ID A0A0N4V365_ENTVE Unreviewed; 1782 AA.
AC A0A0N4V365;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Bromo domain-containing protein {ECO:0000313|WBParaSite:EVEC_0000448301-mRNA-1};
GN ORFNames=EVEC_LOCUS4191 {ECO:0000313|EMBL:VDD89440.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000448301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000448301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD89440.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TAF1 family.
CC {ECO:0000256|ARBA:ARBA00009064}.
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DR EMBL; UXUI01007791; VDD89440.1; -; Genomic_DNA.
DR STRING; 51028.A0A0N4V365; -.
DR WBParaSite; EVEC_0000448301-mRNA-1; EVEC_0000448301-mRNA-1; EVEC_0000448301.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd05511; Bromo_TFIID; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR040240; TAF1.
DR InterPro; IPR022591; TAF1_HAT_dom.
DR PANTHER; PTHR13900; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR PANTHER; PTHR13900:SF0; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF12157; DUF3591; 1.
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.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131}.
FT DOMAIN 1416..1486
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1538..1608
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 125..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1782 AA; 203066 MW; 60F3E90FAA737C84 CRC64;
MHYYNPFLIF SDGSLSLFTY RKCHRWGLPI IFLERVKGPP FVPPSRREDA PLSGILLNPE
LDEIDPSLDW HVIISHEALT FRQFFPHYSQ EGILRFGRLF GANIKSSSRT EIWWPVKTYR
SSNSAALVSD ENNEEKKEVE KQIKEETETS EVKDEGLKTD TEDSSETKGK LELNFAPEPS
AEECVIDDEV LLMRPANYRS SNAEYHAESN GEEIPAWRQC NLYYKYGPSR IWYDRLGVSS
NPSSFDYGFK LKHDKRVRRN SNSKEDKTNE SQRRAKGGVA YVDPFPQSTF LPVNLVRWED
DIIFDGEAAR HQILKDFSSF KQPEYGWIPT QQTRNYESFI TSLKSNAFVQ MFSKPGMTVS
TRYIDLDFPK EPTSTHSIFP MENYDLLNTQ PRVLTLDYHD DPKIFGMPED KAPEEKPADG
ENSSPPKPFD RKEHQFTKKS KMILGQVQQR QKQEEDEQME SSVAQLTDKD PFNLSNDDYY
MPKDVGRTVS SISGGSLIQH SIPAQNIHRT FFPTHLNPFK LRHHHRLPLP KRILRTIGNR
YVVVKTLTKL IKEKEELREK QKAAEGGGEI FFMREVQDLS GKDGVLLMFE YSEEHPPLLN
QPGMASKIRN YYKRKVGKEA EPEWEFGETA FTHTTPFLGQ LSPGQGLQAV ENNLYRAPIY
RHSPNPNDFL LIRTKQGFFI RHCPVPFLVG QECPLYEVPS PNSKRATLFV RDFLLAYIYR
LFWASDQNPR RLKMEDIKSA FPHYAESSVR KRLKNCSDFK RLGQGPDQNY WVLRGDFRLP
SKEEVLAMVT PEMCCAQYSM LAAEQRLKDA GYGEKYFFTP ENEDDSDDQV TIEDEIKCAP
WNTTRAYIAS MKGKCLLDQT GIADPTGCGE GFSYVRVSAK PQKAKEEVTN VPKRLVTGTN
ADLRKLPLKE AKEICRDYGI NSLSRWEIID VIRTLSTQAA KARSDFSGMA RFARGNIRFN
FADMQEKYKR FCQRTFDLQN QTLANPDALS TDEGSSLEDS DNEELATKLE SMLAANKGKK
GISVAERKKL EYEQEEEERK ALQKMINGEN AASSSATKTE KEAPKEPQQK EPSVTNAESS
SVTNTGPRKL KIYRIFRAPD GTESTRVEVI TRPQLIEAYV RIRTTRDDTF IQVYAQMDEQ
YKEERRKEKR RLQDQLRRIR RNELKAKLHG VEIGQPINKA KPAEKKPPVI KPNLLKMRCS
ACHGTGHMKT NKNCPLYGKD SGKSQTKTVG DIHPVALTDE QLEKMAVPTG ELMSVEGTKL
KISKKIYHHS EMLKKNALRL HIPRELISGD KKREEDSNSS AASTSTAAAA TSTTTGEADE
ATTQFEGDEE SHLSDKVPLP EEQPCTPKTS TSTKPSKKSS TASKKHSTVS NIGNRRRSTV
DMDDYLYGPQ KTVHRRRADP RVTMSTQLNE IYNDVRNIPG TEHLMFPVSA KKVPDYYKYI
KQPMDLQQIK KKISENKYEL RKEFLADIKQ MLDNSRLYNG DNHVITEAAR KVFEVVSLRL
IDKEQKLMSL EKAINPLLDD NDIIGFSFIL NEIIQECKNV PKSAIFHTKV DGKRVLNYYE
KVSRPMDLGT MEQNIKEHKY TTVAAFRRDI EQIKINCGIF NGISSPLTAK AGEICDLVDH
LLELRKKQLE ELETNIQATL NDRTDADSVA ASSACLEEPE MLSPGSHTTV VKDETAEEDD
DDTIGHLQTD LALSGDEDID DEDNELSLGF KKAVCVPIPG RNFETTNDTS MSGYDAEGDL
LNSQMHSEGQ LNADLALSDS DEDDDQFISA KRPKIEDDLS TL
//