ID HEPA_HHV11 Reviewed; 750 AA. AC P10192; B9VQD5; Q09IC5; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 21-SEP-2011, entry version 56. DE RecName: Full=DNA helicase/primase complex-associated protein; DE Short=HEPA; DE AltName: Full=Primase-associated factor; GN ORFNames=UL8; OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus OS 1). OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Alphaherpesvirinae; Simplexvirus. OX NCBI_TaxID=10299; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=88274327; PubMed=2839594; RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., RA McNab D., Perry L.J., Scott J.E., Taylor P.; RT "The complete DNA sequence of the long unique region in the genome of RT herpes simplex virus type 1."; RL J. Gen. Virol. 69:1531-1574(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88091053; PubMed=2826807; RA McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., RA Taylor P., Challberg M.D.; RT "Structures of herpes simplex virus type 1 genes required for RT replication of virus DNA."; RL J. Virol. 62:444-453(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nonneuroinvasive mutant HF10; RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019; RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.; RT "Determination and analysis of the DNA sequence of highly attenuated RT herpes simplex virus type 1 mutant HF10, a potential oncolytic RT virus."; RL Microbes Infect. 9:142-149(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17 syn+; RA Cunningham C., Davison A.J.; RT "Herpes simplex virus type 1 bacterial artificial chromosome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP INTERACTION WITH UL9, AND FUNCTION. RX PubMed=7931156; RA McLean G.W., Abbotts A.P., Parry M.E., Marsden H.S., Stow N.D.; RT "The herpes simplex virus type 1 origin-binding protein interacts RT specifically with the viral UL8 protein."; RL J. Gen. Virol. 75:2699-2706(1994). RN [6] RP INTERACTION WITH UL30, AND FUNCTION. RX PubMed=9261356; RA Marsden H.S., McLean G.W., Barnard E.C., Francis G.J., MacEachran K., RA Murphy M., McVey G., Cross A., Abbotts A.P., Stow N.D.; RT "The catalytic subunit of the DNA polymerase of herpes simplex virus RT type 1 interacts specifically with the C terminus of the UL8 component RT of the viral helicase-primase complex."; RL J. Virol. 71:6390-6397(1997). CC -!- FUNCTION: Component of the helicase/primase complex. Unwinds the CC DNA at the replication forks and generates single-stranded DNA for CC both leading and lagging strand synthesis. The primase synthesizes CC short RNA primers on the lagging strand that the polymerase CC presumably elongates using dNTPs. The primase-associated factor CC has no known catalytic activity in the complex and may serve to CC facilitate the formation of the replisome by directly interacting CC with the origin-binding protein and the polymerase. CC -!- SUBUNIT: Associates with the helicase-primase complex composed of CC the primase, the helicase and the primase-associated factor. CC Interacts with origin-binding protein. Interacts with the CC polymerase catalytic subunit. CC -!- SUBCELLULAR LOCATION: Host nucleus (By similarity). CC -!- SIMILARITY: Belongs to the herpesviridae HEPA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14112; CAA32344.1; -; Genomic_DNA. DR EMBL; M19120; AAA45823.1; -; Genomic_DNA. DR EMBL; DQ889502; ABI63470.1; -; Genomic_DNA. DR EMBL; FJ593289; ACM62230.1; -; Genomic_DNA. DR PIR; C29890; WMBEX8. DR RefSeq; NP_044609.1; NC_001806.1. DR DIP; DIP-1097N; -. DR MINT; MINT-6732582; -. DR GeneID; 2703432; -. DR ProtClustDB; PHA3144; -. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR InterPro; IPR004996; DNA_helic/primase-assoc_herpes. DR Pfam; PF03324; Herpes_HEPA; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA replication; Host nucleus; Reference proteome. FT CHAIN 1 750 DNA helicase/primase complex-associated FT protein. FT /FTId=PRO_0000115856. FT COMPBIAS 337 343 Poly-Ala. FT VARIANT 247 247 T -> M (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 330 330 A -> T (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 353 353 A -> V (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 467 467 N -> D (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 471 471 A -> V (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 543 544 AV -> GL (in strain: Nonneuroinvasive FT mutant HF10 and 17 syn+). FT VARIANT 612 612 C -> G (in strain: Nonneuroinvasive FT mutant HF10). SQ SEQUENCE 750 AA; 79926 MW; ECA9ABD0E85CB392 CRC64; MDTADIVWVE ESVSAITLYA VWLPPRAREY FHALVYFVCR NAAGEGRARF AEVSVTATEL RDFYGSADVS VQAVVAAARA ATTPAASPLE PLENPTLWRA LYACVLAALE RQTGPVALFA PLRIGSDPRT GLVVKVERAS WGPPAAPRAA LLVAEANIDI DPMALAARVA EHPDARLAWA RLAAIRDTPQ CASAASLTVN ITTGTALFAR EYQTLAFPPI KKEGAFGDLV EVCEVGLRPR GHPQRVTARV LLPRDYDYFV SAGEKFSAPA LVALFRQWHT TVHAAPGALA PVFAFLGPEF EVRGGPVPYF AVLGFPGWPT FTVPATAESA RDLVRGAAAA YAALLGAWPA VGARVVLPPR AWPGVASAAA GCLLPAVREA VARWHPATKI IQLLDPPAAV GPVWTARFCF PGLRAQLLAA LADLGGSGLA DPHGRTGLAR LDALVVAAPS EPWAGAVLER LVPDTCNACP ALRQLLGGVM AAVCLQIEET ASSVKFAVCG GDGGAFWGVF NVDPQDADAA SGVIEDARRA IETAVGAVLR ANAVRLRHPL CLALEGVYTH AVAWSQAGVW FWNSRDNTDH LGGFPLRGPA YTTAAGVVRD TLRRVLGLTT ACVPEEDALT ARGLMEDACD RLILDAFNKR LDAEYWSVRV SPFEASDPLP PTAFRGGALL DAEHYWRRVV RVCPGGGESV GVPVDLYPRP LVLPPVDCAH HLREILREIE LVFTGVLAGV WGEGGKFVYP FDDKMSFLFA //