ID A0A0V1HAT3_9BILA Unreviewed; 2084 AA.
AC A0A0V1HAT3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Protein polybromo-1 {ECO:0000313|EMBL:KRZ07950.1};
DE Flags: Fragment;
GN Name=PBRM1 {ECO:0000313|EMBL:KRZ07950.1};
GN ORFNames=T11_1130 {ECO:0000313|EMBL:KRZ07950.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ07950.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ07950.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ07950.1};
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:KRZ07950.1}.
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DR EMBL; JYDP01000094; KRZ07950.1; -; 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 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: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 500..570
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 657..727
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 925..1043
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1133..1248
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 1346..1408
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 1427..1455
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1782..2076
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DNA_BIND 1346..1408
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 1073..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1385..1412
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1075..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2084
FT /evidence="ECO:0000313|EMBL:KRZ07950.1"
SQ SEQUENCE 2084 AA; 238414 MW; 1A98D47D085757CB 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 LELSDLEHLA GLDDVPKAES TLHLPAVKLE FNEESARGKV GRKSFDDALT
QYREKLLSVY NAVVNYRDQT GRVVAMAFME KPSKKLYPDY YKVIPEPIDL HMIKAAIDSD
RYTSSQALAA DFELLFENAR HYNEDYSAIY TDANTLNGVF ADAMKHVFPT PLTIPRCSKA
RRSNYNFILK DRSRRGSYSS DSSGNRVSRK SQNISLGEHE LKLWYIYQAI KEFRDPNNRT
LSSVFLKLPS RTDYPDYYEV IRKPIDLQKI CNKLSAKQYD SVEALVSDFA LMFDNACKFN
DPDSLIYKDA LTLQRVLIQK AAELRRGEQH SPPIDVQSDV QELLNRIFSD VLNYQDDLGR
CLSDSLYEAD EEYLIKSKDK NAVTLNIIKK RLAMKWYTRL DRFQQDMLEV FKRARRLKSV
NSQIFEDSVD LQSYFIKVRD ELTKRGDLFY SSAMRFTEKD LISEIDAMRR RNASKSNLES
EVEDNSINEP QEGDVELSSV DVDGIVYNVG HFAYVKHQQN NYKPRILLIS RIWKQSTGAI
GIFGNWYYRP SETCHVSLRK FLKNEVFRTD DYDRIEPSAL AGRCHVLFIK TFVNHKPTNF
ADEDVYVCES RYSIVSQEFK KIKSWQLSSQ GVHLEDRSTP CLLLRMPLNL EPHDDNNGNV
LSSAQQEEST NKQDDNSNSC LLVVDTGRTD VVVGGQKENS STVAYEQIQL NGCWIRLGDC
VYIRVAEHEV KVVLVERIWK SQGDILLHGI PFVGPHQIEH EPTQMFYKKE LFAIEPSETF
NGRSVVGRCA VLSLKDYCSS RPTEVNEADV FLCDSRAIWN EYGKRVIPDN PERKFKIPTF
RLSCEVPEDE VVFFKKPMNA DKEPSPFLMQ RAIVYNDLPL PEQKNDNSRC SNSEIAEPSN
STIATTSTTT TTTTVRVDTP STPKLTSRSK SGYILFSAVI RKRIMAENPE CSFGHISKIV
GGEWKKLSEE EKKKYEEEAQ KIAEEREKAD QLTGGRLHLL PGQIRVYCCK WRDCDYQFDT
VEQLNEHITS MHTSQIVEGS DNQYVCMWLT CSKYRKEGRP FPSLARLHRH IKEKHLPQSA
KCLFPQNLGK HYISISSSSG LDSAQLAQTS MSAFQQQQQQ QQQQTEQHQY YQQQHYLEQQ
QQNAVLMSTS TPAHQFSNVA QTQPIRYASP GSINTPSAHV VYDCSGNQVA GGAYPMHYSG
QPLSPAVQQT MASSSHGGRV RSPASFSMPA TPTKSSVDPG SILVRALEKP VEPIQLQPQV
LRVSKVVHSK KYLNWARNRS GRSSTLSGDN FALKKARKID TLESIAMDSK KTDAVVQALN
LMTKTLYCLL LHVFAQQLLG WQKMASMTSN ICVQVGDIID SWKLTKLLGF GTYGSVYEVL
NLKNDQLEAM KLEDQTSEVS SLKIEILVLR SLNKHNARHC CQLLGSGRKD KFNYMVITLV
GKTFEDISQV MKEKHSGDGK LDSCSAMYLC MQALEGLQDL HAICFIHRDV KPQNFAIGVH
PNVRNVYILD FGTVRKYLRS DGKHRRPRAK AGFRGTFNFA SVYALNLDDQ SRRDDMWSWM
YLLIQMTTGT LPWLDLPPAG NYFSELEQYK TMKNEHMENP AVLLDGCPEE YYAIFNIIKQ
MNYYSAPEYD GIYELLKFSM NRENSSSESL QYEQILNEEA AKNK
//
