ID   HELI_HCMVM              Reviewed;         956 AA.
AC   F5HEN8;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 33.
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=UL105;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
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; AY446894; AAR31655.1; -; Genomic_DNA.
DR   RefSeq; YP_081551.1; NC_006273.2.
DR   PRIDE; F5HEN8; -.
DR   GeneID; 3077546; -.
DR   KEGG; vg:3077546; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; 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..956
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000418233"
FT   REGION          658..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         120..127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ   SEQUENCE   956 AA;  106508 MW;  3196BB7A55BFE9F4 CRC64;
     MSMTASSSTP RPTPKYDDAL ILNLSSAAKI ERIVDKVKSL SRERFAPEDF SFQWFRSISR
     VERTTDNNPS AATTAAATAT VHSSVSSSAA AAASSEAGGT RVPCVDRWPF FPFRALLVTG
     TAGAGKTSSI QVLAANLDCV ITGTTVIAAQ NLSAILNRTR SAQVKTIYRV FGFVSKHVPL
     ADSAVSHETL ERYRVCEPHE ETTIQRLQIN DLLAYWPVIA DIVDKCLNMW ERKAASASAA
     AAAAACEDLS ELCESNIIVI DECGLMLRYM LQVVVFFYYF YNALGDTRLY RERRVPCIIC
     VGSPTQTEAL ESRYDHYTQN KSVRKGVDVL SALIQNEVLI NYCDIADNWV MFIHNKRCTD
     LDFGDLLKYM EFGIPLKEEH VAYVDRFVRP PSSIRNPSYA AEMTRLFLSH VEVQAYFKRL
     HEQIRLSERH RLFDLPVYCV VNNRAYQELC ELADPLGDSP QPVELWFRQN LARIINYSQF
     VDHNLSSEIT KEALRPAADV VATNNPSVQA HGGGGSVIGS TGGNDETAFF QDDDTTTAPD
     SRETLLTLRI TYIKGSSVGV NSKVRACVIG YQGTVERFVD ILQKDTFIER TPCEQAAYAY
     SLVSGLLFSA MYYFYVSPYT TEEMLRELAR VELPDVSSLC AAAAATAAAP AWSGGENPIN
     NHVDADSSQG GQSVPVSQRM EHGQEETHDI PCLSNHHDDS DAITDAELMD HTSLYADPFF
     LKYVKPPSLA LLSFEETVHM YTTFRDIFLK RYQLMQRLTG GRFATLPLVT YNRRNVVFKA
     NCQISSQTGS FVGMLSHVSP AQTYTLEGYT SDNVLSLPSD RHRIHPEVVQ RGLSRLVLRD
     ALGFLFVLDV NVSRFVESAQ GKSLHVCTTV DYGLTSRTAM TIAKSQGLSL EKVAVDFGDH
     PKNLKMSHIY VAMSRVTDPE HLMMNVNPLR LPYEKNTAIT PYICRALKDK RTTLIF