ID W5MM96_LEPOC Unreviewed; 1603 AA.
AC W5MM96;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 {ECO:0000313|Ensembl:ENSLOCP00000009505.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009505.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009505.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AHAT01007641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000009505; -.
DR Ensembl; ENSLOCT00000009516.1; ENSLOCP00000009505.1; ENSLOCG00000007820.1.
DR eggNOG; KOG0386; Eukaryota.
DR GeneTree; ENSGT00940000156887; -.
DR HOGENOM; CLU_000315_15_0_1; -.
DR InParanoid; W5MM96; -.
DR OMA; HHNSYSC; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000007820; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:UP000018468}.
FT DOMAIN 173..208
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 448..520
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 753..918
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1071..1233
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1434..1504
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1543
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1603 AA; 181807 MW; F0B3A2757663F5CD CRC64;
KMSTPDPPMG GTPRPGPSPG PGPSPGAMLG PSPGPSPGSA HSMMGPSPGP PSSGHPLPPQ
GPSGYPQDNM HQMHKPMDPM HEKGMPDDPR YGQMKGMGMR PGGHSGMGPP PSPMDQHSQG
YPSPLGGSEH APSPVPANGP PSGPLMPQGP GGVPIDGGDP QVLGQQNRGG PTPFNQNQLH
QLRAQIMAYK MLARGQPLPD HLQMAVQGKR PMPGMQQQMP SLPPPSGPGA GPSSGPGPAP
SNYNRPHAGM GGPNMLPPGP TGVPPGMQGQ PPNGPPKTWP EGEEAQIFQF VLLVGSRMPE
RMSSENRLQR KLVEPSSSPL NQRDIRSPAN LSEPENGTRV LPFCSLRGAT WLSLILFPPF
RLQARIAHRI QELENLPGSL AGDLRTKANI ELKALRLLNF QRQLRQEVVV CMRRDTALET
ALNAKAYKRS KRQSLREARI TEKLEKQQKI EQERKRRQKH QEYLNSILQH AKDFKEYHRS
VTAKIQKLTK AVATYHANTE REQKKENERI EKERMRRLMA EDEEGYRKLI DQKKDKRLAY
LLQQTDEYVA NLTELVRAHK AAQALKEKKK KKKKKKLENP EGQTPALGPD GEPLDETSQM
SDLPVKVIHV DSGKILTGVD APKAGQLEAW LEMNPGYEVA PRSDSEDSDS EEEEEDEEEQ
QQQQPQPTQA PVEEKKKIPD PDSEDVSEVD ARHIIEHAKQ DVDDEYGGQN FARGLQSYYS
VAHAVTEKVE KQSSLLVNGQ LKQYQIKGLE WLVSLYNNNL NGILADEMGL GKTIQTIALI
TYLMEYKRIN GPFLIIVPLS TLSNWVYEFD KWAPSVVKVS YKGSPAARRA FVPQLRSGKF
NVLLTTYEYI IKDKQVLAKI RWKYMIVDEG HRMKNHHCKL TQVLNTHYLA PRRLLLTGTP
LQNKLPELWA LLNFLLPTIF KSCSTFEQWF NAPFAMTGEK VDLNEEETIL IIRRLHKVLR
PFLLRRLKKE VEAQLPEKVE YVIKCDMSAL QRVLYRHMQA KGVLLTDGSE KDKKGKGGTK
TLMNTIMQLR KICNHPYMFQ HIEESFSEHL GFTGGIVQGP DLYRASGKFE LLDRILPKLR
ATNHKVLLFC QMTSLMTIME DYFAYRNFKY LRLDGTTKAE DRGMLLKAFN DPNSSYFVFL
LSTRAGGLGL NLQSADTVII FDSDWNPHQD LQAQDRAHRI GQQNEVRVLR LCTVNSVEEK
ILAAAKYKLN VDQKVIQAGM FDQKSSSHER RAFLQAILEH EEQDEEEDEV PDDETVNQMI
ARSEEEFDHF MRMDLDRRRE EARNPKRKPR LMEEDELPTW IMKDDAEVER LTCEEEEEKM
FGRGSRQRKE VDYSDSLTEK QWLKAIEEGT LEEIEEEVRQ KKTTRKRKRD RDLDLGAPST
PTTSTRSREK DEDIKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK DSSNGRQLSE
VFIQLPSRKE LPEYYELIRK PVDFKKIKER IRNHKYRSLN DLEKDVMLLC QNAQTFNLEG
SLIYEDSIVL QSVFTSVRQK IEKEEDSEGD ESEEEEEEVD EGSESESRSV KVKIKLGRKE
KSQERGKGRR RPGRGSRAKP VVSDDDSEEE QEEERSASGS EED
//
