ID A0A0V1PKY4_9BILA Unreviewed; 2203 AA.
AC A0A0V1PKY4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Protein polybromo-1 {ECO:0000313|EMBL:KRZ96893.1};
GN Name=Ttbk1 {ECO:0000313|EMBL:KRZ96893.1};
GN ORFNames=T08_1130 {ECO:0000313|EMBL:KRZ96893.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96893.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96893.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96893.1};
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:KRZ96893.1}.
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DR EMBL; JYDM01000005; KRZ96893.1; -; Genomic_DNA.
DR STRING; 92180.A0A0V1PKY4; -.
DR Proteomes; UP000054924; 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:UP000054924};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 48..118
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 187..257
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 338..408
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 502..572
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 690..760
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 994..1112
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1207..1322
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1418..1480
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1499..1527
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1901..2203
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 1418..1480
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 139..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1457..1484
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2203 AA; 252118 MW; B0247ECAF4E9E4F8 CRC64;
MTSKRAHSSD EVPLAKRLRR SALSSAAEEQ AKHIRELFTR MRDFVNEDGR HVSRPFFRFA
SKKLTPEYVK IVTNPMDLTL IHEKVKQDEY ANVDQFMSDV NLMVENAKNF YKKDSVEYGD
ACDLWNMITE ARNKQECNSD SMSEFSNRSI DSSPTPSLSP KRENVNNRTQ ACLLEKLLCT
VLTAKSEDGL LCEAFKVIPS KEEWPYYYEV IRDPIDLRTI SMKLRRGRYR SVNDLEKDLN
QLCRNAKLFN EPSSSVYRAA NAIRKLVAHR KMELTDSNAK SSSYYHEMKK NSAVIDNFLR
EVCAVVEEDS DDEQIPLSTN AQLKNLYTFL RSCRDELSGQ CLVEPFLRCP DRNSFPKYYE
KIAMPISFYA INHKLKVGLY NAVSGMLDDI SLLCSNVKVY FGENSELYKR ALKLQLLAFS
KIQDTDTSQL ELSVWKDLEH LAGLDDVPKT ESTLHLPAVK LEFNEESARG KVGRKSFDDA
LAQYREKLLS VYNTVVNYRD QTGRVVALAF MEKPSKKLYP DYYKVIPEPI DLHMIKATID
SDRYTSSQAL AADFELLFEN ARHYNEDYSA IYTDANTLNG VFADAMKHVF PTPLTIPKCG
KASHHVCQLD ASGASSTDHT HVHKKNKLNS SNGWRSNYNF 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 LESEAEDNSI NEPKVRRLGS LINAVVDIHH
FKAGLSFAVI KGRVDMKSCG EGDVELSSVD VGGTVYNVGH FAYVKQQQNN YKPRILLISR
IWKQPTGAVG IFGNWYYRPS ETCHVSVRKF LKNEVFRTDA YDRVEPSALA GRCHVLFIKT
FVNHKPTNFA DEDVYVCESR YSVVSQEFKK IKVSMQASWQ LSSQGVHLED RSTPCLLLRM
PLNLEPHDAN NGNLLSSVQQ EESTNKQEDN NSSCLLVADT GRTDVVVAGQ KENLSTVAYE
QIQLNGCWIR LGDCVYIRIS EHEVKVVLVE RIWKSQDDIL LHGIPFVSPH QIEHEPTQMF
YKKELFAVEP SETFSGRSVV GRCAVLSLKD YCSSRPTEVN EADVFLCDSR AVWNEYGKRV
IPDNPERKFK LPTFRLSCEV PEDEVAFFKK PMNAEKEPSP FLMQRAIVYN DLPLPEQKNN
NIRFSNSEIA EPSSSTISTT ATTTTTVRVD TPSTPKLTSR SKSGYILFSA VIRKRIMAEN
PECSFGHISK IVGAEWKKLS EEEKKKYEEE AQKIAEEREK ADQLTGGRLQ LLPGQIRVYC
CKWRDCDYQF DTVEQLNEHI TSMHTSQIVE GSDNQYVCMW LTCSKYRKEG RPFPSLARLH
RHIKEKHMPQ SVKCLFPQNL GKHYISMSSS SGLDSAQLAQ TSISAFQQQQ TEQHQYYQQQ
QYLEQQQQNA VLMSTPTPAH QFSNVAQTQP IRYAPPPGSS INAPSAHVAY DNQIAGGAYP
MHYSGQPLSP AVQQTMASSH GGRVRSPASF SMPATPTKSS VDPGSILVRA LEKPVEPIQL
QPQVLHVSKV VHSKTYLNWA RNRSGRTLTL SGDSSELKKA RKIDTLESIA MDSKKTDAVV
QALNIMTKAL YCRVDSLRNL WETNYFCCCT DFALFWTFAM FICWLFQGKK IAVSSILISN
EKIKDDEFLV LLDVLAQLGW QKMASITSNI SVQIGDVIGN WKLTKLLGFG TYGYVYEVLN
LKNDQLEAMK LEDQNPNQSL KVEILVLRSL NKHNARHCCQ LLGSGRKDKF SYMVITLVGK
TFEDISQVMK EKHGDNGKLD SCSAMYLCMQ ALEGLQDLHT LCFIHRDVKP QNFAIGVHPN
LRNVYMLDFG TVRKYLRSDG KHRRPRAKAG FRGTFNFASV YALNLDDQSR RDDMWSWMYL
LIQMTTGTLP WLDMPPTGNY FAELEQYKTM KNEHIENPAV LLNGCPEEYY AIFNIIKQMT
YYSAPEYEGI YELLKFSMKR ENSLSEDEPL QYEKILNEET AHK
//
