DNBI_HHV6Z
ID DNBI_HHV6Z Reviewed; 1132 AA.
AC P52538;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 23-FEB-2022, entry version 78.
DE RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=KA2L, U41;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7983761; DOI=10.1128/jvi.69.1.589-596.1995;
RA Stamey F.R., Dominguez G., Black J.B., Dambaugh T.R., Pellett P.E.;
RT "Intragenomic linear amplification of human herpesvirus 6B oriLyt suggests
RT acquisition of oriLyt by transposition.";
RL J. Virol. 69:589-596(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
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; AF157706; AAB06339.1; -; Genomic_DNA.
DR PIR; T44001; T44001.
DR RefSeq; NP_050222.1; NC_000898.1.
DR SMR; P52538; -.
DR PRIDE; P52538; -.
DR GeneID; 1497043; -.
DR KEGG; vg:1497043; -.
DR Proteomes; UP000006930; 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_0000115753"
FT REGION 1109..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1132
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ SEQUENCE 1132 AA; 127818 MW; B39AB4E6A5103EFF CRC64;
MADENETVVS APVSTAAWIY VFPKEKELLD VLSVLSLMER NSPVVISPLL 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 TEDVYNDNRK IIKCDSTSGK DDKFSANHLA
YACATCPQLL SYVVWNLNRM SVYNAGNAYT EIYNHLVNCS ANLCEFCDGK CCQSCIGTAM
VRVGTRLPAI PKNVKKEPLV MSMFSRYYAE VDILGSFGRK PVSELKEIGK DQQNTLSLDR
GKFVSQIFDY CKKNSLIDPV TGEDTFNVRS KKDFVSIIHG LTQCIEECVS RCIVEMRRTQ
TPREQIENCL QSFNVDTTPY ATAFSPFLTF AYYKVILTVL 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 TIMFDTEVVK GKVLSIVENL
TNDIDPELLI IAEVMRDRED KPTMDDMLFF VDGREALAAS IMLKLNHLVD MNVRDFSIAN
LQSVFEAVSS NDAPVYDFSE ILAEEDDQAS GVLKCDETET ETDEPMTKKN RL
