DNBI_PSHV1
ID DNBI_PSHV1 Reviewed; 1188 AA.
AC Q6UDK2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 58.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=UL29;
OS Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
CC -!- FUNCTION: Plays several crucial roles in viral infection. Participates
CC in the opening of the viral DNA origin to initiate replication by
CC interacting with the origin-binding protein. May disrupt loops,
CC hairpins and other secondary structures present on ssDNA to reduce and
CC eliminate pausing of viral DNA polymerase at specific sites during
CC elongation. Promotes viral DNA recombination by performing strand-
CC transfer, characterized by the ability to transfer a DNA strand from a
CC linear duplex to a complementary single-stranded DNA circle. Can also
CC catalyze the renaturation of complementary single strands.
CC Additionally, reorganizes the host cell nucleus, leading to the
CC formation of prereplicative sites and replication compartments. This
CC process is driven by the protein which can form double-helical
CC filaments in the absence of DNA. {ECO:0000255|HAMAP-Rule:MF_04007}.
CC -!- SUBUNIT: Homooligomers. Forms double-helical filaments necessary for
CC the formation of replication compartments within the host nucleus.
CC Interacts with the origin-binding protein. Interacts with the helicase
CC primase complex; this interaction stimulates primer synthesis activity
CC of the helicase-primase complex. Interacts with the DNA polymerase.
CC Interacts with the alkaline exonuclease; this interaction increases its
CC nuclease processivity. {ECO:0000255|HAMAP-Rule:MF_04007}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007}.
CC Note=In the absence of DNA replication, found in the nuclear framework-
CC associated structures (prereplicative sites). As viral DNA replication
CC proceeds, it migrates to globular intranuclear structures (replication
CC compartments). {ECO:0000255|HAMAP-Rule:MF_04007}.
CC -!- SIMILARITY: Belongs to the herpesviridae major DNA-binding protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04007}.
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DR EMBL; AY372243; AAQ73708.1; -; Genomic_DNA.
DR RefSeq; NP_944402.1; NC_005264.1.
DR SMR; Q6UDK2; -.
DR GeneID; 2656962; -.
DR KEGG; vg:2656962; -.
DR Proteomes; UP000006840; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.190.40; -; 2.
DR HAMAP; MF_04007; HSV_DNBI; 1.
DR InterPro; IPR035989; DBP_sf.
DR InterPro; IPR043031; Viral_ssDBP_head.
DR InterPro; IPR000635; Viral_ssDNA-bd.
DR Pfam; PF00747; Viral_DNA_bp; 1.
DR SUPFAM; SSF118208; SSF118208; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; Host nucleus; Reference proteome.
FT CHAIN 1..1188
FT /note="Major DNA-binding protein"
FT /id="PRO_0000406857"
FT REGION 1145..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1188
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT MOTIF 838..839
FT /note="Required for filament formation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
FT COMPBIAS 1149..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 127868 MW; 2C7EEE885DBCF30B CRC64;
MESGGVETTR QGKTESLQYA VGPMAYVYAR SNLTIDPEEW GLLCAKSSDQ PSTAVAPLIP
GLTVEEAFNT SIAAIIATKS SGMVGGAASA ILSPCHFSPS VYVFYGGERI NATSLAPGLT
ALCDEARTKF GFSSPPPGGP VSNAKETSGE TICAALDMDP ETTMLYLVVA EPFCEAVYMC
NTFLHFGGAD SVYINSEFVR RVPIYPVQMY MPDIALRLCR NPFDTNSRNI GEGCAYPKPL
YNKSLNRVLH GAVLAPQGQS LRTRDLEAVA RAATAVAFDG NFEGCVLAAD KTFTQPATPQ
AKSAAQKPQA DVERRAACSL AADLALTTRV SVSCAPYKFE GNASAPYCQW PMFCDAKTPD
ERAAALSKFM AELAGIVGAG FFAVNSPLYA SEVVDGGAAA DPGDKHASSN LTRFFFACGL
HTLGCPTVDY AGNRVSDGTG DCALASASGF EYGPEHLAYA CGFSPELTAR ALFYLERCSR
YQLGADCRGG ANTLKFVAAE TTMAAECRWC TETTRQYCVR HTLHRLRSRL PTPRAPRRGP
MAVFGAVDAE YTDCDQLGNF APYSHMKRAG EGDSARNVMN DTYRGLCGRV MQFLVSEGLV
RADTGEDARN IQSAKDLCDT YDRISNMVDE ECAKFIAALS GARGYHYKEH LASSAHTFAV
SLNPYSTSFC PMLSHLVTQT KSIILQDLIL SQVPSTFDKG QPETKMFRSA AMPTLRSAFM
GMLDKGFVSG RQEPVVVSAS SVTAPDTSVP STEKSVAQYE YSLTRGQVLK LKEFKVKNRI
VFNGFEGRRG GVRMQGMADS FSRPASVKHI NILGGPLGFL LKRYHEMIFG PENNVFQFWN
KVIGGTMPMS HLTPEIRKTL NYIRRVSKAY AESNYVKAQP QTILELANFM VTNKILEYCG
HGGTNGSFYI STPSAAVMSA TRNKDPSAEL AWLPAVANPT TKNLTEAAEK SIASEPEKNW
VSTSMVTNAC RLVMGTKPII GLGIMVSKYI GQQSSTTVFQ AGNWSGFMGA SGIQSVNAGL
SGDTTRKCML ACKRTGALIK AGPSSSFTES SLAGQVRSMV EAGCTPHAIY AVALRVLGEG
LRDVTTDTWV AIVEDRFLIE ALEELHAQIA ASTPNGWTHE AAMAELNKHG NEEVATDGEM
LNFDCDDDDA DKDAPHGAKS DVPNGDDEDV FAGPSAKKRT LATEILFC
