BRLF1_EHV2
ID BRLF1_EHV2 Reviewed; 682 AA.
AC Q66652;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 02-JUN-2021, entry version 56.
DE RecName: Full=Putative transcription activator BRLF1 homolog;
GN Name=50;
OS Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX NCBI_TaxID=82831;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT "The DNA sequence of equine herpesvirus 2.";
RL J. Mol. Biol. 249:520-528(1995).
RN [2]
RP SEQUENCE REVISION.
RA Davison A.J.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae TAF50 family. {ECO:0000305}.
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DR EMBL; U20824; AAC13838.2; -; Genomic_DNA.
DR PIR; S55645; S55645.
DR RefSeq; NP_042647.2; NC_001650.2.
DR PRIDE; Q66652; -.
DR GeneID; 1461040; -.
DR KEGG; vg:1461040; -.
DR Proteomes; UP000007083; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR004998; Herpes_TAF50.
DR Pfam; PF03326; Herpes_TAF50; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Early protein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..682
FT /note="Putative transcription activator BRLF1 homolog"
FT /id="PRO_0000406052"
FT REGION 396..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 76570 MW; 0DE309BE785D532E CRC64;
MEPKDFQPEI KPPKPFCIEQ FVGCSKEFKE KTLRLITLYH ECLINARGGD DFMRYMYDVC
LSLEQEMRQY NALAGFLLEC NLFNLWNLFR NYKNKQSAES ANTNPCALMA QQFLKFHTER
LLVCTDRFFS TGCCSQINMP YDLCQHVFKF QQDLRKRCIA SWKTLSGGRR AFMTVVQDIF
TCFTTLRANE LITPRQQAFF KLSYPPCRVQ NVINILNVVH TQGIKDLKSL NMQKIKKRTP
HAGIFSASGQ PLFPIPEALL VDFNGEGIIR SDIADVSPFL QNPEEFLATD FFTYIKRFQG
VGVQIRDPEP RYQPASQQPQ QALRPQQQVL QQATAYPASV QAGGFAIQTE SPMEGTSAQY
FLAAQQHGVV GLFPSTATLV PIAGSTGVTE VVSYGHNSTS PVSTFSAPST SVTEADHQTQ
PRRSRKATAK RKHQQVQDGN EDEGPQRHPQ AHSRQFFQGA ASHQTAQPAQ VLQQSVIHGT
QGALYFMGPA QQIPGDHSQI PVISNAMLQS VLQQQGGSGA AIYDLSQLQP CVVPVQQQAA
QEVAVPTAVI HYQPAMQPQP QPYQQQQFLQ PQQQAQTPSP QMQQRQLTPQ SSPEPADEEE
EGPLNLTTRT EDHEILEEIL SNLYPEERRQ QEQQHQQGEE AAPASPSQHE EQAGPSNQSG
ETSQELDIFS LHNLHLRKSL FE