ID   S7Q425_MYOBR            Unreviewed;       176 AA.
AC   S7Q425;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Protein Dr1 {ECO:0000256|ARBA:ARBA00018742};
DE   AltName: Full=Down-regulator of transcription 1 {ECO:0000256|ARBA:ARBA00032651};
DE   AltName: Full=Negative cofactor 2-beta {ECO:0000256|ARBA:ARBA00030451};
GN   ORFNames=D623_10016256 {ECO:0000313|EMBL:EPQ15622.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ15622.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
CC   -!- SIMILARITY: Belongs to the NC2 beta/DR1 family.
CC       {ECO:0000256|ARBA:ARBA00009245}.
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DR   EMBL; KE164164; EPQ15622.1; -; Genomic_DNA.
DR   RefSeq; XP_005879046.1; XM_005878984.2.
DR   AlphaFoldDB; S7Q425; -.
DR   SMR; S7Q425; -.
DR   GeneID; 102241180; -.
DR   KEGG; myb:102241180; -.
DR   CTD; 1810; -.
DR   eggNOG; KOG0871; Eukaryota.
DR   OrthoDB; 297906at2759; -.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0017054; C:negative cofactor 2 complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   PRINTS; PR00615; CCAATSUBUNTA.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT   DOMAIN          12..75
FT                   /note="Transcription factor CBF/NF-Y/archaeal histone"
FT                   /evidence="ECO:0000259|Pfam:PF00808"
FT   REGION          152..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   176 AA;  19444 MW;  36E7E59F2FD6CAB5 CRC64;
     MASSSGNDDD LTIPRAAINK MIKETLPNVR VANDARELVV NCCTEFIHLI SSEANEICNK
     SEKKTISPEH VIQALESLGF GSYISEVKEV LQECKTVALK RRKASSRLEN LGIPEEELLR
     QQQELFAKAR QQQAELAQQE WLQMQQAAQQ AQLAAASASA SNQAGSSQDE EDDDDI
//