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Database: UniProt
Entry: A0A0V1PAD4_9BILA
LinkDB: A0A0V1PAD4_9BILA
Original site: A0A0V1PAD4_9BILA 
ID   A0A0V1PAD4_9BILA        Unreviewed;      1814 AA.
AC   A0A0V1PAD4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Protein polybromo-1 {ECO:0000313|EMBL:KRZ93042.1};
GN   Name=PBRM1 {ECO:0000313|EMBL:KRZ93042.1};
GN   ORFNames=T08_7422 {ECO:0000313|EMBL:KRZ93042.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ93042.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ93042.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ93042.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ93042.1}.
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DR   EMBL; JYDM01000029; KRZ93042.1; -; Genomic_DNA.
DR   STRING; 92180.A0A0V1PAD4; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
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; cd21984; HMG-box_PB1; 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; IPR037382; Rsc/polybromo.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
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   SMART; SM00439; BAH; 2.
DR   SMART; SM00297; BROMO; 6.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   SUPFAM; SSF47370; Bromodomain; 6.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          51..121
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          208..278
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          360..430
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          523..593
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          713..783
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          980..1100
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          1187..1303
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          1380..1448
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DOMAIN          1461..1491
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DNA_BIND        1380..1448
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          139..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1419..1446
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        145..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1814 AA;  208250 MW;  EF01BCF210AD8E17 CRC64;
     MKRDHSVDES TMADVPMAKR LRRSALSSAA EEQARLCREL FTSLREFTNS EGAYISRPFL
     RLPSKKSLPE YYSVIENPID LTQIHEKVKT DEYSHVDRFM EDINLLVENA KRFYGEGSSE
     YADASELWNQ IVELRSKQEY NSDSHSEIST RSPESSPSRS SRSYRSFSPH RLHRTKENPS
     PMSGCEPVSA HVFEHLLASV LRERSEGGGR LLCDAFRLLP SKELWPDYYE TIRDPIDLQL
     IAKRVRSGRY RNLNDIERDF NLLCRNARLF NEPGSQVYRD AKTIRKFILK KKAELLDVGC
     KSIDRNLMSN DSAVVDRLLN LTEKDLAMEE DSDDEQLPLE TERQVKYLYS FLRNWRENGA
     DQSIVEPFLR LPDKRTNAEY YNNVESPVSF FVINKRLKNG CYENVNALLE DIVQLCSNAK
     ATNLQNSFLY NVSELRAVKL EELACRKVRE MNNMPGTSEP CTSTSTGRAD YLEVDDSESG
     FSSVNSPAVQ MDTTSTELDE SQAVFKEKLL TVFNAVVNYR DETGRFVASA FMEKPSKKLY
     PDYYKVIPEP IDLNTIRNAI EADKYSSSQA LAADFELLFE NARHYNEDYS VIYTDANTLN
     RIFLATMSRV CPTPIYSTKA NHFINRGRKS FSRESTLGSC LRLRSGSDAA NTITTTAITA
     PSVATNIAAA TASPVQQRFQ RAAAARGVGM CNNNLEVKLQ TLFRRVRDYA DCRGRVLSTM
     FQKLPPKSDY PDYYEVIKKP IDLQKIQSRI MLGQYERLDA LVADLALVFD NACKYNDPES
     QIYKDALMLQ RVMLLKQAEL QSDEKTRGSV NVQVAVQELL MNLFLGMQTY IGSQGRCVFD
     SFYRMQEIFD VDKESLTFER IKRNLEKKRY RRMDRFQQDI FHLFSEIRRY KGPGDQMWND
     AIELQTFFIR TRDQLAKRGE WFYSPAMAFS EKDLHREVEE DCKAFKLRSE IEEKRDHLKT
     LLSKHKLGDI DMTKHEWNGV CYCIGDFAYV KPIDSNSTRM HIMQIHRLWK DSGTNEMMVF
     GRWLYQPWET YHLLSRTFLQ NEVFLSEKFD HIDAKRLSGK CCVLFIKKYL QYRVLNFDEK
     DVYVCESLYI KRGKQFRKLL TWDTDLPGAE WLQLEERSEP LVPVRVPSIF AQTNEQQQSS
     AGNVSFEDFD HDCSVLQMER VEVVAPNDNS NQTGEVDFEQ LYAQEGIWLK LGDSVYVRNS
     DGDSKIVFVE RLWKAGNNQA FLSGVTFVDP SRVEHEPTRL FYRNELFALD NSQSFPVSSV
     YGLCAVLSYK DYCAFRPTEL TEEQIYLCDL RVVLGQQSKL IIPESHEKKF RFKAFRLSAD
     VLEDEILFFK KTVLPEKVAS PYLMKRELAM NMDDYVADSP DQDSSDQFMF HDIQSTPKLT
     SRSKSGYILF SAVARKRIMA ENPDCSFGSI SKIVGAEWKK LSKSEKKRYE EEAQRIAEER
     EKADADVGGR FHLLPGQIRV YCCRWKDCDY QFENAEQLNE HVTNVHTAQI GNNNSNNSWH
     SYAFCRQKIY DNLFVRSVET GDNQYVCLWH TCTKYRKDGR PFPSMPRLHR HIREKHVPAS
     AKCIYAQNRS RNYMPLAVVD SPRACDNFSP STQPTVVPQV AQSILAAQLL SQPVAQTTQG
     GVYPYPTTPL QSVHYSHNVE ASTHAIHPEN SRLIYENQNM PLYAALPQNS AARIPAEVAN
     LHSNIEANVV AETNQPLYGI QEGSVVVQPG QQQMMDRFGA PVQQAPSSSA AAEESLLPVF
     VAIPKKPNPI SSDAAVYLSA IEGILSGASS RSGNVVHVGK YFSKIPQTDE ELIQGYLRMQ
     RRLFLEGQET RGMQ
//
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