ID A0A0V1AEI1_9BILA Unreviewed; 1796 AA.
AC A0A0V1AEI1;
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:KRY23234.1};
GN Name=BAZ2B {ECO:0000313|EMBL:KRY23234.1};
GN ORFNames=T12_7999 {ECO:0000313|EMBL:KRY23234.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY23234.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY23234.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY23234.1};
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:KRY23234.1}.
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DR EMBL; JYDQ01000004; KRY23234.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V1AEI1; -.
DR Proteomes; UP000054783; 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:UP000054783};
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 657..729
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 903..967
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1513..1563
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1567..1616
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1700..1770
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 612..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1676
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..280
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 458..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1796 AA; 194312 MW; 0904892DA448EA49 CRC64;
MDISRPSSSS SGLGRGGSLC STNGCADNGR PNSVSSSASA SSQSPFGTTV EQLMGSRSVS
AAANAAASLS NASAFSSVGG GGGSFASFNP FFFPFMPYAV GGASPISGFW PYAFPATTGD
YFLQMATLFG GRNQQSAGAG AAAATGSAAA ASVLEESFPE ILHRLSKAAS GNTAEQTTVM
QACSSSSSSP NAASTAAAES SPPPVVEQAA ASFWTKGESS SSSSSTSGAG SLVQKSQTGG
SGQPRTKQRQ QSAGDKRRAD EQIDFSNPKR RGESGGKRKS PDEQVMTTST SNGGSTTVGD
EPTSTSTTGS GGSGSGGGKR FAVSPLDQQN IFNASAAAWA ALSNQILLTN LQTGLFTGGL
GAAANPVQQA AEPPSVAVTV PSIASTDDRA TSASTTLPST MTSPLKRTTT TTLEPEPATP
TRASGARQAT TGGGRRAVSS RRGRTPTASR RGSAGRGRPA TISSNDTRRP APSASTLDPK
ETNRSSVDDT IDDVASGQPR SPAALSQFYF AFSSLDHFMN PNAYAASAGT AGRSGPGRPR
RRAGRGSRGG ITVRQQLAMM KRAGSGVGST TAVGNKASPQ AQPVVIESTD ANFVDTSTTT
TTATTAALDL RTKSNKATPT QQHADLSSSG TQHATNGHLD NNLMEKNLGE TTNRKRVVNP
KLLRNPILCG WRRQTVIRHI SASGIRGDVL YYAPCGKRLG SYVEVMRYLR KNGIINLTKE
DFSFSSKIIV GEFVCNRRDS LKSGLVNLSE SDVLTLLSQL KNGSGGSLSS SMKNSPNEGA
NDSLSRRSKR VTTALVRKSS VTKATTQRRK LEFKQSDGER GGRVRNLKAQ QKLKKQQNKQ
EAPAVKRVVA KAAAVMREEQ KLLKNNEKEV KVRQVRVPVE DTEVEHAKPL PEFTPVKHLQ
LDSSAFADLL MVMQFVTTFG HVLNIKKSDI PSLATMHAGL LNNPPDQQAV VNLTKTLLSL
LLEYSNLPTG ASAVCTCTGL TLKDETVTDA NYSELLRLFF TSRDDPSCLQ LSNSLESNSF
EAVDPSVKVR MLAYMCNDLL YCRNVVREVE SNIEELAKLK SDKWSKKGKI RALRLARAAK
VGEQQQKKVV VVGKDKKLDE SAVSELGASS AEKYDPNAEA NNNQQLHNCD ESTKDDLKSE
QQQQQQQQGG GEPGHSGALF ESELTPEEKQ MSPEEIDKMI DTLSKEVDQM RCKISNRGLK
IRSLPLGQDR LRRNYWMINE IRGILVQSVE SGSNTVETDV RDCVTALRDA VVALMNDDHH
QGSIAENDAI EADDRLLKSA YAKASAPAGG GGCDSCCWWI IDQPSKVDEL LQSLSQRGIR
ERLFSRSLAK YSDTYKECAF GDKSAIELTP TIRRSGPSFV EQMMTVLTAM QQLEDKCYQA
NIHVPGWHPE EGGEYNNNNN NNNNYSAESE LSLLNNDNGD ILALVKARLL NLEKNIERRY
LTPFINHNEA KMFQSNSSRA KLSSKGNGGI SEDLPAQIVH WRQGVDGARS AAQFHMCMDA
LESFVAWEKS IMKAMCQICR DDCNESQLLL CDGCDMGYHT YCFRPKMTKV PEEDWYCPEC
VAKATRRSCC LVCCRHSSQP MLACAECGRE YHAECVDLDP VKSVKSNWRC FGCCKLRKSL
SNGPSTPKRR KLESKEKRRP VESSNKKSPN KKVVKSEKKK QQPEKKTASN SGSPTTATTA
VTYSGFDYEE ICSIILAELD AHRDSWPFKK PVDSKLVPLY KKVIKKPMDL SAIHAKLISH
KYQRGEDFVK DVNLVFDNCK TFNEDDSKIG KAGHSLRRFF TRRWKELHAA TQLKRF
//
