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Database: UniProt
Entry: W5MBS5_LEPOC
LinkDB: W5MBS5_LEPOC
Original site: W5MBS5_LEPOC 
ID   W5MBS5_LEPOC            Unreviewed;      1095 AA.
AC   W5MBS5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Bromodomain testis associated {ECO:0000313|Ensembl:ENSLOCP00000005834.1};
GN   Name=BRDT {ECO:0000313|Ensembl:ENSLOCP00000005834.1};
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:ENSLOCP00000005834.1, 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:ENSLOCP00000005834.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01018345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01018346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01018347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MBS5; -.
DR   STRING; 7918.ENSLOCP00000005834; -.
DR   Ensembl; ENSLOCT00000005842.1; ENSLOCP00000005834.1; ENSLOCG00000004853.1.
DR   eggNOG; KOG1474; Eukaryota.
DR   GeneTree; ENSGT00940000154549; -.
DR   HOGENOM; CLU_001499_0_1_1; -.
DR   InParanoid; W5MBS5; -.
DR   OMA; IKAREPT; -.
DR   Proteomes; UP000018468; Linkage group LG10.
DR   Bgee; ENSLOCG00000004853; Expressed in ovary and 13 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd05497; Bromo_Brdt_I_like; 1.
DR   CDD; cd05498; Bromo_Brdt_II_like; 1.
DR   Gene3D; 1.20.1270.220; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR   InterPro; IPR031354; BRD4_CDT.
DR   InterPro; IPR043508; Bromo_Brdt_I.
DR   InterPro; IPR043509; Bromo_Brdt_II.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR027353; NET_dom.
DR   InterPro; IPR038336; NET_sf.
DR   PANTHER; PTHR22880:SF238; BROMODOMAIN TESTIS-SPECIFIC PROTEIN; 1.
DR   PANTHER; PTHR22880; FALZ-RELATED BROMODOMAIN-CONTAINING PROTEINS; 1.
DR   Pfam; PF17035; BET; 1.
DR   Pfam; PF17105; BRD4_CDT; 1.
DR   Pfam; PF00439; Bromodomain; 2.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
DR   PROSITE; PS51525; NET; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          45..117
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          281..353
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          503..585
FT                   /note="NET"
FT                   /evidence="ECO:0000259|PROSITE:PS51525"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..457
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..663
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..842
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1075
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1095 AA;  122338 MW;  F095D33A75A3C4DB CRC64;
     MSFVKAEPPP VVKNPPPPEY RNPRKPGRLT NQLQYLQKVV IKALWRHSFA WPFQEPVDAV
     KLNLPDYYTI IKTPMDLSTI KRRLENNYYW KAMECVEDFN TMFTNCYVYN RPGDDIVLMA
     QALEKLFLQK VAQMPQEEVE ITPTVNKEGG KGLTKLKSRS PVSEVVFQQT VTVIPPDALR
     AIPSAPLMPA QLSSKIKKGV KRKADTTTPA ASVVTSCESS PTPAEPKPCK LASRRGSGRP
     IKPPKKDLPD SQQQHQVGKK PKLSEQLKCC SVILKEMFAK KHAAYAWPFY KPVDTETLGL
     HDYHDIIKHP MDLGTIKKKM DDRVYKDAQE FASDFRLMFL NCYKYNPPGH EVVAMARKLQ
     DVFEMRFAKI PAGAAERAPP APPVPDERES SSGSDSDSDG SSDSDSSSDA EEERAQRLAQ
     LQEQLKAVRD QLQLLSQAPL LKPKKKKKEK SKKEKRKKDR DRRELSRKKG YGDKKKPKSK
     AQKMSSKGSL ESKKSKVPGM PCDAEEEEPA LPMTYDEKRQ LSLDINKLPG DKLGKVVNII
     QSREPTLRDS NPEEIEIDFE TLKPSTLRAL ERYVMTCLRK RPRKPNLEKK SSKSQEALQS
     EKKQELEKRL QHVGERLNPA KKPKSQCEEV APPKGLQGPS QLSDSSSSSS SDSSSSDSST
     SDSSDSESEQ KKMKQSNTDI TDVKIIKKEV NQMTTSLWNS AIKRHTEPQT KSNSQPTVTQ
     SKQPELNTSQ PLEHEEITVS PPALHTRLPP QPSRPSAKAT PLPLKHRVSS LQADSPPQPP
     EPASALQEAV RHPQSSHLPS SGSALSQAAP DPHSHFSPLP LLQSPLTQPE PTPTPLLHPP
     QNPPTRAQGE GMSSLLSPLS SPLGPQGPQQ PPSTPSNPAL TCRAVEGMHE IPGSVKLFLN
     CLTIILDLLS QWFHKVLPRC SPYLVETCAS KARVVTGVDI VLRNADSWAS LGKMASATPS
     MIKSSSESFQ QFRKAAMEKE ERERALRRLQ VEQAGREKKP VPEQPRYCWG AGVWHRLQMG
     SPTVRDADRE AAVERVGTPP GPEAPKQEAP LSSVDQERER ARRREQERRR REAMSGIIDM
     TLQSDIMATF EKNLY
//
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