ID Q20947_CAEEL Unreviewed; 1209 AA.
AC Q20947;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 2.
DT 27-MAR-2024, entry version 163.
DE SubName: Full=Bromo domain-containing protein {ECO:0000313|EMBL:CAA93473.3};
GN Name=bet-2 {ECO:0000313|EMBL:CAA93473.3,
GN ECO:0000313|WormBase:F57C7.1a};
GN ORFNames=CELE_F57C7.1 {ECO:0000313|EMBL:CAA93473.3}, F57C7.1
GN {ECO:0000313|WormBase:F57C7.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA93473.3, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA93473.3, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA93473.3,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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DR EMBL; BX284606; CAA93473.3; -; Genomic_DNA.
DR PIR; T22845; T22845.
DR RefSeq; NP_509770.2; NM_077369.4.
DR AlphaFoldDB; Q20947; -.
DR SMR; Q20947; -.
DR STRING; 6239.F57C7.1a.1; -.
DR EPD; Q20947; -.
DR PaxDb; 6239-F57C7-1a-2; -.
DR PeptideAtlas; Q20947; -.
DR EnsemblMetazoa; F57C7.1a.1; F57C7.1a.1; WBGene00010199.
DR GeneID; 181257; -.
DR KEGG; cel:CELE_F57C7.1; -.
DR UCSC; F57C7.1b; c. elegans.
DR AGR; WB:WBGene00010199; -.
DR WormBase; F57C7.1a; CE31548; WBGene00010199; bet-2.
DR eggNOG; KOG1474; Eukaryota.
DR OMA; HNTIARP; -.
DR OrthoDB; 168195at2759; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00010199; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; Q20947; baseline and differential.
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; 1.20.920.10; Bromodomain-like; 2.
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 PANTHER; PTHR22880:SF243; BET (TWO BROMODOMAINS) FAMILY PROTEIN; 1.
DR PANTHER; PTHR22880; FALZ-RELATED BROMODOMAIN-CONTAINING PROTEINS; 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.
PE 1: Evidence at protein level;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Proteomics identification {ECO:0007829|EPD:Q20947,
KW ECO:0007829|PeptideAtlas:Q20947};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 299..371
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 571..643
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1209 AA; 133723 MW; A50740C93309E5E0 CRC64;
MSDYSAKPSG SLARIGDYDL SSDDSDQNDE DETLIASKTI QTGAVQVNDI AVAEASPAET
DAKSSASPVS GPEPPTSAVV ENRDLDEFKK ESGSNDDKQE EINEDKDSNE ETVFQQTESG
SADVVDKTDV KQKDSDSSAD DDHSHSKSGS VHSPQKPQGS TTPCSVQSPA SPVGDEQAVK
MEEVEEPIVA SEEVPDKKPE SVKESTDSES SGSEHGFEKM DTAEKVEDEC NDDEVAASNG
TEEPEPGDKA ADTVNPWETP RQEPVDGVVQ PRTEPPAGKP TRHTNCLDFV LFTVVKDALK
HKHSWPFQLP VDAIKLEIPE YHNIVNTPMD LRTIEKRLRN LYYWCAEDAI KDINQVFINC
YSFNPPEYDV YKMAKTLEKQ VLSQLTQLPR SEKPADLADH HRRGMFSAST PSGKTKGPKQ
RGRKSTRGRK KTSLPRGAST FKDESVDDNN DDESSKVDSI NFDDDDDTAT EKDAESRAES
VQPEVVNEEP KPSTSQPPSK KRKAENGEPA VAVKIATPAT PVAAHPQEET PRRKNPNTLI
EWKHLVPRWQ GKIPEWQKFC SKLLNEIHSV KNKGFAQVFY LPVDPIKLKI YDYLEVITNP
MDLQTIKKKL DFKQYAEPEE FVHDINLMVD NCCKYNPKGS PAHSNALELR SFFEQRWKLF
PRPGVDPIIA DSYINQNLVV NTDLIEDERI NSYLSAVKAE EKKCAEKLEQ LRSMSEGLYT
IAMQRREAKL AGNTAPALAQ NQLSQLEGLG ISIKSTPMMI PELISPALSV RSSSRAPVPK
IIDDIGPSPI KARKISKPRA SMASNVSVPY TPTGNPRGRK PKKSGRPKKN IYSPATVSER
ISQQPPFEVT PYVSIYGRKV VGTNDKIELS ERMASIPQMY ITPILRIIQI GHHNTGKTIT
SLRSLCEEEI DFNDVSDDLV IELLDYLEMI QKDKAKAEQV RQELEVKAKF YGFEAYDNKL
GTIPKTRNMP PPLQHRMRSD SPSPSASRTG NQSSDSDSAS DDSSDDEPSR SNSNVAGPRR
ALELSGNSSS ASTPAGPSKA QPAVVRPSSK SVASKPAYTK RTLSESSSSS DSNGSSSDSS
DSDSEPKPQA KKPEPPQKKV AKKPAPQQKK KAPLSILDEL LPDTPEKKPV MASVPTTSGS
ARQLPPDSYQ KPSQISEAEL KAQKEQEHNA ALQRREEARR LRALEDQQQV LNQHEVMHEF
ESQYGDFSY
//
