN DLEKDVMLLC QNAQTFNLEG SLIYEDSIVL
QSVFTSVRQK IEKDEHRFVV FSSHLCVLSP SARSVKVKIK LSRKEKGDRG GKSQRRRGRG
SRAKPVVSDD DSEDEQEEER SASGSEDD
//
