ID A0A0V0UEC7_9BILA Unreviewed; 1793 AA.
AC A0A0V0UEC7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B {ECO:0000313|EMBL:KRX49059.1};
GN Name=BAZ2B {ECO:0000313|EMBL:KRX49059.1};
GN ORFNames=T05_4595 {ECO:0000313|EMBL:KRX49059.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX49059.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX49059.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX49059.1};
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 -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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:KRX49059.1}.
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DR EMBL; JYDJ01000021; KRX49059.1; -; Genomic_DNA.
DR STRING; 144512.A0A0V0UEC7; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15545; PHD_BAZ2A_like; 1.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45915:SF2; IP14655P-RELATED; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 658..730
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 904..968
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1510..1560
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1564..1613
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1697..1767
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1793 AA; 193951 MW; 1D319C4314266403 CRC64;
MDISRPSSSS SGLGRGGSLC STNGCADNGR PNSVSSSASA SSQSPFGTTV EQLMGSRSVS
AAANAAASLS NASAFSSVGG GGGSFASFNP FFFPFMPYAV GGASPISGFW PYAFPATTSD
YFLQMATLFG GRNQQSAGAG AAGATGSAAA ASVLEESFPE ILHRLSKAAS GNTAEQTTVM
QACSSSSSSP NAASTAAAES SPPPVVEQAA ASFWTKGESS SSSSSTSGAG SLVQKSQTGG
SGQPRTKQRQ QSAGDKRRAD EQIDFSNPKR RGESGGKLKS PDEQVMTTST SNGGSTTVGD
EPTSTSTTGS GGSGSGGGKR FAVSPLDQQN IFNASAAAWA ALSNQILLTN LQTGLFTGGL
GAAANPVQQA AEPPSVAVTV PSIASTDDRA TSASTTLPST MTSPLKRTTT TTLEPEPATP
TRVSGARQAT TGGGRRAVSS RRGRTPTASR RGAAGRGRPA TISSSDTRRP APSASTLDPK
ETNRSSVDDT IDDVASGQPR SPAALSQFYF AFSSLDHFMN PNAYAASTGS AGRSGPGRPR
RRAGRGSRGG ITVRQQLAMM KRAGSGVGST TAVGNKASPQ AQPVGIESTD ANVVDTSTTT
TTTATTAALD LRTKSNKATP TQQHADLSSS GTQHATNGHL DNNLMEKNLG ETTNRKRVVN
PKLLRNPILC GWRRQTVIRH ISASGIRGDV LYYAPCGKRL GSYVEVMRYL RKNGIINLTK
EDFSFSSKII VGEFVCNRRD SLKSGLVNLT ESDVLTLLSQ LKNGSGGSLS SSMKNSPNDG
ANDSLSRRSK RVTTALVRKS SVTKATTQRR KLEFKQSDGE RGGRVRNLKA QQKLKKQQNK
QEAPAVKRVV AKAAAVMREE QKLLKNNEKE VKVRQVRVPI EDTEVEHAKP LPEFTPVKHL
QLDSSAFADL LMVMQFVTTF GHVLNIKKSD IPSLATMHAG LLNNPPDQQA VVNLTKTLLS
LLLEYSNLPT GASAICTCTG LTLKDETVTD ANYSELLRLF FTSRDDPSCL QLANSLESNS
FEAVDPSVKV RMLAYMCNDL LYCRNVVREV ESNIEELAKL KSDKWSKKGK IRALRLARAA
KVGEQQQKKV VVVVGKDQKL DESAVSELGA SSAEKYDPNA EANNNQQLHN CDESTKDDLK
SEQQQQQQQQ GGGEPGHSGA LFESELTPEE KQMSPEEIDK MIDTLSKEVD QMRCKISNRG
LKIRSLPLGQ DRLRRNYWMI NEIRGILVQS VESGSNTVET DVRDCVTALR DAVVALMNDD
HHQGSIAEND AIEADDRQLK SAYAKASAPV GSGGDDSCCW WIIDQPSKVD ELLQSLSQRG
IRERLFSRSL AKYSDTYKEC AFGDKSAIEL TPTMRRSGPS FVEQMMTVLT AMQQLEDKCY
QANIHVPGWH PEEGGEYNNN NYSAESELSL LNNDNGDILA LVKARLLNLE KNIERRYLTP
FINHNEAKMF QSNSSRAKLS SKGNGGSLED LPAQIVHWRQ GVDGARSAAQ FHMCMDALES
FVAWEKSIMK AMCQICRDDC NESQLLLCDG CDMGYHTYCF RPKMTKVPEE DWYCPECVAK
ATRRSCCLVC CRHSSQPMLA CAECGREYHA ECVDLDPVKS VKSNWRCFGC CKLRKSLSNG
PSTPKRRKLE PKEKRRPVES SNKKSPNKKV VKSEKKKQQP EKKTASNSGS PTTATTAVTY
SGFDYEEICS IILAELDAHR DSWPFKKPVD SKLVPLYKKV IKKPMDLSAI HAKLISHKYQ
RGEDFVKDVN LVFDNCKTFN EDDSKIGKAG HSLRRFFTRR WKELHAATQL KRF
//
