ID A0A0V0RT76_9BILA Unreviewed; 1803 AA.
AC A0A0V0RT76;
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:KRX17683.1};
GN Name=BAZ2B {ECO:0000313|EMBL:KRX17683.1};
GN ORFNames=T07_15066 {ECO:0000313|EMBL:KRX17683.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX17683.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX17683.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX17683.1};
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:KRX17683.1}.
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; JYDL01000084; KRX17683.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0RT76; -.
DR Proteomes; UP000054630; 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:UP000054630};
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 666..738
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 912..976
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1520..1570
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1574..1623
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1707..1777
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 187..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1803 AA; 195096 MW; 2073C0742CB3C0C3 CRC64;
MHEEESLIET ITVDLTTTYT LLGRGGSLCS TNGCADNGRP NSVSSSASAS SQSPFGTTVE
QLMGSRSVSA AANAAASLSN ASAFSSVGGG GSSFASFNPF FFPFMPYAVG GASPISGFWP
YAFPAATGDY FLQMATLFGG RNQQSAGAGA AAAAATGSAA AASVLEESFP EILHRLSKAA
SGNTAEQTTV MQACSSSSSP NAAASTAAAE SSPPPVVEQA AASFWTKGES SSSSSSTSGA
GSLVQKSQTG GSGQPRTKQR QQSAGDKRRA DDQIDFSSPK RRGESGGKPK SPDEQVMTTS
TSNGGSTTVG DEPTSTSTTG SGGGSGGGKR FAVSPLDQQN IFNASAAAWA ALSNQILLTN
LQTGLFAGGL GAAANPVQQA AEPPPVAVTV PSIASTDDRV TSASTTLPST MTSPSKRTTT
TTLEPAPATP TRASGVRQAT MGGGRRAVSS RRGRTPTASR RGAAGRGRPA TISSNDTRRP
APSASTLDPK ETNRSSVDDT IDDVASGQPR SPAALSQFYF AFSSLDHFMN PNAYAASASS
TGRSGPGRPR RRAGRGSRGG ITVRQQLAMM KRAGSSVGST TAVGNKVSPQ AQPVAIESTD
ANVVDTVTTT TTTTAALDLR TKSNKATPTQ QHADLSSSGT QRATNGHLDN NLMENNLGET
TNRKRVVNPK LLRNPILCGW RRQTVIRHIS ASGIRGDVLY YAPCGKRLGS YVEVMRYLRK
NGIINLTKEN FSFSSKIIVG EFVCNRRDSL KSGLVNLSES DVLTLMSQLK NNGSGGSLPS
SMKNSPNDGA NDSLSRRSKR VTTALVRKSS VTKATTQRRK LEFKQSDGER GRVRNLKAQQ
KLKKQPNQQE APAVKRVVAK AAAVMREEQK LLKNNEKEVK VRQVRVPVED TEVEHAKPLP
EFTPVKHLQL DSSAFADLLM VMQFVTTFGH VLNIKKSDIP SLATMHAGLL NNPPDQQAVV
NLTKTLLSLL LEYSNLPTGA SAICTCTGVA LKDETVTDAN YSELLRLFFT SRDDPSCLQL
SNSLESNSFE AVDPSVKVRM LAYMCNDLLY CRNVVREVES NIEELAKLKS DKWSKKGKIR
ALRLARAAKV GEQQQKKVVV VGKDQKLDES VVSELGASSA EKYDPNAGAN NNQQLHNCDE
STKDDLKSEQ QQQQQQQGGA EPGHSGALFE SELTPEEKQM SPEEIDKMID TLSKEVDQMR
CKISNRGLKI RSLPLGQDRL RRNYWMINEI RGILVQSVES GSNTVETDVR DCVTALRDAV
VALMNDDHHQ GSIAENDAIE EADDRQLKSA YAKASAPAGG GGGGDSCCWW IIDQPSKVDE
LLQSLSQRGI RERLFSRSLA KYSDTYKECA FGDKSAIELT PTIRRSGPSF VEQMMTVLTA
MQQLEDKCYQ ANIHVPGWHP EEGGEYNNNN NYSAESELSL LNNDNGDILA LVKARLLNLE
KNIERRYLTP FINHNEAKMF QSNSSRAKLS SKGNDGSSED LPAQIVHWRQ GVDGARSAAQ
FHMCMDALES FVAWEKSIMK AMCQICRDDC NESQLLLCDG CDMGYHTYCF RPKMTKVPEE
DWYCPECVAK ATRRSCCLVC CRHSSQPMLA CAECGREYHA ECVDLDPVKS VKSNWRCFGC
CKLRKSLSNG PSAPKRRKLE PKEKRRPVES SKKKSPNKKV VKSEKKKQQP EKNASSNSGS
PTTATTAVTY SGFDYEEICS IILAELDAHR DSWPFKKPVD SKLVPLYKKV IKKPMDLSAI
HAKLISHKYQ RGEDFVKDVN LVFDNCKTFN EDDSKIGKAG HSLRRFFTRR WKELHAATQL
KRF
//
