ID W5MX36_LEPOC Unreviewed; 1682 AA.
AC W5MX36;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Polybromo 1 {ECO:0000313|Ensembl:ENSLOCP00000012945.1};
GN Name=PBRM1 {ECO:0000313|Ensembl:ENSLOCP00000012945.1};
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:ENSLOCP00000012945.1, 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:ENSLOCP00000012945.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AHAT01020757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01020758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000012945; -.
DR Ensembl; ENSLOCT00000012972.1; ENSLOCP00000012945.1; ENSLOCG00000010556.1.
DR eggNOG; KOG1827; Eukaryota.
DR GeneTree; ENSGT00390000003017; -.
DR HOGENOM; CLU_001483_1_0_1; -.
DR InParanoid; W5MX36; -.
DR OMA; WQFYETL; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000010556; Expressed in larva and 13 other cell types or tissues.
DR GO; GO:0016586; C:RSC-type complex; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04717; BAH_polybromo; 2.
DR CDD; cd05524; Bromo_polybromo_I; 1.
DR CDD; cd05517; Bromo_polybromo_II; 1.
DR CDD; cd05520; Bromo_polybromo_III; 1.
DR CDD; cd05518; Bromo_polybromo_IV; 1.
DR CDD; cd05515; Bromo_polybromo_V; 1.
DR CDD; cd05526; Bromo_polybromo_VI; 1.
DR CDD; cd21984; HMG-box_PB1; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR037968; PBRM1_BD5.
DR InterPro; IPR037382; Rsc/polybromo.
DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00439; Bromodomain; 6.
DR Pfam; PF00505; HMG_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR PRINTS; PR00886; HIGHMOBLTY12.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47370; Bromodomain; 6.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 5.
DR PROSITE; PS50014; BROMODOMAIN_2; 5.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 65..135
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 203..273
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 391..461
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 530..600
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 670..740
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 950..1068
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1151..1267
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1374..1442
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 1374..1442
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1541..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1297..1327
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1682 AA; 192799 MW; 6F7C42E77FAAAF97 CRC64;
MGSKRRRATS PSSSISGGDF DDAQTSTPGP GSSRKRRRAS NIPTVDPIAV CHELYNTIRD
YKDDHGRLLC ELFLRAPKRR NQPDYYEVVT QPIDLMKIQQ KLKMEEYDDV EQLTSDFQLM
FNNAKSYYKA DSPEYKAACR LWDLYLRTKN EFVQRGDYEE EDEDGEDTQE NPGTSTEEET
ASNSLKEVLE QLLEAVVTHT EPSGRLISEL FQKLPSKVHY PDYYAIIKEP IDLKTIAQRI
QMGHYKSVTA MAKDIDLLTK NAKTYNEPGS QVFKKDANNI KKLFIQKKAE LEHAEPTKSS
IRIRYNIIAF INLMQTNHVF DRNRRSAQGD RLSAITMALQ YGSESDEDAL LAGAVRYDEV
ESEAESINSC MNINNPIFQL YEAVRGGRNS QGQLIAEPFL QLPSKKEYPD YFHQIKQPIS
LHQIRNKMRN NEYESVDQID ADLNLMFENA KRYNLPNSAI YKRVMKLQQI LQLKRKELSR
REEAEDGDSM LSSATSDTGS AKRKSMKKNA KKHRLKILYS AVTEAREAST GRRLCDLFMV
KPSKKDYPDY YKIILEPVDL KTIEHNIRSD KYLTEDAFME DMKLMFRNAR HYNEEGSQKK
VYNDANFLEK ILKEKRKELG PLPEDEDMAS PKLKISRKSG ISPKKSKYLT PLQQKLNELY
EAVKNYTDKR GRRLSAIFLR LPSRQELPDY YVTIKKPIDM EKIKSHMMAN KYQDVDSLVE
DFVLMFNNAC TYNEPESLIY KDALVLHKVL LETRRDLEGG EESHVPNVTM LIQELIHNLF
VSVLSHQDDE GRCYSDSLAE IPSRDPGNPN KPLLNFEIIR NSIENNRYRR LDVFQEHMFE
VLEKARRLHR TDSEIFEDAV ELQQFFIKIR DELCKNGEIL LSPALSYTTK HLHNDVEKEK
KEKLPKEMEE DKLKREEEKK EAEKSDEHSG GGWQSGLQRT YSQDCSFKNS MYHVGDYVYV
EPAEPNLQPH IVCIERLWQD DAGEKWLYGC WFYRPNETFH LATRKFLEKE VFKSDYYNKV
PVSKILGKCV VMFVKEYFKL HPEGFRPEDV FVCESRYSAK TKSFKKIKMW TMPVSSVRFV
PRDVPLPVVR VASMFANATK HEQEKTPEMA EEGRGVDAKG IIDKEREDVP VEMPSGEPGC
QYYEQLHYND MWLKVGDCVF IKSHGLVRHR VGRIEKMWVR DGAAYFLGPI FIHPEETEHE
PTKMFYKKEV FLSNLEETCP MACVIGKCVV SSFKDYLSCR PTEVSEDDVL LCESRYNDTD
KQMKKFKGLK RFSLSAKVVD DEIYYFRKPI VPQKEPSPLL EKKIQELEAK FAELEGVEDE
MEEIGEEDGE VTETPSMPQL QTPLASELDI MPYTPPQSTP KSIKGSVKKE GSKRKINMSG
YILFSSEMRA VIKAQHPDFS FGELSRLVGT EWRNLEATKK AEYEERAAKV AEQQERERAA
QQQQGASPRA GTPVGALMGV VPPPTPMGML NQNITPGSGM MGGFGPPMLP LQGSVDGMVS
MGSMQPHHMG VPPLTHHLPP GMPVIPGIPF SGVIGQGVNS MGGSPGGGNP YSQQMGIHGQ
GQQAPPPYPG QGQPGQPALQ QPSTPMFVAP PPKTQRLLHS EAYLKYIEGL SAESGTVSRW
DHTLTARRKD VHLTKEQESR LPSHWLKSKG AHTTMADALW RLRDLMLRDT LNIRQNYNLQ
NV
//
