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Database: UniProt
Entry: A0A0R3R5L3_9BILA
LinkDB: A0A0R3R5L3_9BILA
Original site: A0A0R3R5L3_9BILA 
ID   A0A0R3R5L3_9BILA        Unreviewed;       401 AA.
AC   A0A0R3R5L3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=PHD-type domain-containing protein {ECO:0000313|WBParaSite:BTMF_0001530301-mRNA-1};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001530301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0001530301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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DR   AlphaFoldDB; A0A0R3R5L3; -.
DR   STRING; 42155.A0A0R3R5L3; -.
DR   WBParaSite; BTMF_0001530301-mRNA-1; BTMF_0001530301-mRNA-1; BTMF_0001530301.
DR   Proteomes; UP000050602; Unplaced.
DR   GO; GO:0016589; C:NURF complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
DR   CDD; cd15560; PHD2_3_BPTF; 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; IPR038028; BPTF.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
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; PTHR45975; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1.
DR   PANTHER; PTHR45975:SF2; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 2.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          144..195
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          202..253
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          285..355
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  45702 MW;  B543299F0DCED993 CRC64;
     LGGIIHSDET ASNKVDEQST IQLPSENSNV QCAKTTGLIP DLSIQQQSGE LSVKDQPLMD
     SGQQVEDTSQ QRRSERSKKK KSWDESFIKI ESLSTSQIPD SSETKTNGKT RKEQLRMTRG
     TTPSTSSRPG TACSESIPDI DTTKRHCKCN QPYDPKKFYV GCDLCYQWFH GKCVGISERK
     SKKMTSWLCA DCAKEQKSSE KELYCVCQTP YDDSQFYVGC DGCEGWFHPR CVDITQEDAE
     KAAEYLCPQC TQNKQANESS TSSSPPILLD RPDFDLLWHA FDSLKSHRTS WPFRQAVDQK
     NHPDYYSIIK KPMDLSIVQR KLEHYEYHSL KEFTTDIAQI FENARIFNSK DSAIYQCADI
     LEKQFRERIV KVKSAIETRA SGKKGVSIFK YLYKKLISDA N
//
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