HELI_EHV1V
ID HELI_EHV1V Reviewed; 881 AA.
AC Q6S6U7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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=57;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS45941.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45941.1; -; Genomic_DNA.
DR Proteomes; UP000008296; 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_0000115848"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ SEQUENCE 881 AA; 99481 MW; E7FC4279DC560875 CRC64;
MESADILPGS RGTVDRRCEG SEEKITPPRP VEDFNPQLFP NEVYLNFTSM HGIQPVVARI
RELSRKTVSA AMVPPLEWFE RLPRLETPLD IEPLHLPFSV YLISGNAGSG KSTCIQTLNE
TMDCVITGAT RVAAQNVYTK LSSAFATRHI NTIFQEFGFR GNHVQAQLGK YQYSCSSSPP
PIEELQKRDI VYYWEVLVDI TRRLFESTAS RGEFENIRAL ERLLGRAPGS LTRLAFCTNG
SLPAFTRTNI VIIDEAGLLG RHLLTVVVYC WWMLNAAYKS PQYAEGKVPV IVCVGSPTQT
DSLESRFEHK NLKCHVRSSE NVLTHIITNR TIREYVSLST NWAIFINNKR CQEYEFGELM
KVLEYGLPIT EEHMRLVDTF VVPEAYINNP ANLPGWTRLY SSHKEVSAYM AKLHAHLKVS
GERQFVVFTL PAYTFVKTAA FDEYKKITQQ PSLSLDKWLA ANASRVSNYS QSRDQDAGKT
QCEYYSEHGV VVARTDVTYV LNSQVSVTTR MRKFVFGFSG TFETFDAVLK DDAFIKTQGE
TSVEYAYRFL STLLFSGMIN FYNFLKRPGL DEGRVREAYR RMAALTAKLI PGASVLESAC
DNPSGAPLNF RGLTDPPGFT GGTTNDWDDD NDVVFAALNE GAIDMLYCNY EFVRPETTQE
VYSQFLMLKT MFVGRYSIFM DLFGGDFESS PFDTFVDNIS YKGCEIFVGS MRGGVSSIAL
QTDSYTLMGY TSAPVYPFVE ELARRKLHEG IAELFGAMNM PRMVLRDQHG FMSVLNVNLS
EFVESVDDVE LDMATAVDYG LSSRLAMTIA RSQGLSLDKV AICFPRNNLR INSVYVAMSR
TVSSRFLRMN LNPLRERHER DTVISEHILA ALRDRDVQIV Y