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Database: UniProt
Entry: A0A165LBH2_EXIGL
LinkDB: A0A165LBH2_EXIGL
Original site: A0A165LBH2_EXIGL 
ID   A0A165LBH2_EXIGL        Unreviewed;       428 AA.
AC   A0A165LBH2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Tudor/PWWP/MBT {ECO:0000313|EMBL:KZV97640.1};
GN   ORFNames=EXIGLDRAFT_832759 {ECO:0000313|EMBL:KZV97640.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV97640.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV97640.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV97640.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV425928; KZV97640.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165LBH2; -.
DR   STRING; 1314781.A0A165LBH2; -.
DR   InParanoid; A0A165LBH2; -.
DR   OrthoDB; 4271850at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   CDD; cd05840; PWWP_ScIOC4-like; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   InterPro; IPR035503; IOC4-like_PWWP.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   PANTHER; PTHR12550; HEPATOMA-DERIVED GROWTH FACTOR-RELATED; 1.
DR   PANTHER; PTHR12550:SF49; JIL-1 ANCHORING AND STABILIZING PROTEIN, ISOFORM A; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          110..173
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   REGION          69..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  47098 MW;  B11DCAACE3B519A5 CRC64;
     MLLTLFSMAP GTHHVAKPYF ARSSNALSLG RTRSEGKVGV RRRLKRRRQA TVGLCRELSC
     LISSRSSSRR AIQHPAHSEH PPPPKHPAPT PTRMSAASTP VKAGAHEFAV RDVVLAKLKG
     YPQWPAMVVD PDNVPSGVQD ERPSGKRHFC VRFFPAGDYA WLSPRDISPL SRSEIDKFLA
     VPKGAKRAGE LLKGYKVAMD PTKWESEIEQ EIAARAARGG ADDDEDVEEE DEPMDGEKTK
     KRRRSSVGGS KKDEVAGKKK RRTSSGKKNG LSAETVESEE DEKPAVAAPA VERKKEREKE
     EDEKFAHLKN DIGASHIKTV RHQLQKTFLS KGTPTEKDLE ASDALFKELE TTDIPVDYLG
     YSKIGKVMRH IASLDDSAIP REAEYGFKRR AGDLVSKWHK VANSSSLPPA PTPVAPIGNG
     NGLQAMVQ
//
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