ID G0P3M3_CAEBE Unreviewed; 2469 AA.
AC G0P3M3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGT44274.1};
GN ORFNames=CAEBREN_14128 {ECO:0000313|EMBL:EGT44274.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL380047; EGT44274.1; -; Genomic_DNA.
DR STRING; 135651.G0P3M3; -.
DR EnsemblMetazoa; CBN14128.1; CBN14128.1; WBGene00152853.
DR eggNOG; KOG1473; Eukaryota.
DR eggNOG; KOG1632; Eukaryota.
DR HOGENOM; CLU_000284_0_0_1; -.
DR InParanoid; G0P3M3; -.
DR OMA; FEDFCTA; -.
DR Proteomes; UP000008068; 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; 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; 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; 2.
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; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
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:UP000008068};
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 204..264
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 2173..2224
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2233..2284
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2321..2391
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2425..2450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2469 AA; 283119 MW; F67FF19DA810EF24 CRC64;
MGPRGRSKRK LHSESGTSVG DSEEIDDTTT TVASASRPRR SRVPKRYLDD DYSPPPSKKR
AGNRSTPSDA GDEEVDVKLE PIRPSSQQTP KGSVATPGTS RSLKSRGRPK KNPTPPRRKS
LKQRQEDDVI YMDDDSEEEE ESSDDEFIMN EEQKDDLDYS DEDLNFSDIK PNIEEETFCP
WIENPETLPK LDLPETSQDI PIPISSTMDA IEIYEILRSY HRTLRITPFT FEDFCAALIS
KNNSCIMAEV HMALLRVCLK SDDEELTQYS VTETNNSVNI MIHHMDTLTY AEILRQYIEA
YPFTDSCVRD AINVENYPYV GYEPKIVVLL FMSYRFLYSS EFKKVVSNMG RFQTDENCRV
CGKSNGRVVG CSQCEASFHV ECSNLKPFPE ILVCNICKRN SVRGVLPLDE TVEKEPLRSQ
PIGRDRYGRF YWFICRRIII QSVDETEIHY YSTPPQLYQL LQRLDRHYYE KDLCEAIRLR
VDEFLEQMTL TVEMTAERRE AAIDNVMRKS MIGYEFAEAT ISPIYLHKDS MKRMASILRD
CSEKVIKQET TDTDQEEEDG TRSSGPLEKP VSFDEDSILP ESMLGIFNGS LINTFWSGGA
SQEELIQSFV QSPSINAQSL WRMGDEENDQ SFMQYYNYYM RNEMAESFLS RKKAADKKKY
MASKFSIIEQ FEWVVAKDRQ FYGNSVLHNK FVGWTLSKIA RKIPTDLMHR KWNEASKGFD
IEISVADDFK KLAHCLLQLD AVTRKTIYVQ QWWSGLGQTK LERITLDQRE NFNKDQQRNK
KLEMDALAKD LDDSFIRVNY SKPKWPNTYI LRQKGETYRN AGKGMMGGWA WVAKKYVEKW
VTIPKKPMLP LDDKTTEKKI ESTSNQKARN LERLITGIVR KRDCNKSASI VANNTLNNKC
YSPSCRNSKT FTVPNAICYS PSCRNGIFVG ANDRHVETET IKKEVLGEDK AWPIPEIQTF
ATKRGFKSIF VLQKKILRQM ILTAGCQQVY MPGFSAGIKS NLLIWPYPAP RPTLDLCWKW
QTLNSRSLHS VALQLKIMWS SIKWNEFEPD DTHPDRRVVI DTPSHDERRR IIRHKEMPPY
GQYERYELEI EIIPLYDEQE EEDDSWLSRN RSSDCSQRGT SRKKRSQRNL DNRQATAIRK
EWVDGVTLKA FEIKDYWKWV RMEAEKMVRR KIEAAKKMAK AKEDAERQRL MMLQRPVTVH
RVPSIALERT NVPYMGANRR SAIGIGQDSN ESGRNLEKYN NSDLQPRSSS MYYPPSTSSV
HRVQPNPVIR RVPVSSNAQL NRFPLQQNQY ITRVAAGADS TSNGTALAPQ RGISHSRQNS
PVGEPTTSTR QTLSTTEEVL GSNSPTNDSS DHQLPIGNFS STGPQRAQQP VRQIHPGQVV
VRPSPGTTGN VVYLKSTVGG TQKMMIRKAV GPSETIRHQG YPPGTVLDRG QSSHSARPIG
IQQSQQIRQI LTPGGAQRYV RVQNPINRQT DQTSRRVLHA GQQSPIESSQ HFPPQLQQPP
PVPQNPRFII QGRTPPPKPP NETDSILEAA TQMTQQHRDL NSDSSCVFGE PMRRVLPVAE
EAVGAHTTGS DNDDQPPIIP RYDPANSDTQ RLNQPARQVY TGQQVIRTMQ NSSGNKGNVI
YLKSTDGATQ KMMVRQSGKP DQSSYRSQDH VPGAVLPGGS RVVAVRSAGA PHTQQVRQMY
ASGSAPRYVR VQNTAGSQFQ RPMEQINRRI VHTGQQRRME FTDHDQGTNT QSQSLQQQTQ
HTRYVLQGAV SQPVNSTKTP RAVLPRGGMT MQMMQQAQHS DHRRLISSGR QKQKVTTYRD
FMASRGYLDA SKFMYGKIQT KPTFLPFEFN EEEEREINEA IAREEEWMRL EEENKISAYD
SAGNPIRTFT PSSDVNRAPP YVSNLLPSVD DTSDDKVIKQ VLDVMFSQVC RWDRQYGWSK
THMKRARQKN DNEKVHLRKV RMTQREVLIS EHMERLKKEI NKRRTKMENE AEQQCGLLTP
WRKSRTRPNR CDLSLSHLSS QQDPDFDLEH EMCSIFPKFE SAELDWEHFG YLLNDEMSKS
SEIKQKISTF HKPIEPIGKE TKRRRRNADM EIVELAAKPK SEVKKEVINP ADITLGGDTY
DYRDQKPLDS IAINVSRRRR TSATLSKSED EDEKKLHISA TTRCAKGRRT SEPTPRVTFY
APGLSSADID VAIPHCICQQ LFDSSKLYVS CDMCGRWYHG ECVNVTEKMC AKLEQWTCDQ
CTEEQERVKE QPALYCVCKK PYDDTKFYVG CDSCQGWFHP ECVGTTRADA EQAAEYNCPN
CLADSMGYES EGSEASVSSL FNVHLTRGDY SFVMELLELL LEHRMSTPFR NPIDCNECPD
YDKVIKKPMD LTTISRKVEQ TEYLFLGEFV NDVNLMFENA KTYNPKDNAV FKCAETMQEV
FDKKLYDVRE IMRAHQQVLL FQQQQQHNPI SSARKRVQSE SQKTTDSLDI DSDQLLPLDA
NLMSQLFDY
//
