ID Q8IHI6_BRUMA Unreviewed; 1864 AA.
AC Q8IHI6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE SubName: Full=Polybromodomain protein {ECO:0000313|EMBL:CAC70156.1};
GN Name=BMBAC01P19.02b {ECO:0000313|EMBL:CAC70156.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CAC70156.1};
RN [1] {ECO:0000313|EMBL:CAC70156.1}
RP NUCLEOTIDE SEQUENCE.
RA Gulliano D.B., Hall N., Jones S.J.M., Clark L.N., Corton C.H.,
RA Barrell B.G., Blaxter M.L.;
RT "Conservation of long-range and micro-synteny between the genomes of two
RT distantly related nematodes.";
RL Genome Biol. 3:57.1-57.14(2002).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AL606837; CAC70156.1; -; Genomic_DNA.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR CDD; cd04717; BAH_polybromo; 2.
DR CDD; cd05524; Bromo_polybromo_I; 1.
DR CDD; cd05520; Bromo_polybromo_III; 1.
DR CDD; cd05515; Bromo_polybromo_V; 2.
DR CDD; cd05526; Bromo_polybromo_VI; 1.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 6.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
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 InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16062:SF22; BAH DOMAINCONTAINING PROTEIN; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00439; Bromodomain; 5.
DR Pfam; PF00505; HMG_box; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF47370; Bromodomain; 6.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 3.
DR PROSITE; PS50014; BROMODOMAIN_2; 5.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 53..123
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 184..254
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 340..410
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 525..595
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 699..769
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 967..1086
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1187..1305
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1441..1512
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1522..1550
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DNA_BIND 1441..1512
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 301..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1864 AA; 213490 MW; 2ED1D6BA7F2A4B97 CRC64;
MSGVKRKACV REEISPIIPS KHGRRSRNVR EELHDLRQCA ELVDALRSYR TADNRILCES
FIRAPSRRTD PKYFDVVTHP IDLTRIQQKI KTEEYSSVED LSADVRLLVN NNKTYYKEGS
QEYKDACELW ELFESHRKEM LGNASVAKME EHQKNKTVEA KRDVVSVDLL EEIIVCTLEL
TDETGRLLSP PFRVLLSQEE FPTYYDRIKK PIDLKQITIK IRSGEYRTWQ QFDADFRLMC
KNAKAFNELG SVISKDASML LKNYMKRKAE LCNSKHKPLT IKRISANKQV LDELLAQNAT
VNSSEEYSED SEEDEDSEHS SEPKWILYWT IRNEPNPVDP ETNLADPFLE LPSKSWYPDY
FDEISDPMSL FMINKKLKRD EYHTLEELLK DIVLVFENAK TYNVEGSDIY EAAAKLERLA
RSKTRALLKT IKVNEVEERI SDKSAQSPTV TRSVWKKLRK IEGSTSMQVA CSGPEPESFA
ISASNVEGSE FKRRGSSRGW SNEMQAVFRK KLTILWNTVY DHMDGKRRIA TAFMFLPSRK
DYPEYYSYIE KPIDLTTIKH KIETDQYTSI SDFMKDMDLL VHNAWDFNEP GSQIYRDATT
LQSVVRNALS GIPGLPVGSN LSVSEAFLPH MRLSDNLRPA SPSCSAIFTD RAPAVSPMNF
TKTGRGTPRR MLGPTSELEF DKIKLYELYN LIRNYKDERG RELSLPFLQL PSKFDYPDYY
DVIRRPIDLT KIRNRITSNY YDSTDALISD FNLMFDNACR YNEPESMIYK DALSLQKLIL
LKRRDLCKNT ASAINVQSEV QALLASILIS VNNHQDSDGR CFSDSLADLP GMLRRKGIDS
VNIPFSIDEM KRSVDKGRYR RLDKFQDDLF FLFNAAMDHA HSDSQVFEDT VELWMYYLKT
RDDLTRTTLL SPARWYTEKM LLTHVDNIRK RKLMEEAKDD EENKKSETLG PKADGDIDLG
STGQGGIIYR VNDYAYVAPS EETVSQRHIM RIERLYRDSD GQTFARGTWC YRPEETFHLA
TRKFCENEVF LTSYYDTVTV DRLIGKCHVM PVRQFMRQKP KGFEDSDIYV CECRYMGRQL
HFKKLKHWPY RPEDEKVEYV KREKPLTVLK RVTSVFASRK TFQTHPGALI GVNDDESVDS
TSSLEDDRLK KLPAVLEKQR VEVICSDAPE GINKSMVFYE QMQYNDRWYQ LGDFVYVYNP
LKNRNAILRV DKLWRTVEGD GFFSGPYFAR PREIKHEPAR MFYKQEVFAV DQPDITIPLE
NVQGFCTVMT VKEYTKGRPT EIDESDVYVV ESKVRGYEDG GKRCSLTGYK PSHYMSRNVS
QNDANDCTVL PINEQKTKDD VDQLLSSEVT KTEDFHSNVP STSKGIVEQA GTVTKLGTIS
TSFSSISVDD DSSSGSNQVA GTIRNLPTID QEEPMNDAYA KKLKHSLKEL VTWLAAQPKL
NARSKSGYIL FSAEVRKKVM QENPDAGFGE VSKIVGIEWK KLSEEQKKQY EIRAEYIANE
RAKQEAREPP HMRILPGQIR VYMCKWQTCD FQYDNPEELY DHVKTIHTSQ IVVDGENQFV
CLWTSCLKYR KDGKPFPSLP RLHRHIKEKH LATSAKSIYP NQRSKNYIPT YVPGSSASSV
TPGTTTFVAV QQPANGSQQV HQTYTIQQAP LTYVTQAVVS THQIVANGYV NGTAVAVAPT
AYLAATPTVV HTSSPHGYHP YQQVRQVTTS STAQPIAVAA QNYTAVPLQT VSYTAPSTSQ
QPSPVITDPG RTIVQAPKPA QPIFVAPPNT VQIKRVMHSE VYLKYIESLS SSQQKTVSKY
SRSLLANQRN TTPSQKISTT QWLKEAKDNG VRDEEVVKAL WRLRDALLES TVNIAREMDC
AGPL
//