ID   DNBI_ALHV1              Reviewed;        1127 AA.
AC   O36360;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   23-FEB-2022, entry version 72.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007}; Synonyms=6;
OS   Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX   NCBI_TaxID=654901;
OH   NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA   Ensser A., Pflanz R., Fleckenstein B.;
RT   "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL   J. Virol. 71:6517-6525(1997).
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; AF005370; AAC58057.1; -; Genomic_DNA.
DR   PIR; T03105; T03105.
DR   RefSeq; NP_065509.1; NC_002531.1.
DR   SMR; O36360; -.
DR   PRIDE; O36360; -.
DR   GeneID; 911793; -.
DR   KEGG; vg:911793; -.
DR   Proteomes; UP000000941; 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..1127
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000405753"
FT   REGION          1098..1127
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1127 AA;  126887 MW;  0A2F4CD774492D7B CRC64;
     MALKHQLNHA VEDNLGSKAP IGPCGFIYIY PETHFNFKEI SLLGDKYAEA GAFSLPLLHG
     VTVEEAFVPN VKAVYKKIDM TTVSVKLSTF YNRAIIFHNV EKFESIFSGP GLGSLCKEAC
     DLFGYVPFTP LGEGSTDVSD ICPPVWQEKD AIMAVVITEG FKERLHLGKL IYLKSQMHSV
     MINKTEVYRI PLYDEDLFTK KSSLRRLYLP AVSEYLYYTL YTSLAQSLRV HNAASLVEAI
     QEQFVHDKYK MAKLVSFKEY PLATVGACDT TLMVIDAVAA ELGLSYSLSF FEAPQEKTKV
     QDYYSWDIFA SCETDSDRLE ALSKWNALQA IHIHAQLFST NSIYYVNRVA RQAPIPNSKV
     EPNVYNSYYL QHGLANLCEE TLFEDGSPAF TGAPASSLDG SSFTLQHLAY AAAFSPNLLA
     RMCYYLQFCQ HQKSTLNPAY NITEYVGSAA NSPVCSLCSG QCPCVCINTL FYRLKDRFPP
     VLQGSRRDPY VITGITNVFN ELDFLGNFAS FRDKDEDQNQ TEETPRYTYW QLNQTLTEKL
     EAAGLVDSPV ADEGAGGSGS MNLEKFVRTF SDIDSLVDAE AAKFINTMIK NNVNFKESIK
     GVSHVIQYNC NTYWQAPCSL MLNLYYRSIL TIIQDIALPI STVYESENPA QGYKPNEWLK
     LHYQTLWTNF KSFFIDKGVI TGTEMKVVHA EQFSDFFDVD AATNNMYSPV KVQVRLARAQ
     VLALKNIKVK NRILFSGTSM SEHYQNAFLK TANRRDNYIL AGPYVKFLNS FHRQLFPNLK
     ISCLYLWSNF CKKKQIPCVP GVSAEALNKF FSYINNNSKQ FEEVNMLDVV PDSYVTYAKQ
     RLNNAILRAC GQTQFYAVTI HSIFPKVQET CALEYPHVLG TSSVDSVEDY VNNVQNLKAL
     TVNSSLRESA ANLARSRPIV TLPVVVNKYT GIAGNAQLFQ SANLGYFMGR GVDKNLLGDS
     LFVKKQQNSY MRKKYLFMTP LVGNLLKPSY THQGTAFEIE TVKRTIQSIL EDQADEDVLN
     RVVCELVKSL GAGCADLTLD DIQFYLGSYG MFSENILEKL DQLRELVGPW THEWAESVLK
     SGTCETDEVQ FVAFEEEQVK LTSMDHSGKV VGGKKRKIAT MFDDLDL