HEPA_HCMVM
ID HEPA_HCMVM Reviewed; 873 AA.
AC F5HIG1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 23-FEB-2022, entry version 27.
DE RecName: Full=DNA helicase/primase complex-associated protein {ECO:0000255|HAMAP-Rule:MF_04010};
DE Short=HEPA {ECO:0000255|HAMAP-Rule:MF_04010};
DE AltName: Full=Primase-associated factor {ECO:0000255|HAMAP-Rule:MF_04010};
GN Name=UL102;
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 presumably elongates
CC using dNTPs. The primase-associated factor has no known catalytic
CC activity in the complex and may serve to facilitate the formation of
CC the replisome by directly interacting with the origin-binding protein
CC and the polymerase. {ECO:0000255|HAMAP-Rule:MF_04010}.
CC -!- SUBUNIT: Associates with the primase and the helicase to form the
CC helicase-primase complex. Interacts with the origin-binding protein.
CC Interacts with the polymerase catalytic subunit. {ECO:0000255|HAMAP-
CC Rule:MF_04010}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04010}.
CC -!- SIMILARITY: Belongs to the herpesviridae HEPA family.
CC {ECO:0000255|HAMAP-Rule:MF_04010}.
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DR EMBL; AY446894; AAR31652.1; -; Genomic_DNA.
DR RefSeq; YP_081548.1; NC_006273.2.
DR PRIDE; F5HIG1; -.
DR GeneID; 3077548; -.
DR KEGG; vg:3077548; -.
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:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR HAMAP; MF_04010; HSV_HEPA; 1.
DR InterPro; IPR004996; HSV_HEPA.
DR Pfam; PF03324; Herpes_HEPA; 1.
PE 3: Inferred from homology;
KW DNA replication; Host nucleus; Reference proteome.
FT CHAIN 1..873
FT /note="DNA helicase/primase complex-associated protein"
FT /id="PRO_0000418266"
FT REGION 394..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 94080 MW; 844F50617EBB045F CRC64;
MTAQPPLHHR HHPYTLFGTS CHLSWYGLLE ASVPIVQCLF LDLGGGRAEP RLHTFVVRGD
RLPPAEVRAV HRASYAALAS AVTTDADERR RGLEQRSAVL ARVLLEGSAL IRVLARTFTP
VQIQTDASGV EILEAAPALG VETTALSNAL SLFHVAKLVV IGSYPEVHEP RVVTHAAERV
SEEYGTHAHK KLRRGYYAYD LAMSFRVGTH KYVLERDDEA VLARLFEVRE VCFLRTCLRL
VTPVGFVAVA VTDEQCCLLL QSAWTHLYDV LFRGFAGQPP LRDYLGPDLF ETGAARSFFF
PGFPPVPVYA VHGLHTLMRE TALDAAAEVL SWCGLPDIVG SAGKLEVEPC ALSLGVPEDE
WQVFGTEAGG GAVRLNATAF RERPAGGDRR WLLPPLPRDD GDGENNVVEV SSSTGGAHPP
SDDATFTVHV RDATLHRVLI VDLVERVLAK CVRARDFNPY VRYSHRLHTY AVCEKFIENL
RFRSRRAFWQ IQSLLGYISE HVTSACASAG LLWVLSRGHR EFYVYDGYSG HGPVSAEVCV
RTVVDCYWRK LFGGDDPGPT CRVQESAPGV LLVWGDERLV GPFNFFYGNG GAGGSPLHGV
VGGFAAGHCG GACCAGCVVT HRHSSGGGGS GVGDADHASG GGLDAAAGSG HNGGSDRVSP
STPPAALGGC CCAAGGDWLS AVGHVLGRLP ALLRERVSVS ELEAVYREIL FRFVARRNDV
DFWLLRFQPG ENEVRPHAGV IDCAPFHGVW AEQGQIIVQS RDTALAADIG YGVYVDKAFA
MLTACVEVWA RELLSSSTAS TTTCSSSSVL SSALPSVTSS SSGTATVSPP SCSSSSATWL
EERDEWVRSL AVDAQHAAKR VASEGLRFFR LNA