ID A0A0N5D0Y7_THECL Unreviewed; 1556 AA.
AC A0A0N5D0Y7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2B {ECO:0000313|WBParaSite:TCLT_0000648601-mRNA-1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000648601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000648601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR WBParaSite; TCLT_0000648601-mRNA-1; TCLT_0000648601-mRNA-1; TCLT_0000648601.
DR OMA; GMIMWER; -.
DR Proteomes; UP000046394; Unplaced.
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; IPR018359; Bromodomain_CS.
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; SM00571; DDT; 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; PS00633; BROMODOMAIN_1; 1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 326..398
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 623..687
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1246..1296
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1300..1355
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1430..1500
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 80..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 864..891
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 80..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1556 AA; 174152 MW; 36B3E59291167E80 CRC64;
MGDQMQQNFL AMLAAQAVNQ NNMPMNLLFP NMNFPPANAL DMLLWNNVMQ LSQPGFFVPQ
QQLPQESFEE VLHRMAGVSS TSASISGSGN QQTAAEVDSR ESSSQPIGYS VSDIASTSTT
NLGLLNIDPD SPTKGLEPGE IPKRRDNNRS RNGISSLPTN QVPSTSGISL NSNILEASAR
CYAALAASAS QQQQQQQQQQ QLQQNEILAA VLQNAANFER ARFAVANTVT PSIRQGSSNT
CVNSVGNPSL KRITTAHQHV SNTSCKKEDN SRASGSLPAS STSSRLNESP LDLSFRKSKS
GSKERGRSFA DHASGVDSES SRKRTQVDAS LIRIPLKSGW RRQTCIRTIS ASGVRGDVIY
YAPCGKKLGS YAEVTRYLTK KNIKNIGREN FSFSCKVIVG EYILFKDDKD GSKVPDRVSE
EKILAEIANC SATNTVRRSS GAHVKAPSSL AGTDQSSTFV SAVDKNSMKL MEEATLRQLH
RQLLRRQGEQ HMYAQLLLSL CQGQQLQQRH LQLQQQQLPL ITTGDLLENQ KSRNLSAGAV
NIAVISTSTT ISTSATTTTT AVPTVIIPNT GAVETKPTKS DLTDEERQEE RLKALRLPTD
DLLIEEARKL PTLDSIENLS VNAPTFANVL MVDEFVRNFG HVLRIDPNTL PTLNEFLAGL
QNDPVHLKSF LLLTKTLLQL VLEYPGLPSG IAGRTPLGQA LKDVGVHREN YSELLKMFLL
SRDEEGKRLG AKLEGSSFEC LDPESKASIL AFLCNELLYC RNVVRDIESN MEEMTRLKGE
KWLREGKSRA LRAVQTRKRA ALKRLRHDIK DEDVASSRAG TPGSEPSESS EEVESLLQPS
RLKALTPGLG QCDVLTEEEE AMTVDELEAY IGRLNCEVEE LRERHNLLIN RVRIQPIGQD
RFHRFYWVLQ RIGVPLVESI ASSSLHNPAI NVDVTCRQDP PSIVEDPQIF INPDIIACVE
DILDILCGSE ERPDKGKKVR LRRLDNKCKR GWWMISNAKL MEQLRGAFHG RGIRERILHR
VLNKDNLTFK PMKLERVSRP LTINEINKAM INRISSLITS FEQKIVAANV HCRPMPSTGD
GRDDDAESEV SQDAWMFDDT YEFVNDAEAE EKRSFVEWDS FKKLKERLLE AEKSIERRYL
LHRYYAGTTI PAEKILFTQQ QNVQNGSNNV DASAVVDGGE PQSEPSESSS TSCHYDGEAI
AVDESGNTEL LQRWRDYVQK AKTGGQIMFA IQALDSAIAW EKSIMKASCQ ICRTSENESQ
LLLCDACDMG YHMYCFRPRI AVVPDGEWYC PLCVQRACRK VVCLLCSKWN QPNSHPIEPI
IVCSKCYNGY HISCFDRSPT VSDPKQWTCP GCLNADGFSS ELANSLLNGD VEMLVTQPEG
QGKQIVHVQE ETSGGKQETP RHRRRMTPAD YDFPPDMMKN LFYSMVEELW ARPESTPFQY
PVDTKEVPFY KKVIKKPMDL HQIRLNIEVN KYATQESFIE DVELIFENCR TFNEDESPVG
QLGAALHKFY VKRWKQLRYN YSKRLKRLRN PRTVHSVAVA SSSSPVIETS CPDLYS
//
