HEPA_HHV6U
ID HEPA_HHV6U Reviewed; 662 AA.
AC P52375;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 02-JUN-2021, entry version 63.
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=U74; Synonyms=HDRF1;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7941342; DOI=10.1006/viro.1994.1589;
RA Nicholas J.;
RT "Nucleotide sequence analysis of a 21-kbp region of the genome of human
RT herpesvirus-6 containing homologues of human cytomegalovirus major
RT immediate-early and replication genes.";
RL Virology 204:738-750(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(1995).
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; U13194; AAA68465.1; -; Genomic_DNA.
DR EMBL; X83413; CAA58366.1; -; Genomic_DNA.
DR RefSeq; NP_042967.1; NC_001664.2.
DR PRIDE; P52375; -.
DR DNASU; 1487955; -.
DR GeneID; 1487955; -.
DR KEGG; vg:1487955; -.
DR Proteomes; UP000009295; 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..662
FT /note="DNA helicase/primase complex-associated protein"
FT /id="PRO_0000115861"
SQ SEQUENCE 662 AA; 76316 MW; 2E29BBAF108F7621 CRC64;
MHLRGCACHL SLYCVYNDWE NKIYRVPIFQ CLFLEAETRS LKTFLIRGQS LDQESLNEIE
VTRKETMLWD LQEQSNMMDK KIAAISNLIM NNGELVRTLS KFFVPLTVVL GDDGLEILEA
YVCGEELMLP LDTVPVILRC IGDYAALDTK HLLSNECTQA SKKIRFGYSV MDFHFSLTVS
DVKICFSHTD TGEAVCEKMK QIFSFSVCAF GGEQVLLVTP KNAYALLFDD DLCLLLLQSV
FAFLHEKIFG VYKQVLVQLC EYIGPDLWPF GNERSVSFIG YPNLWLLSVS DLERRVPDTT
YICREILSFC GLAPILGPRG RHAVPVVREL SIEMPGSETS LQRFRFNSQY VSSESLCFQT
GPEDTHLFFS DSDMYVVTLP DCLRLLLKST VPKAFLPCFD ENATEIDLLL KFMSRLQHRS
YALFDAVIFM LDAFVSAFQR ACTLMGMRWL LVRDLHMFYL TCDGKDTHVV MPLLQTAVEN
CWEKTTEIKQ RPTFQCAEIS RCGFIVYARF FLSSGLSQSK EAHWTVTASK YLSACIRTNK
TGLCFASITV YFQDMMCVFI ANRYNVSYWI EEFDPNDYCL EYHEGLLDCS RYTAVMSEDG
QLVRQARGIA LTDKINFSYY ILVTLRVLRR WVESKFEDVE QTQFIRWENR MLCEHIHLLH
LN