ID A0A158PQF1_BRUPA Unreviewed; 2200 AA.
AC A0A158PQF1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=DDT domain-containing protein {ECO:0000313|WBParaSite:BPAG_0000171301-mRNA-1};
GN ORFNames=BPAG_LOCUS1694 {ECO:0000313|EMBL:VDN82880.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000171301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0000171301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN82880.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UZAD01000154; VDN82880.1; -; Genomic_DNA.
DR STRING; 6280.A0A158PQF1; -.
DR WBParaSite; BPAG_0000171301-mRNA-1; BPAG_0000171301-mRNA-1; BPAG_0000171301.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; Unassembled WGS sequence.
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); 3.
DR InterPro; IPR038028; BPTF.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_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; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000278627};
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 176..236
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 327..372
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1943..1994
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2001..2052
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2084..2154
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1846..1880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1243
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1918..1936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2200 AA; 251128 MW; 5342FD31B65B12B5 CRC64;
MPRGRPRGRG RSSAGKTVAK SSPSCYGRNR GRAKLTGISM KSKSTKTSKS RENRQAWDES
DEEYDRPDYY TDSSDGFDSD TSTAQRSSLF YSPEFSFVEI YFVNKLMIDS AAMDLEDEAE
DEEIEETSSV ASRVPTPGAS LYETDESVEC PWLEIPAEQL PILKLPKGSK DLLIDEKYLF
DALEVYETCR WYYQAIRLSP FLFEDFCAAL STEGQTNLLA EIHIALLKLS LKDDDDEQII
LSVQDTNNSF NIMLQLLEPM TYAEVLRQYL ESDPQRFPAE VLEAASGNYP FVGVKQRLTV
LSWLCDRFFQ TNEYRNIVRN EGKLTVDEHC RECGKPGDVL LCDGCEACYH LSCTNLADVP
DGKWLCQVCE LHKVRGVTDC QVPGYRSPRM PMRFKPLGRD RHGRLYWFMV RRIFVQNDID
GSVHYYSTLP QLYFLLNMLS VNEYEKHLAA VFMDLLPLIE EHMRMTLQLT GDYGRSARAR
NKTDLYLHAD NVIRMGGILA KPLFSQLRES DDERIVVAIG YTKHVEVSKY LLLCKVEELL
GFTGNCLKDT FWTAGMQTHE VITKKEVIET SFHTALVNGD IDEVHSVELG FRLGEGDTLS
HYVNQYSMNE YAKNPIQRAK ERDKKKYMSG RFSLMDEGEF EWTVAKGRTL TGTPIQIGKI
IQNSMESFAQ KIPSVLMHRL WKRDGLDYFK KGLSAPPTVE LLKDLLLRFE CAIRRPVLHN
VWWSTLGHTR LIRITVEDRE RRQRYETKKK KQERELWAAE PDDDEVIWVK HHKVGSILKR
TLWRQNDEGY RVNGRGTLGG WLWKSNTFHR TFIPRAEKPN IGKILEPTSL ANRKAIHLEK
IVKCLNEWRI AELEGEERKW QKELLKKCYS PTCRMGIMPL PITSENDSVQ GCYSLTCRQA
VSQSMGRTTS SVVHARPPSS SPSKSQQENG KDVKTLEMNK PFPLPLPFDY RVRRTGEQKL
TDKFFRALKR LARQGGINLN YFAPGFHRLA KSNNQVWNYP CQRPLFDNCW RYLVLRAQSY
HSIALHLRVL YACIRWADMH REPDEVSFYS LNQDRKADFR VTVHLADHDE VRTVIGHKEY
PPDGMYEQYK LSVELIPLDD NVELDDANEG LGSAAYHPSK SLEKTLRKRK ATRGRSENGA
VRKDHVKVVE RWIDGIELKP WEIANYWKNI ENRARRGLNA PSVVTVGNRI PAPVIKHHES
PTVHSNRISG ERRRPQPKRM PDYDYDIKDD EDEDDDDEYI DVETLPSIVE KSNSSLEPRP
KVSRLSEQRS ERHLAESPYK AQWQNPNILR QYEQVARRPG ELLGGGKYTM FQKPDGTFCR
VMVYQNHPTQ STRTASAPGS VRTPPMIASQ PRTGTYQRES VRIPVTRRVV SVPGSSHGSP
VAPVGKRLLL IRRSDGTTQY LRPVTTGTGT PGAYRTVRTT QAGGATINDV RGSATNSPFV
RPLGTTRTVF TGNQSVGRVL RLPARTVSVV NQPSSENQAS STVRIGRMQP KRRVDGDEML
SDHSTDPSTA QVDEEYRLLT EKGLRSSGKP LGTAPVSGST RPAVTVQPRQ GLTAVVHSSL
DQQTSSGHIF GDHDPMVGSG SSAIGGDRYA NMVRTETRTA GVTVRAHHGA EVVRVRLHGR
GVSSLYGKTQ NELTDMTSSV GHSYASSRTH IKYIGTIDIR SNLYIRPFEQ VDQRVIKEVL
DNLITEVCIM DAENGWHRRH IQRIFEERQE ERKRREMQQR ALKIERLSAR QLETELGERI
EWFKREVNKR RLKLEERAEA EAGMIAPWRR PRRARELFPD SSAQLQAIAG MPVEPSTISL
GGIIHSDETA SNKVDEQSTI QLPSENSNVH CAKTTGLIPD LSIQQQSGEL SVKDQPLMDS
GQQVEDTSQQ RRSERSKKKK SWDESFIKIE SLSTSQIPDS SETKTNGKAR KEQRRMTRGT
TPSTSSRPGT ACSESIPDID TTKRHCKCNQ PYDPKKFYVG CDLCYQWFHG KCVGISERKS
KKMTSWLCAD CAKEQKSSEK ELYCVCQTPY DDSQFYVGCD GCEGWFHPRC VDITQEDAEK
AAEYLCPQCT QNKQANESST SSSPPILLDR PDFDLLWHAF DSLKSHRTSW PFRQAVDQKD
HPDYYSIIKK PMDLSIVQQK LEHYEYHSLK EFTTDIAQIF ENARIFNSKD SAIYQCADIL
EKQFRERIVK VKSSIETRAS GKKGVSIFKC LYKKLISDAI
//
