HELI_GAHVM
ID HELI_GAHVM Reviewed; 858 AA.
AC Q9E6R1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=MDV017;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14197.1; -; Genomic_DNA.
DR RefSeq; YP_001033933.1; NC_002229.3.
DR GeneID; 4811478; -.
DR KEGG; vg:4811478; -.
DR Proteomes; UP000008072; 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..858
FT /note="DNA replication helicase"
FT /id="PRO_0000406580"
FT BINDING 75..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ SEQUENCE 858 AA; 97204 MW; 127F4458DD9CDD83 CRC64;
MSQESNDLFC EATYLNFTAM HGIQSIITRV RALADATLSD ELIPPLSYFI EASNHENPVE
LEARDLPFAV YLISGNAGSG KSTCIQTLSE ILDCIITGTT KVASQNIYCK LSNSYTSPHI
NTIFQEFGFK GNHVQANLGK WQYVCSTSPP TMKELQKKDI VYYWEVLSDI TKSMLKVLDS
ETGPGKFDVI RTLEDLLGKP RGNLSWMTFG IHGSLPSFTR SNIIIIDEAG LLGKYLLTAI
VYCWWLTNAV YRTPQYKRGL KPVLICVGSP TQTSSLESTF EHSKLRCNVR ISENILTYII
CNQTLRSYLD LSNNWAIFIN NKRCTEPEFG DLLKTLEYGL PITEEHARMA DNFVVPEAFI
NNPANLPGWT RLYSSHKEVS TYMSRLHDYL KTSGNNKFVV FTLPAYTFIS LENFERYRTA
ANQPHITLEK WLNVNAGRLS NWSQSRDQDA TQTRCEIRSQ QGLAISCSDI TYVLNSQVAV
TTRLRKWVFG FCGTFENFLS VLKDDSFIKT HGEGSIEYAY RFLSHLLFNG MINFYNYLQQ
RSLSEHAVKT AYNKLATLTN TILFPQRQLS AGDGENFNDV IVPTDLCHFE GKGIEDVDIQ
QRHENVDDVI FSALDDQMID LLYCNYEFGH AETSSEIYTQ FSMLKTMFMG RYSIMVELFG
RNFSTSRFDS YVDNVSSRGC EIFINNMRGG MLSLALQTDS YTLMGYTFAR VNAFADEPIR
RKIQPHVAEV LGELNMPTIV LKDQHGFMAA VNSNINDFVE SVDDHELKMA VTADYGISSK
LAMTIARSQG LSLERVAICF AHSGLKLSSV YVAMSRVTSS KYLRMNINPL RETHSRDDNN
ISEHLLAALR DPKVHIVY