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HELI_VZVO
ID   HELI_VZVO               Reviewed;         881 AA.
AC   Q9J3N5; Q4JQS0; Q4JR29;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, 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=ORF55;
OS   Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=341980;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=10720545; DOI=10.1086/315335;
RA   Argaw T., Cohen J.I., Klutch M., Lekstrom K., Yoshikawa T., Asano Y.,
RA   Krause P.R.;
RT   "Nucleotide sequences that distinguish Oka vaccine from parental Oka and
RT   other varicella-zoster virus isolates.";
RL   J. Infect. Dis. 181:1153-1157(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC   Oka varicella vaccine Varivax (V-Oka-Merk);
RX   PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA   Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA   Vassilev V.;
RT   "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL   J. Virol. 82:11023-11044(2008).
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; AF206304; AAF61656.1; -; Genomic_DNA.
DR   EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ008354; AAY57664.1; -; Genomic_DNA.
DR   EMBL; DQ008355; AAY57735.1; -; Genomic_DNA.
DR   IntAct; Q9J3N5; 4.
DR   MINT; Q9J3N5; -.
DR   ChEMBL; CHEMBL4523677; -.
DR   PRIDE; Q9J3N5; -.
DR   Proteomes; UP000002603; Genome.
DR   Proteomes; UP000008504; Genome.
DR   Proteomes; UP000008505; Genome.
DR   Proteomes; UP000008506; 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.
FT   CHAIN           1..881
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000385138"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
FT   VARIANT         492
FT                   /note="T -> S"
SQ   SEQUENCE   881 AA;  98893 MW;  5D3290EDB2E489F6 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 NTLVVVTTRL RKLVIGFSGT FQSFAKVLRD DSFVKARGET SIEYAYRFLS
     NLIFGGLINF YNFLLNKNLH PDKVSLAYKR LAALTLELLS GTNKTPLHEA 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
 
 
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