ID Q9DPS5_MEHV1 Unreviewed; 839 AA.
AC Q9DPS5;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Replication origin-binding protein {ECO:0000256|ARBA:ARBA00014069};
DE AltName: Full=OriBP {ECO:0000256|ARBA:ARBA00031715};
GN Name=HVT016 {ECO:0000313|EMBL:AAG45746.1};
OS Meleagrid herpesvirus 1 (MeHV-1) (Turkey herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC Mardivirus meleagridalpha1.
OX NCBI_TaxID=37108 {ECO:0000313|EMBL:AAG45746.1, ECO:0000313|Proteomes:UP000175168};
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1] {ECO:0000313|EMBL:AAG45746.1, ECO:0000313|Proteomes:UP000175168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FC126 {ECO:0000313|EMBL:AAG45746.1};
RX PubMed=11134310; DOI=10.1128/JVI.75.2.971-978.2001;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of turkey herpesvirus.";
RL J. Virol. 75:971-978(2001).
CC -!- FUNCTION: Functions as a docking protein to recruit essential
CC components of the viral replication machinery to viral DNA origins. In
CC the presence of the major DNA-binding protein, opens dsDNA leading to a
CC conformational change in the origin that facilitates DNA unwinding and
CC subsequent replication. {ECO:0000256|ARBA:ARBA00025279}.
CC -!- SIMILARITY: Belongs to the herpesviridae OriBP family.
CC {ECO:0000256|ARBA:ARBA00007195}.
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DR EMBL; AF291866; AAG45746.1; -; Genomic_DNA.
DR RefSeq; NP_073302.1; NC_002641.1.
DR GeneID; 918581; -.
DR KEGG; vg:918581; -.
DR OrthoDB; 680at10239; -.
DR Proteomes; UP000175168; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003450; Replication_origin-bd.
DR Pfam; PF02399; Herpes_ori_bp; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000175168}.
FT DOMAIN 45..210
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 839 AA; 94490 MW; F2F752CA1AF26ABA CRC64;
MIDYASSASL SRMLYGKDLI EWIAKNRPAI TVERQSDGPV AFPSPLCTGA RSTLVVRAPM
GSGKTTALLC WLRSLLCNSL TSVLIVSCRR SFTETLSGRL NNGGIAGFVT YLTAGDYIMK
GKQFYRLLVQ IESLHRIDHK LLHSYDIVIL DEIMSTIGQL FSPTMKHLRK VDSMLTSLLR
KCPQIVAMDA TINAQLVDML AFLRGEENIH VIIGEYASRG FSMRCCKILR SLGTDTLLNV
LNPTNSKGTP QIQNTSDLIR STSRSYLQQS TFFYELGRRL EGGLNVCIFS STISFSEIAA
RFCLAYTNAV LVLNSTRDEP VDMNLWSNYR VVIYTTVVTV GLSFNTTHFH SMMAYVKPTI
NGPDMVSVYQ SLGRIRSLRL NEVLIYMDAS GARSDPIFTP MLLNHVIDKN GGWATGFYQV
TNMLCRNFRR DCFPTFGLSE LLFLFPRFKY KHLFERCTLN NISDSLNIIH ALLESNLMQV
TFDGCDHGFD SDTFFSFLMA LRTDSLASQK DLKLVRGQAV CNIPLEVDIL DSDVVAVFVR
KYIKPTISFQ SLSTFLTKLS EPIARDQFIN ITMLDACRAT PAALYSEAVF RRIYDFYASG
SIPIIGSNGK LDTVSLTPDF NTSGRWDLYR LCCKWADSLH INPLEGNNCS IDPSLLLQLV
NTDYSTYARA VLEVARCYLL DAQTATKRPV ITTKNVLSGL NNKHCNQLSN IEHAVSLLKA
TWEILFGLRV VKSTSTFPGG KKVKNLRKAE IEALLDGVGI NRTLVKTHKD LYRLLMKNKV
AFQNPRYEIR RPKWYDLIRS RLDTELGIYH DIMELETVLA EVPASYWPAI DGAIDFHRL
//