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HELI_HHV8P
ID   HELI_HHV8P              Reviewed;         788 AA.
AC   Q2HR89; D0UZQ6;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 54.
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=ORF44;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
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; AF148805; ABD28894.1; -; Genomic_DNA.
DR   RefSeq; YP_001129396.1; NC_009333.1.
DR   PRIDE; Q2HR89; -.
DR   DNASU; 4961457; -.
DR   GeneID; 4961457; -.
DR   KEGG; vg:4961457; -.
DR   Proteomes; UP000000942; 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; IDA:UniProtKB.
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..788
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000423803"
FT   BINDING         73..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ   SEQUENCE   788 AA;  88237 MW;  6584683373CEF404 CRC64;
     MDSSEGCTDM DEPSPGFILN MTSDAKVRSV VEQIDRLSNI TTSPPEMGWY DLEFDPLEDE
     GPFLPFSAYV ITGTAGAGKS TSVSALHQNL NCLITGATVV AAQNLSRALK SYCPTIYHAF
     GFKSRHINIC QRKVPKVTQS SIEQLQRYEL ARYWPTVTDI IREFMRKKQK GQYSSLSQSA
     FRLLCRMGGA NLWTSNIIVI DEAGTLSSHI LTAVVFFYWF YNSWLDTPLY RNGAVPCIVC
     VGSPTQTDAF QSVFNHTQQR NEISACDNVL TFLLGKREVA DYIRLDENWA LFINNKRCTD
     PQFGHLLKTL EYNLDISPEL MDYIDRFVVP KSKILDPLEY AGWTRLFISH QEVKSFLATL
     HTCLSSNKDA VSTKLFTCPV VCEVFTEPFE EYKRAVGLTH MTPIEWVTKN LFRLSNYSQF
     ADQDMAVVGT YITDASTQIT FATKFVKNSY ATLTGKTKKC ICGFHGSYQR FKSILDGELF
     IESHSHDNPA YVYSFLSTLL YNAMYSFYAH GVKQGHEEFL RDLRELPVSQ ELISEMSSED
     VLGQEGDTDA FYLTASLPPS PTHAALPTLV AYYSGAKELF CNRLALARRH FGDEFLHSDF
     STFTVNIVVR DGVDFVSTSP GLHGLVAYAS TIDTYIIQGY TFLPVRFGRP GGQRLSEDLR
     RKMPSIVVQD SSGFIACLEN NVTKMTETLE GGDVFNICCA GDYGISSNLA MTIVKAQGVS
     LSRVAISFGN HRNIRASLVY VGVSRAIDAR YLVMDSNPLK LMDRGDAQSP SSKYIIKALC
     NPKTTLIY
 
 
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