ID A0A0V1HBN3_9BILA Unreviewed; 2005 AA.
AC A0A0V1HBN3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Protein polybromo-1 {ECO:0000313|EMBL:KRZ07949.1};
DE Flags: Fragment;
GN Name=PBRM1 {ECO:0000313|EMBL:KRZ07949.1};
GN ORFNames=T11_1130 {ECO:0000313|EMBL:KRZ07949.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ07949.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ07949.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ07949.1};
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:KRZ07949.1}.
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DR EMBL; JYDP01000094; KRZ07949.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0016586; C:RSC-type complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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 Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 2.
DR SMART; SM00297; BROMO; 6.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00220; S_TKc; 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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS50011; PROTEIN_KINASE_DOM; 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:UP000055024};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 49..119
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 188..258
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 339..409
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 503..573
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 660..730
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 901..1018
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1108..1223
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1267..1329
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1348..1376
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1703..1997
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 1267..1329
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 137..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1306..1333
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1050..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2005
FT /evidence="ECO:0000313|EMBL:KRZ07949.1"
SQ SEQUENCE 2005 AA; 229799 MW; E1C1F8337A1E22DB CRC64;
MTSKRAHSSD EVPLAKRLRR SALSSAAEEQ VAKHIRELFT RMRDFVNEDG RHVSRPFFRF
ASKKLTPEYV KIVTNPMDLT LIHEKVKQDE YANVDQFMSD VNLMVENAKN FYKKDSVEYG
DACDLWNMIT EARNKQECNS DTMSEFSNRS IESSPTPSLS PKRENVSNRT QACLLEKLLC
TVLTAKSEDG LLCEAFKVIP SKEEWPYYYE VIRDPIDLRT ISMKLRRGRY RSVNDLEKDL
NQLCRNAKLF NEPSSSVYRA ANAIRKLVAH RKMELTDSNA KSSSYCHEMK KTTAVIDNFL
REVCAVVEED SDDEQIPVST NAQLKNLYTF LRGCRDEVSG QCLVEPFLRC PDRSSFPKYY
EKIAMPISFY AINHKLKVGL YNAVSGMLDD ISLLCSNVKV YFGENSELYK RALKLQLLAF
SKIQDTDTSQ LELSVRKDLE HLAGLDDVPK AESTLHLPAV KLEFNEESAR GKVGRKSFDD
ALTQYREKLL SVYNAVVNYR DQTGRVVAMA FMEKPSKKLY PDYYKVIPEP IDLHMIKAAI
DSDRYTSSQA LAADFELLFE NARHYNEDYS AIYTDANTLN GVFADAMKHV FPTPLTIPRC
SKARRSNYNF ILKDRSRRGS YSSDSSGNRV SRKSQNISLG EHELKLWYIY QAIKEFRDPN
NRTLSSVFLK LPSRTDYPDY YEVIRKPIDL QKICNKLSAK QYDSVEALVS DFALMFDNAC
KFNDPDSLIY KDALTLQRVL IQKAAELRRG EQHSPPIDVQ SDVQELLNRI FSDVLNYQDD
LGRCLSDSLY EADEEYLIKS KDKNAVTLNI IKKRLAMKWY TRLDRFQQDM LEVFKRARRL
KSVNSQIFED SVDLQSYFIK VRDELTKRGD LFYSSAMRFT EKDLISEIDA MRRRNASKSN
LESEVEDNSI NEPQNNYKPR ILLISRIWKQ STGAIGIFGN WYYRPSETCH VSLRKFLKNE
VFRTDDYDRI EPSALAGRCH VLFIKTFVNH KPTNFADEDV YVCESRYSIV SQEFKKIKSW
QLSSQGVHLE DRSTPCLLLR MPLNLEPHDD NNGNVLSSAQ QEESTNKQDD NSNSCLLVVD
TGRTDVVVGG QKENSSTVAY EQIQLNGCWI RLGDCVYIRV AEHEVKVVLV ERIWKSQGDI
LLHGIPFVGP HQIEHEPTQM FYKKELFAIE PSETFNGRSV VGRCAVLSLK DYCSSRPTEV
NEADVFLCDS RAIWNEYGKR VIPDNPERKF KIPTFRLSCE VPEDEVVFFK KPMNADKVDT
PSTPKLTSRS KSGYILFSAV IRKRIMAENP ECSFGHISKI VGGEWKKLSE EEKKKYEEEA
QKIAEEREKA DQLTGGRLHL LPGQIRVYCC KWRDCDYQFD TVEQLNEHIT SMHTSQIVEG
SDNQYVCMWL TCSKYRKEGR PFPSLARLHR HIKEKHLPQS AKCLFPQNLG KHYISISSSS
GLDSAQLAQT SMSAFQQQQQ QQQQQTEQHQ YYQQQHYLEQ QQQNAVLMST STPAHQFSNV
AQTQPIRYAS PGSINTPSAH VVYDCSGNQV AGGAYPMHYS GQPLSPAVQQ TMASSSHGGR
VRSPASFSMP ATPTKSSVDP GSILVRALEK PVEPIQLQPQ VLRVSKVVHS KKYLNWARNR
SGRSSTLSGD NFALKKARKI DTLESIAMDS KKTDAVVQAL NLMTKTLYCL LLHVFAQQLL
GWQKMASMTS NICVQVGDII DSWKLTKLLG FGTYGSVYEV LNLKNDQLEA MKLEDQTSEV
SSLKIEILVL RSLNKHNARH CCQLLGSGRK DKFNYMVITL VGKTFEDISQ VMKEKHSGDG
KLDSCSAMYL CMQALEGLQD LHAICFIHRD VKPQNFAIGV HPNVRNVYIL DFGTVRKYLR
SDGKHRRPRA KAGFRGTFNF ASVYALNLDD QSRRDDMWSW MYLLIQMTTG TLPWLDLPPA
GNYFSELEQY KTMKNEHMEN PAVLLDGCPE EYYAIFNIIK QMNYYSAPEY DGIYELLKFS
MNRENSSSES LQYEQILNEE AAKNK
//
