ID A0A0V1M9I2_9BILA Unreviewed; 2121 AA.
AC A0A0V1M9I2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Protein polybromo-1 {ECO:0000313|EMBL:KRZ68541.1};
DE Flags: Fragment;
GN Name=PBRM1 {ECO:0000313|EMBL:KRZ68541.1};
GN ORFNames=T10_2587 {ECO:0000313|EMBL:KRZ68541.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ68541.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ68541.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ68541.1};
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:KRZ68541.1}.
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; JYDO01000162; KRZ68541.1; -; Genomic_DNA.
DR STRING; 268474.A0A0V1M9I2; -.
DR Proteomes; UP000054843; 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; 1.
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; 1.
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:UP000054843};
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 962..1080
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1381..1443
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1462..1490
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1819..2113
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 1381..1443
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 1115..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1420..1447
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1117..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2121
FT /evidence="ECO:0000313|EMBL:KRZ68541.1"
SQ SEQUENCE 2121 AA; 242401 MW; 4E656ED2C005021B CRC64;
MTSKRAHSSD EVPLAKRLRR SALSSAAEEQ VAKHIRELFT RMRDFVNEDG RHVSRPFFRF
ASKKLTPEYV KIVTNPMDLT LIHEKVKQDE YANVDQFMSD VNLMVENAKN FYKKDSVEYG
DACDLWNMIT EARNKQECNS DTMSEFSNRS IESSPTPSLS PKRENVSNRT QACLLEKLLC
TILTAKSEDG LLCEAFKVIP SKEEWPYYYE VIHDPIDLRT ISMKLRRGRY RSVNDLEKDL
NQLCRNAKLF NEPSSSVYRA ANAIRKLVAH RKMELTDSNA KSSSYCHEMK KTTAVIDNFL
REVCAVVEED SDDEQIPMST 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 EADEEYLIKT KDKNAVTLNI IKKRLEMKWY TRLDRFQQDM LEVFKRARRL
KSVNSQIFED SVDLQSYFIK VRDELTKRGD LFYSSAMRFT EKDLISEIDA MRRRNASKSN
LESEVEDNSI NEPQVRLGSL INAVDIQHSE AGLSFAVKKG RVDMRSCCEG DVELSSVDVD
GIVYNVGHFA YVKHQQNNYK PRILLISRIW KQSTGAIGIF GNWYYRPSET CHVSVRKFLK
NEVFRTDDYD RIEPSALVGR CHVLFIKTFV NHKPTNFADE DVYVCESRYS IVSQEFKKIK
VSKQASWQLS SQGVHLEDRS TPCLLLRMPL NLEPHDDNNG NVLSSAQQEE STNKQDDNSN
SCLLVVDTGR TDVVVGGQKE NSSTVAYEQI QLNGFWIRLG DCVYIRVAEH EVKVVLVERI
WKSQGDILLH GIPFVGPHQI EHEPTQMFYK KELFAIEPSE TFNGRSVVGP RPTEVNEADV
FLCDSRAIWN EYGKRVIPDN PERKFKIPTF RLSCEVPEDE VVFFKKPMNA EKEPSPFLMQ
RAIVYNDLPL PEQKNDNSRC FNSEIAEPSS SSSTIATSTS TTTTTTSTTV RVDTPSTPKL
TSRSKSGYIL FSAVIRKRIM AENPECSFGH ISKIVGGEWK KLSEEEKKKY EEEAQKIAEE
REKADQLTGG RLHLLPGQIR VYCCKWRDCD YQFDTVEQLN EHITSMHTSQ IVEGSDNQYV
CMWLTCSKYR KEGRPFPSLA RLHRHIKEKH LPQSAKCLFP QNLGKHYISI SSSSGLDSAQ
LAQTSMSAFH QQQQQQQTEQ HQYYQQQHYL EQQQQNAVLM STSTPAHQFS NVAQTQPMRY
ASPGSINAPS AHVVYDCSGN QVAGGAYPMH YSSGQPLSPA VQQTMASSSH GGRVRSPASF
SMPATPTKSS VDPGSILVRA LEKPVEPIQL QPQVLRVSKV VHSKKYLNWV RNRSGRSSTL
SGDNFALKKA RKIDTLESIA MDSKKTDAVV QALNIMTKTL GDEISVLLHV FAQQLLGWQK
MASMTSNICV QVGDIIDSWK LTKLLGFGTY GSVYEVLNLK NDQLEAMKLE DQTSEVSSLK
IEILVLRSLN KHNARHCCQL VGSGRKDKFN YMVITLVGKT FEDILQVMKE KHSGDGKLDS
CSAMYLCMQA LEGLQDLHAI CFIHRDVKPQ NFAIGVHPNL RNVYMLDFGT VRKYLRSDGK
HRRPRAKAGF RGTFNFASVY ALNLDDQSRR DDMWSWMYLL IQMTTGTLPW LDLPPAGNYF
SELEQYKTMK NEHMENPAVL LDGCPEEYYA IFNIIKQMNY YSAPEYDGIY ELLKFSMNRE
NSSSESLQYE QILNEEAAKD K
//
