HELI_HHV7J
ID HELI_HHV7J Reviewed; 820 AA.
AC P52357;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DNA replication helicase {ECO:0000255|HAMAP-Rule:MF_04030};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04030};
GN Name=HELI {ECO:0000255|HAMAP-Rule:MF_04030}; OrderedLocusNames=U77;
OS Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=57278;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA Nicholas J.;
RT "Determination and analysis of the complete nucleotide sequence of human
RT herpesvirus.";
RL J. Virol. 70:5975-5989(1996).
CC -!- FUNCTION: Component of the helicase/primase complex. Unwinds the DNA at
CC the replication forks and generates single-stranded DNA for both
CC leading and lagging strand synthesis. The primase synthesizes short RNA
CC primers on the lagging strand that the polymerase elongates using
CC dNTPs. Possesses helicase-like motifs and therefore may act as the
CC helicase subunit of the complex. {ECO:0000255|HAMAP-Rule:MF_04030}.
CC -!- SUBUNIT: Associates with the primase and the primase-associated factor
CC to form the helicase-primase complex. {ECO:0000255|HAMAP-
CC Rule:MF_04030}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04030}.
CC -!- SIMILARITY: Belongs to the herpesviridae helicase family.
CC {ECO:0000255|HAMAP-Rule:MF_04030}.
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DR EMBL; U43400; AAC54738.1; -; Genomic_DNA.
DR PIR; T41978; T41978.
DR Proteomes; UP000009246; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04030; HSV_HELI; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003840; DNA_helicase.
DR InterPro; IPR034711; HSV_HELI.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02689; Herpes_Helicase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; Helicase; Host nucleus; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..820
FT /note="DNA replication helicase"
FT /id="PRO_0000115851"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ SEQUENCE 820 AA; 92914 MW; FC2E3CFC88B224D3 CRC64;
MSLSSLFNGK YDTKFLLNMS SAAKVELIVE KVAALADACL ETPLPTDWFR NILDPELEFN
SNFEEIHSIG DEEFAQPLPF LPFRVLLITG TAGAGKTSSI QTLAANSDCL ITATTSIAAQ
NLSGLLNRTK SAQVKTIFKT FGFNSSHVSM NERISCSVTT LDSIADQQKH DLSTYWNVIA
DIAERALNAA NGKTKVIPDL CESSVIVIDE AGVILRHILH TVVFFYWFYN GLHKTQLYKN
RVIPCIVCVG SPTQSGALIS SFNPLTQNKD VKKGFDILSA LICDDILSNY CKISENWVIF
VNNKRCTDVE FGEFLKHIEF GLPLKPELIE YVDRFVRPAT YIRNPTNEIG MTRLFLSHYE
VKSYFKVLHE QVELTNKDNL FTFPVYFIIQ NKAFEDYKNE ISNFTLEIEP WFKTNLHRLN
TYSQFADQDL SKTIQIEEIV LDDGSVEETL ITCHLKHIKH SSIGVTSRTK SSTVGFSGTY
EKFVELLQSD LFIEKTACEY SVHAYSFLTG LMYGGMYSFC LSEFTTSEVM TEIRKIKLPN
IDFLQTMTAE VSLQTFDESD EYYDLHIAPT DEEMLASDPC PDPFFLKYKQ LPLTNVLTFE
EISYLYTVFK EIFISRFAIL QRHSKEMFGK SNLITYNRNN VSSKRCGEIC SHVKSFYGML
TYAVPANNYT LEGYTYDNVI FLGTDKMLPP IIYKRGLPKI VIKDEMGFIS ILDNNVSKLT
DTVNGNSFHI CTTIDYAIVS KVAMTVTKSQ GLSIQRVALD FGNDPKNLKL SSIYVGMSRV
VDPNNLIMNL NPLRLNYEND NIIASHIVKA LKNKDTMLIF