HEPA_HCMVA
ID HEPA_HCMVA Reviewed; 873 AA.
AC P16827; Q68286; Q7M6F6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 23-FEB-2022, entry version 69.
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 AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
RX PubMed=7853511; DOI=10.1128/jvi.69.3.1734-1740.1995;
RA Smith J.A., Pari G.S.;
RT "Human cytomegalovirus UL102 gene.";
RL J. Virol. 69:1734-1740(1995).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
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; X17403; CAA35338.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U18289; AAA67889.1; -; mRNA.
DR EMBL; BK000394; DAA00236.1; -; Genomic_DNA.
DR PIR; S09867; S09867.
DR MINT; P16827; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW DNA replication; Host nucleus; Reference proteome.
FT CHAIN 1..873
FT /note="DNA helicase/primase complex-associated protein"
FT /id="PRO_0000115865"
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"
FT CONFLICT 15
FT /note="T -> A (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="S -> T (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="P -> S (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="T -> A (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="G -> S (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..412
FT /note="PLPRDDGDGENNVVEVSS -> RCRVTTATVKTTSWKSAR (in Ref. 2;
FT AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="S -> G (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="Y -> C (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="S -> G (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="K -> R (in Ref. 2; AAA67889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 94050 MW; C2DB3734306FA4CB CRC64;
MTAQPPLHHR HHPYTLFGTS CHLSWYGLLE ASVPIVQCLF LDLGGGRAEP RLHTFVVRGD
RLPPAEVRAV HRASYAALAS AVTTDADERR RGLEQRSAVL ARVLLEGSAL IRVLARTFTP
VQIQTDASGV EILEAAPALG VETAALSNAL SLFHVAKLVV IGSYPEVHEP RVVTHTAERV
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 TTACSSSSVL SSALPSVTSS SSGTATVSPP SCSSSSATWL
EERDEWVRSL AVDAQHAAKR VASEGLRFFR LNA
