ID A0A0V0SMU1_9BILA Unreviewed; 2129 AA.
AC A0A0V0SMU1;
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:KRX28221.1};
GN Name=PBRM1 {ECO:0000313|EMBL:KRX28221.1};
GN ORFNames=T07_12712 {ECO:0000313|EMBL:KRX28221.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX28221.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX28221.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX28221.1};
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:KRX28221.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDL01000001; KRX28221.1; -; Genomic_DNA.
DR Proteomes; UP000054630; 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 CDD; cd04717; BAH_polybromo; 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 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; 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; 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:UP000054630};
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 964..1082
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1180..1295
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1395..1457
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1476..1504
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1827..2088
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 1395..1457
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2108..2129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1434..1461
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2129 AA; 243710 MW; 9FAC56AFCE0AD188 CRC64;
MTSKRAHSSD EVPLAKRLRR SALSSAAEEQ VAKHIRELFT RMRDFVNEDG RHVSRPFFRF
ASKKLTPEYV KIVTNPMDLT LIHEKVKQDE YANVDQFMSD VNLMVENAKN FYKKDSVEYG
DACDLWNMIT EARNKQECNS DSMSEFSNRS IDSSPTPSLS PKRENVNNRT QACLLEKLLC
TVLTAKSEDG LLCEAFKVIP SKEEWPYYYE VIRDPIDLRT ISMKLRRGRY RSVNDLEKDL
NQLCRNAKLF NEPSSSVYRA ANAIRKLVAH RKMELTDSNA KSSSYYHEMK KTSAVIDNFL
REVCAVVEED SDDEQIPLST NAQLKNLYTF LRSCRDELSG QCLVEPFLRC PDRSSFPKYY
EKIAMPISFY AINHKLKVGL YNAVSGMLDD ISLLCSNVKV YFGENSELYK RALKLQLMAF
SKIQDTDTSQ LELSVWKDLE HLAGLDDVPK TESTLHLPAV KLEFNEESTR GKVGRKSFDD
ALAQYREKLL SVYNTVVNYR DQTGRVVAMA FMEKPSKKLY PDYYKVIPEP IDLHMIKATI
DSDRYTSSQA LAADFELLFE NARHYNEDYS TIYTDANTLN GVFADAMKHV FPTPLTIPKC
SKARRSNYNF ILKDRSRRGS YSSDSSGNRV SRKSQNISLG EHELKLWYIY QAIKEFRDPN
NRTLSSVFLK LPSRTDYPDY YEVIRKPIDL QKICNKLSAK QYDSVEALVS DFALMFDNAC
KFNDPDSLIY KDALTLQRVL IQKAAELRRG EQHSPPIDVQ SDVQELLNRI FSDVLNYQDD
LGRCLSDSLY EADEEYLIKT KDKDAVTLNI IKKRLEMKWY TRLDRFQQDM LEVFKRARRL
KSVNSQIFED SVDLQSYFIK VRDELTKRGD LFYSSAMRFT EKDLISEIDA MRRRNASKSN
LESEVEDNSI NEPKVSRLGS LINAVVDIQH FEAGLSFAVI KGRVDMKSCG EGDVELSSVD
VGGTVYNVGH FAYVKQQQNN YKPRILLISR IWKQPTGAVG IFGNWYYRPS ETCHVSVRKF
LKNEVFRTDA YDRVEPSALA GRCHVLFIKT FVNHKPTNFA DEDVYVCESR YSVVSQEFKK
IKVSKQASWQ LSSQGVHLED RSTPCLLLRM PLNLEPHDAN NRNLLSSVQQ EESTNKQEDN
NNNNNSCLLV ADTGRTDVVV AGQKENLSTV AYEQIQLNGC WIRLGDCVYI RVSEHEVKVV
LVERIWKSQD DILLHGIPFV SPHQIEHEPT QMFYKKELFA VEPSETFSGR SVVGRCAVLS
LKDYCSSRPT EVNEADVFLC DSRAVWNEYG KRVIPDNPER KFKLPTFRLS CEVPEDEVAF
FKKPMNAEKE PSPFLMQRAI VYNDLPLPEQ KNSNIGCFNS EIAESSSSTI STTTTSTTTT
NTTVRVDTPS TPKLTSRSKS GYILFSAVIR KRIMAENPEC SFGHISKIVG AEWKKLSEEE
KKKYEEEAQK IAEEREKADQ LTGGRLQLLP GQIRVYCCKW RDCDYQFDTV EQLNEHITSM
HTSQIVEGSD NQYVCMWLTC SKYRKEGRPF PSLARLHRHI KEKHMPQSLK CLFPQNLGKH
YISMSSTSGL DSAQLAQTSM SAFQQQQQQQ QTEQHQYYQQ QQYLEQQQQN AVLMSTPTPA
HQFSNVAQTQ PIRYAPPGSS INAPSAHVAY DNQTAGGAYP MHYSGQPLSP AVQQTMASSH
GGRVRSPASF SMPATPTKSS VDPGSILVRA LEKPVEPIQL QPQVLRVSKV VHSKTYLNWA
RNRSGRTLTL SGDNSELKKA RKIDTLESIA MDSKKTDAVV QALNIMTKAL YCRVDILLDI
LAQLGWQEMV SMTSSINVQI GDVIGNWKLT KLLGFGTYGY VYEVLNLKND QLEAMKLEDQ
NPNQSLKVEI LVLRSLNKHN ARHCCQLLGS GRKDKFSYIV ITLVGKTFED ISQVMKEKHG
DSGKLDSCSA MYLCMQALEG LQDLHTICFI HRDVKPQNFA IGVHPNLRNV YMLDFGTVRK
YLRSDGKHRR PRAKAGFRGT FNFASVYALN LDDQSRRDDM WSWMYLLIQM TTGTLPWLDM
PPTGNYFSEL EQYKNIKNEH IDNPAVLLNG CPEEYYAIFN IIKQMTYYSA PEYEGIYELL
KLSMKKENSS SEDEPLQYEK ILNEETAHK
//
