HELI_ALHV1
ID HELI_ALHV1 Reviewed; 783 AA.
AC O36393;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=44;
OS Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX NCBI_TaxID=654901;
OH NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA Ensser A., Pflanz R., Fleckenstein B.;
RT "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL J. Virol. 71:6517-6525(1997).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF005370; AAC58090.1; -; Genomic_DNA.
DR PIR; T03138; T03138.
DR RefSeq; NP_065542.1; NC_002531.1.
DR GeneID; 911763; -.
DR KEGG; vg:911763; -.
DR Proteomes; UP000000941; 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..783
FT /note="DNA replication helicase"
FT /id="PRO_0000405739"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ SEQUENCE 783 AA; 87663 MW; F6C081D087D96169 CRC64;
MEHIPKSFIL NMTSEAKVRM IVQKIKALSE ETTSDSPDIS WFDAEFDPDD LGPRLPFSTY
CITGTAGAGK STSIAALHQN LNCLITGATV VAAQNLSKTL HSFCPTIYTA FGFKSRHINL
LNRKPQIKLC GDSDITAVQY YELSKYWPVI KDIIGEFCKK KKFGLYASMS EEAYRVFGCL
GSPQLWTTNI IIIDEAGTLS SHVLMAVVFL WWFFNGWLNT RQYLNGKIPC IVCVGSPTQT
DAYHSQFDHS KQQQHVRECD NVLSLIIGNK TVSDYVKISE NWALFINNKR CTDPEFGHML
KVLEYGLEIS DDVMEYINRL VVPRSKIMDP MQYVGWTRLF LSHSEVKQYL GSLHSALSSN
QSSTTCTLFT CPIVCEVFHD AVEEYKEAVN VPSLTPLEWL ARNTYRLSNY SQFIDQDMTT
VSTDVGEAST KVTYATKFVK GSYVSVNGKT KKCFMGFMGT YAQFKRVLDS ESFLDTHGHE
QPEHAYAFLC QLLYNSMYNF YQAAVQSDCA SYISALNNIP IPEVLCAPAH SELACSEPLN
EGEDLFYHKT LPPPTARSTS LANIIAIYQG LKDIFIARME AATRYQMPNF GYSSFNTFLS
NTIVKNNVDF VSAEPISGLL DYASTVESYM LQGYTFSPIY FGKLPLQSTL SKDLRDKLPN
LVVRDADGFI CCLDNNLTKM TENLESGAQI HMCSVGDYGI SSKLAMTIAK AQGLSLDKVA
VCFGNHQKIK RSHVYVALSR ATDANNLVID SNPLSNRECE MDICKSSKHI VAALCNPQTL
LIY