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Database: UniProt
Entry: E3MHU4_CAERE
LinkDB: E3MHU4_CAERE
Original site: E3MHU4_CAERE 
ID   E3MHU4_CAERE            Unreviewed;      1504 AA.
AC   E3MHU4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFP02138.1};
GN   ORFNames=CRE_25005 {ECO:0000313|EMBL:EFP02138.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR   EMBL; DS268446; EFP02138.1; -; Genomic_DNA.
DR   RefSeq; XP_003104216.1; XM_003104168.1.
DR   STRING; 31234.E3MHU4; -.
DR   EnsemblMetazoa; CRE25005.1; CRE25005.1; WBGene00062191.
DR   eggNOG; KOG1245; Eukaryota.
DR   eggNOG; KOG2342; Eukaryota.
DR   HOGENOM; CLU_002479_0_0_1; -.
DR   InParanoid; E3MHU4; -.
DR   OMA; CEATGKD; -.
DR   OrthoDB; 1382023at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   CDD; cd04369; Bromodomain; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047171; BAZ1A.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR008551; TANGO2.
DR   InterPro; IPR028942; WHIM1_dom.
DR   InterPro; IPR028941; WHIM2_dom.
DR   InterPro; IPR013136; WSTF_Acf1_Cbp146.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46510; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR   PANTHER; PTHR46510:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF02791; DDT; 1.
DR   Pfam; PF05742; TANGO2; 1.
DR   Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR   Pfam; PF15612; WHIM1; 1.
DR   Pfam; PF15613; WSD; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS51136; WAC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000008281};
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}.
FT   DOMAIN          22..131
FT                   /note="WAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51136"
FT   DOMAIN          473..540
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          1409..1484
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          265..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1158..1211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1340..1376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          416..447
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        278..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1340..1369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1504 AA;  173592 MW;  360AE97DBAD9EC42 CRC64;
     MPLLNKQPFI PRPVPDGTTR ETRLWHCKPT GEFFASHEDF FKRMILLNTT SWSCSMTRKS
     NLTYFEAVQS EKEAEKELIE FPESLELPIL FITHKYTNRG RFEELVNDIY HIMKDRFFMN
     EEVTFNEKTR KLTARIVTSY CTQQQILDAN GMEVEIGHEI KEPLLPGADS YRYTIEILEQ
     GLSEGDKFRE HISNEKLFRS KNVGARQKIR LFLKNSCHLP PDGDRYTIRD CFIPKVESLW
     WSDVMSGSEP MCPQTPVLQR GRIPNMLKNG EDVGGGAAGA GERKERTPKR EKRDPSAPPR
     PRGRPPKTPE QRALAQQEKK QRKRAEAPPP GPDDFDLTSS GALTFHGHPM TSSSSPAKKK
     IRRSSTSKNE KKKAKIIEQQ GDLDFYFTEA RRLGIDVTGL EQDEKLLSPK KVAEFKMRVK
     EEKDVEREAL KEEKKRKIRE KAAYNKKRED LLCNDLKPMP KFPSLEIPTW MSDEEFGDFL
     FIMQFFSTFK EILPLKEIRG NDEIQFSDIV LAVKCNDPQN SPFADLMRVL LSIRTDIADE
     EDGDEADFSN RDEIYLINAQ NCDPANVVYG ESIREISDLH FKIRKIHGKS VRHLPVDWMT
     LTEVLRLIFE TSGYYTGIST HRHRLYARGN YRGYEDPAFE FRHAHPQIME KLRTQTVFDL
     EPSERLEIMK TLIYQLLTYS KFRIHLEKHQ MELTELRKEQ KRLKTWDAGQ EADSNAARLL
     MEYDSQSGGG GGGGVKDVEK EALVKRFKTY LKALNEGRRY DKEDLDTILL DAVPYTSLTL
     DEIVTARDLQ KAEFKTLMQS ITSKLFSTYC KVSDIRLGSD RAYRRYIVID KLSAILVENP
     TSSELRIECD EPSVLEVSED SESHDVFRCT GHLESCEVHG ATRDSKTRWS YIKNREQFDE
     FVGSLNSRGL REHEMLEELQ EYRLNLLELL EDTEDALGDA TWQENLMTEE TDPADSYNID
     WDAEIRDLLL DFEEKLDQGQ MGSIEKKFKI SRPAWREKLK ENGDVSGVLT ENLKIFDEDV
     VEMDDVIGMS DSRKLAIAFF MIIRSIQLKF IKPPFISPNR DEHGNLKPSE LFIRWQRALL
     QTDSHSALSL FISTFEGAIK WDKSRLQGKC KSCRRKAVAH ELILCSECDN CYHLKCAKLA
     EPEDDWMCTT CRAQHRKTEN EAKRMAREEL NNISINETDL SSSESQETPS TSSEQQPTTS
     MIKTASGRSV KKVHYSEVHE GLSLKSRKSN GMVAAAATPT TPSERPHRNV TMRNSEYHVI
     SNSPLTKPYQ KAIYGRRLIS ERLRDSNEMS VEQVFENLMS IATDKTHCYP DAQLQSHTQN
     TDEYHQSLSA IFIKYPERTR DYDTDNENNH SDDDEGTSDA SDGENTRKRK IPAAAAVAKS
     KSLVDSPRVI IPTTKEKMSS IESLLKEAMR QECSWPFLQP VDPKEVPDYY DVIERPMDLR
     TMMNKIKQRV YNKPAEVREE MIRVDFEQIL TNCETYNETE SEIYQLSREL QDFVTARLDA
     IIGQ
//
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