ID   DNBI_ELHVK              Reviewed;        1143 AA.
AC   Q18LF9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   23-FEB-2022, entry version 44.
DE   RecName: Full=Major DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04007};
GN   Name=DBP {ECO:0000255|HAMAP-Rule:MF_04007};
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
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; AF322977; ABG36560.1; -; Genomic_DNA.
DR   SMR; Q18LF9; -.
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.
FT   CHAIN           1..1143
FT                   /note="Major DNA-binding protein"
FT                   /id="PRO_0000408151"
FT   REGION          1140..1143
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04007"
SQ   SEQUENCE   1143 AA;  130078 MW;  2E75DE55CF150E70 CRC64;
     MSSDDNNIAS SASSGHGAWI YITEKTPDVL DILNRLVLTS ADSDVTIAPL LYDVTVEPGF
     ELTVKCPLML TDNNVILKLS NFMPCVFIIN STSSEDFRFC EDVVGNVSEI CEGAASRYGY
     TADFTEFNER TETTDSDVCS NVNVPESDYF VYIACTYGYK ELLFKGYLIP HWQDLRDISI
     GNRRGYKIPL LSPFLFTQCK DDTVQLTDQF ILDNGFYNPD LTKTLYSYIF RPLAVSLRYL
     DVTHLISVTL NQYITDTHAT AKLCDKKVYT CHGNNKLSTG DRDVLALCDI LANEVTVSYL
     TPFLDSAYDA PSTLDFYSWP IVKDKTHAEI LENLDQFLLH MSVHIGTLIF SGNSVLYQNK
     ISKVGGQSDG SNGQSVEGLL KSIYHTTGIQ LLYEDGYDDT RSLVRQHTAK PKNLKFNMDH
     LSFGASFSSH VLTKIVWFLN RSEEYKTTQS VSSTCYLVIN SSTGTCTACD GKHCNTCIGA
     LMCRMATRFP NINRQQKKEP CVTTLLTRMF ADMTILGSFG KKYNTERDTQ QKDGRVSAEP
     LDKAKYVLNI LDYCKRECLI DSDGNDTLKI SSKQEFIKII TGLNRTIDDE LIKLLSDMRK
     HSNAKDDLNN STMSFTLDLN PHAYAFSPLL QFVYMKTLVN ILESLAIVVI AEKISSYPMT
     QSAYSRWVKQ HFQSVYSEFK KSIYKKGFLT LSDYKMKNTT TNDTFTDFSH LKRDYKIDNT
     VRSSIATVNY QCRLWNFHVS SLRDFRIKYK PIPKNKDSPY FQKADKGIQN PVCGPLSFLI
     TRFHKDIFPN VNVSPMTLWQ RIYSNTLKNF NVDLGDKHDV ETFIKFMFEQ TVEYEGSNSI
     DVRPETILQY IEFRFVNRLL HASGHRGQYI GIVQALCTTL SDTKVDGLPC YLDSSRTFGT
     VSEYHAYCRE YNGTVKVGRT RPYCNTNGMF ERRPLVTVPY ALEKYTGAAG NASIFQCGQL
     GYFSGTGIDR NLGMINRTSD YNFMRRKHIF CTPLTDVLFT KISRGAHVFD FDMLKQRIKQ
     LLDEHCGGFD IELAILSEIL KHVKEPNYND LLFITGYQEH IASSLFDKIK VLDELEISSY
     SIESLQEIFP EKEELNDTEA TGSGYDFSFI IPKATDVDEI TGLNIQEFTN IEDETPLVKR
     MRL