ID   HELI_HHV2H              Reviewed;         881 AA.
AC   P28277; P89428;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 81.
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=UL5;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA   Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT   "The genome sequence of herpes simplex virus type 2.";
RL   J. Virol. 72:2010-2021(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-881.
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(1991).
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; Z86099; CAB06765.1; -; Genomic_DNA.
DR   EMBL; D10470; BAA01267.1; -; Genomic_DNA.
DR   PIR; PQ0332; WMBEHQ.
DR   RefSeq; YP_009137156.1; NC_001798.2.
DR   ChEMBL; CHEMBL4630722; -.
DR   PRIDE; P28277; -.
DR   DNASU; 1487338; -.
DR   GeneID; 1487338; -.
DR   KEGG; vg:1487338; -.
DR   Proteomes; UP000001874; 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; IPR003840; DNA_helicase.
DR   InterPro; IPR034711; HSV_HELI.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02689; Herpes_Helicase; 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..881
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000115846"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ   SEQUENCE   881 AA;  98884 MW;  03DC2AFF9ACD85D5 CRC64;
     MAASGGEGSR DVRAPGPPPQ QPGARPAVRF RDEAFLNFTS MHGVQPIIAR IRELSQQQLD
     VTQVPRLQWF RDVAALEVPT GLPLREFPFA AYLITGNAGS GKSTCVQTLN EVLDCVVTGA
     TRIAAQNMYV KLSGAFLSRP INTIFHEFGF RGNHVQAQLG QHPYTLASSP ASLEDLQRRD
     LTYYWEVILD ITKRALAAHG GEDARNEFHA LTALEQTLGL GQGALTRLAS VTHGALPAFT
     RSNIIVIDEA GLLGRHLLTT VVYCWWMINA LYHTPQYAGR LRPVLVCVGS PTQTASLEST
     FEHQKLRCSV RQSENVLTYL ICNRTLREYT RLSHSWAIFI NNKRCVEHEF GNLMKVLEYG
     LPITEEHMQF VDRFVVPESY ITNPANLPGW TRLFSSHKEV SAYMAKLHAY LKVTREGEFV
     VFTLPVLTFV SVKEFDEYRR LTQQPTLTME KWITANASRI TNYSQSQDQD AGHVRCEVHS
     KQQLVVARND ITYVLNSQVA VTARLRKMVF GFDGTFRTFE AVLRDDSFVK TQGETSVEFA
     YRFLSRLMFG GLIHFYNFLQ RPGLDATQRT LAYGRLGELT AELLSLRRDA AGASATRAAD
     TSDRSPGERA FNFKHLGPRD GGPDDFPDDD LDVIFAGLDE QQLDVFYCHY ALEEPETTAA
     VHAQFGLLKR AFLGRYLILR ELFGEVFESA PFSTYVDNVI FRGCELLTGS PRGGLMSVAL
     QTDNYTLMGY TYTRVFAFAE ELRRRHATAG VAEFLEESPL PYIVLRDQHG FMSVVNTNIS
     EFVESIDSTE LAMAINADYG ISSKLAMTIT RSQGLSLDKV AICFTPGNLR LNSAYVAMSR
     TTSSEFLHMN LNPLRERHER DDVISEHILS ALRDPNVVIV Y