GenomeNet

Database: Pfam
Entry: HSV_VP16_C
LinkDB: HSV_VP16_C
Original site: HSV_VP16_C 
#=GF ID   HSV_VP16_C
#=GF AC   PF12149.6
#=GF DE   Herpes simplex virus virion protein 16 C terminal
#=GF AU   Mistry J, Gavin OL
#=GF SE   pdb_2k2u
#=GF GA   20.10 20.10;
#=GF TC   25.00 71.70;
#=GF NC   17.40 15.80;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 17690987 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Domain
#=GF RN   [1]
#=GF RM   18630911
#=GF RT   NMR structure of the complex between the Tfb1 subunit of TFIIH
#=GF RT   and the activation domain of VP16: structural similarities
#=GF RT   between VP16 and p53.
#=GF RA   Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski
#=GF RA   JG;
#=GF RL   J Am Chem Soc. 2008;130:10596-10604.
#=GF DR   INTERPRO; IPR021051;
#=GF CC   This domain is found in viruses, and is about 30 amino acids in
#=GF CC   length. It is found in association with Pfam:PF02232. This
#=GF CC   domain is the C terminal of the HSV virion protein 16. This
#=GF CC   protein is a transcription promoter. The C terminal domain is
#=GF CC   the carboxyl subdomain of the acidic transcriptional activation
#=GF CC   domain. The protein binds to DNA binding proteins to carry out
#=GF CC   its function. Such proteins include TATA binding protein, CBP,
#=GF CC   TBP-binding protein, etc.
#=GF SQ   2
#=GS VP16_HHV11/461-490  AC P06492.1
#=GS VP16_HHV11/461-490  DR PDB; 2PHG B; 465-490;
#=GS VP16_HHV11/461-490  DR PDB; 2PHE C; 465-490;
#=GS VP16_HHV2H/461-490  AC P68336.1
VP16_HHV11/461-490             DSAPYGALDMADFEFEQMFTDALGIDEYGG
#=GR VP16_HHV11/461-490  SS    XXXX-CCCTCCCCCHHCCHCCCCCTCCC--
VP16_HHV2H/461-490             DPVSYGALDVDDFEFEQMFTDAMGIDDFGG
#=GC SS_cons                   XXXX-CCCTCCCCCHHCCHCCCCCTCCC--
#=GC seq_cons                  DsssYGALDhsDFEFEQMFTDAhGID-aGG
//
DBGET integrated database retrieval system