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DNBI_HHV6U
ID   DNBI_HHV6U              Reviewed;        1132 AA.
AC   P52338;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   23-FEB-2022, entry version 74.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=U41;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
CC   -!- FUNCTION: Single-stranded DNA-binding protein required for DNA
CC       replication.
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; X92436; CAA63167.1; -; Genomic_DNA.
DR   EMBL; X83413; CAA58375.1; -; Genomic_DNA.
DR   RefSeq; NP_042934.1; NC_001664.2.
DR   SMR; P52338; -.
DR   PRIDE; P52338; -.
DR   GeneID; 1487919; -.
DR   KEGG; vg:1487919; -.
DR   Proteomes; UP000009295; 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; -; 1.
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..1132
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000115752"
FT   REGION          1112..1132
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1132 AA;  127763 MW;  4468D3E5559F02D8 CRC64;
     MADENETVVS APVSTAAWIY VFPKDKELLD VLSVLSLMER NSPIVISPLL MNLTVENDFS
     TTVKTPITNF GGTILTKITS FMPVCFFFHG TEQLVGMAED HGDLIRLCEQ TRQKFHLQSF
     EVPTARKVID IKALCSAVGK DADSVICHVA CGNGFKELLF AGLLIPCVEE QIQVQVGEYS
     CVKIPLYSAT LFETEETISL SSCTEFIQER GFFLPALSET LFYYVFTSWG TTLRFSNTKE
     LIDAGLKQFT QDGEQTVKLA PHKTYLGISG QKISAVEKDF LMLVDSVVTE LSFSHVAEYL
     DSVYDPSQIM NFNDWPIIRN SETHAERMAQ LTNLKLHLSS HLAVLIFAPN SILYCSKLAF
     IPNVKQAFNS VMTQELLLRS LSFCNALSSL SDDVYNDNRK IIKCDSTSGK DDKFSANHLA
     YACATSPQLL SFVVWNLNRM SVYNAGNAHT EIYNHLVNCS ANLCEFCDGK CCQSCIGTAM
     VRVGTRLPAI PKNVKKEPLV MSMFSRYYAE VDILGSFGRK PVSELKEIGK DQQNTLSLDR
     GKFVSQIFDY CKKNSLIDPV TGEDTFNVRS KKDFVSIIHG LTQCIEECVS RCIVEMRRTQ
     TPREQIENCL QSFNVDTTPY ATAFSPFLTF SYYKVILTVL QNLALIVASG HVVDRPCTGN
     SISKWLVQQY QSLYGTFHSS YLKKGFLNTR TVKVASNVDM EQILDCDLYK SGKYVKTTIQ
     AKLCRLSMQC LRDFRIKNRP FNKSSKTAHN NPYFKKNVKH KKNPLSGCIS FLLFKYHDKL
     FPNVKISCLE LWQRFLLNNV PKTLDIGNPE EVKTFIKFAF SITNTYDEID IIDIQPECLS
     TFIDCYFHNK FLSALGFHDY LTSLHGLTSK LVTQNPVLFP VVLDKQPKFS SIQEYLVYVK
     KLVLDGVPNP VIASLSKEPN FGTIFTSRSL VTFGLTLEKF VSLANREYFQ FGQLGWIGGS
     GVDRNLNPTS SALQDFRFMR QKTIIATKFS EVIVKKVRRE AIMFDTEVVK GKVLSIVENL
     TNDIDPELLI IAEVMRDRED KPTMDDMLFF VDGREALAAS IMLKLNHLVD MNVKDFSITN
     LQSVFETVSS NDAPVYDFSE ILAEEDDQGN GVLKCDETET ETDEPMTKKN RL
 
 
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