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Database: UniProt
Entry: A0A165L1J2_9APHY
LinkDB: A0A165L1J2_9APHY
Original site: A0A165L1J2_9APHY 
ID   A0A165L1J2_9APHY        Unreviewed;       484 AA.
AC   A0A165L1J2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   SubName: Full=DUF926-domain-containing protein {ECO:0000313|EMBL:KZT63874.1};
GN   ORFNames=DAEQUDRAFT_699611 {ECO:0000313|EMBL:KZT63874.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT63874.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT63874.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT63874.1,
RC   ECO:0000313|Proteomes:UP000076727};
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).
CC   -!- SIMILARITY: Belongs to the NKAP family.
CC       {ECO:0000256|ARBA:ARBA00009313}.
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DR   EMBL; KV429152; KZT63874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165L1J2; -.
DR   STRING; 1314783.A0A165L1J2; -.
DR   OrthoDB; 2883730at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   InterPro; IPR040466; NKAP.
DR   InterPro; IPR009269; NKAP_C.
DR   PANTHER; PTHR13087; NF-KAPPA B ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR13087:SF0; NKAP_C DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF06047; Nkap_C; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          372..473
FT                   /note="NF-kappa-B-activating protein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06047"
FT   REGION          1..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  56585 MW;  533124276A3182AE CRC64;
     MATVHPSRMA LVPQDPPKDV YSQSRDRRRS PSPRPSRRRS PSPPRERDKD VDRYGRREPA
     RNRDERRERE GEPSKRNRAR ADDYFDEAGG GGQEPRKRSR SRSADRERDH EREERRERER
     PRRRSPEYGE YRRLSPPRES APAPWRQQEN MYPRGREVGR FAGGGNDFME SRRQQRENST
     FSIWPPSPKA PTRDLSGERD SKHRKKSHKR RYDSDSDTDT DSEEERRRKR KERKKSRKEK
     KDKERDRERE RSRERRKHRS RSRRYSDEED SEDERELRRR KDHRRSATRT RSPEQGPPTT
     EAEDEWVEKS GSTGLLAPAQ SSASSPKPSS IQPPATNSLQ QPTAAEDDDE DDEVGPKLPQ
     TAKSSRSKVD ERQYGGALLR GEGSAMAAFL KDGTDVRIPR RGEIGLQSDE IASFESVGYV
     MSGSRHRRMN AVRMRKENQV ISAEEKRGIL KLQQEERERR EAILREEFQQ LVSDKLKSQG
     GPAK
//
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