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Database: UniProt
Entry: A0A165SXS5_9APHY
LinkDB: A0A165SXS5_9APHY
Original site: A0A165SXS5_9APHY 
ID   A0A165SXS5_9APHY        Unreviewed;       144 AA.
AC   A0A165SXS5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Histone-fold-containing protein {ECO:0000313|EMBL:KZT72641.1};
GN   ORFNames=DAEQUDRAFT_743660 {ECO:0000313|EMBL:KZT72641.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72641.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT72641.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT72641.1,
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).
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DR   EMBL; KV429040; KZT72641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165SXS5; -.
DR   STRING; 1314783.A0A165SXS5; -.
DR   OrthoDB; 297906at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0017054; C:negative cofactor 2 complex; IEA:InterPro.
DR   GO; GO:0140223; F:general transcription initiation factor activity; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR042225; Ncb2.
DR   PANTHER; PTHR46138; PROTEIN DR1; 1.
DR   PANTHER; PTHR46138:SF1; PROTEIN DR1; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   4: Predicted;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          17..81
FT                   /note="Transcription factor CBF/NF-Y/archaeal histone"
FT                   /evidence="ECO:0000259|Pfam:PF00808"
SQ   SEQUENCE   144 AA;  16170 MW;  5E50539B550C8D5B CRC64;
     MSDRETGGLP VSDEDLSLPK ATVAKMITEL LPPEVSCAKE TRDLVIECCV EFIHLISSEA
     NEICEKESKK TIAPEHIISA LKHLGFETFT AEVEDVLKDH KQQQKDREKK VSKLESSGLT
     EEELLRQQEE LFAASRAKFQ SAQQ
//
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