HELI_VZVD
ID HELI_VZVD Reviewed; 881 AA.
AC P09303;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=ORF55;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27938.1; -; Genomic_DNA.
DR PIR; C27215; WZBE55.
DR PRIDE; P09303; -.
DR Proteomes; UP000002602; 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_0000115852"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ SEQUENCE 881 AA; 98849 MW; 17763B9CDC7332D8 CRC64;
MKRSISVDSS SPKNVFNPET PNGFDDSVYL NFTSMHSIQP ILSRIRELAA ITIPKERVPR
LCWFKQLLEL QAPPEMQRNE LPFSVYLISG NAGSGKSTCI QTLNEAIDCI ITGSTRVAAQ
NVHAKLSTAY ASRPINTIFH EFGFRGNHIQ AQLGRYAYNW TTTPPSIEDL QKRDIVYYWE
VLIDITKRVF QMGDDGRGGT STFKTLWAIE RLLNKPTGSM SGTAFIACGS LPAFTRSNVI
VIDEAGLLGR HILTAVVYCW WLLNAIYQSP QYINGRKPVI VCVGSPTQTD SLESHFQHDM
QRSHVTPSEN ILTYIICNQT LRQYTNISHN WAIFINNKRC QEDDFGNLLK TLEYGLPITE
AHARLVDTFV VPASYINNPA NLPGWTRLYS SHKEVSAYMS KLHAHLKLSK NDHFSVFALP
TYTFIRLTAF DEYRKLTGQP GLSVEHWIRA NSGRLHNYSQ SRDHDMGTVK YETHSNRDLI
VARTDITYVL NSLVVVTTRL RKLVIGFSGT FQSFAKVLRD DSFVKARGET SIEYAYRFLS
NLIFGGLINF YNFLLNKNLH PDKVSLAYKR LAALTLELLS GTNKAPLHEA AVNGAGAGID
CDGAATSADK AFCFTKAPES KVTASIPEDP DDVIFTALND EVIDLVYCQY EFSYPKSSNE
VHAQFLLMKA IYDGRYAILA ELFESSFTTA PFSAYVDNVN FNGSELLIGN VRGGLLSLAL
QTDTYTLLGY TFAPVPVFVE ELTRKKLYRE TTEMLYALHV PLMVLQDQHG FVSIVNANVC
EFTESIEDAE LAMATTVDYG LSSKLAMTIA RSQGLSLEKV AICFTADKLR LNSVYVAMSR
TVSSRFLKMN LNPLRERYEK SAEISDHILA ALRDPNVHVV Y