HEPA_HHV6Z
ID HEPA_HHV6Z Reviewed; 662 AA.
AC P52451;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 02-JUN-2021, entry version 68.
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=CB1R;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8634027; DOI=10.1007/bf01718406;
RA Lindquester G.J., Inoue N., Allen R.D., Castelli J.W., Stamey F.R.,
RA Dambaugh T.R., O'Brian J.J., Danovich R.M., Frenkel N., Pellett P.E.;
RT "Restriction endonuclease mapping and molecular cloning of the human
RT herpesvirus 6 variant B strain Z29 genome.";
RL Arch. Virol. 141:367-379(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
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; AF157706; AAB06357.1; -; Genomic_DNA.
DR PIR; T44219; T44219.
DR RefSeq; NP_050253.1; NC_000898.1.
DR PRIDE; P52451; -.
DR DNASU; 1497074; -.
DR GeneID; 1497074; -.
DR KEGG; vg:1497074; -.
DR Proteomes; UP000006930; 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_0000115862"
SQ SEQUENCE 662 AA; 76550 MW; 5EDC7429E888B0AC CRC64;
MHLRGCACHL SLYCVYNDWE NKIYRVPIFQ CLFLEAETRS LKTFLIRGQS LDQESLNEIE
VTRKETMLWD LQEQSNMMDK KIAAISSLIM NNGELLRKLS KFFVPLTVVL GDDGLEILEA
YVCGEEPMLP LDTVPVILRC VGDYAALDTK HLLSNECTQA SKKLRFGYSV MDFHFSLTVS
DVKICFSHTD TGEAVCEKMK QIFYFSVCAF GGEQVLLVTP KNAYALLFDD DLCLLLLQSV
FAFLHEKIFA VYKQVLVQLC EYIGPDLWPF GNERSVSFIG YPNLWLLSVS DLERRVPDTT
YICREILSFC GLAPILGPRG RHAIPVIREL SVEMPGSETS LQRFRFNSQY VSSESLCFQT
GPEDTHLFFS DSDMYVVTLP DCLRLLLKST VPRAFLPCFD ENATEIELLL KFMSRLQHRS
YALFDAVIFM LDAFVSAFQR ACTLMEMRWL LVRDLHVFYL TCDGKDSHVV MPLLQTAVEN
CWEKITEIKQ RPAFQCMEIS RCGFVFYARF FLSSGLSQSK EAHWTVTASK YLSACIRANK
TGLCFASITV YFQDMMCVFI ANRYNVSYWI EEFDPNDYCL EYHEGLLDCS RYTAVMSEDG
QLVRQARGIA LTDKINFSYY ILVTLRVLRR WVESKFEDVE QAEFIRWENR MLYEHIHLLH
LN