HEPA_EHV1B
ID HEPA_EHV1B Reviewed; 716 AA.
AC P28946; Q6DLF7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 02-DEC-2020, 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 OrderedLocusNames=54;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
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; AY665713; AAT67311.1; -; Genomic_DNA.
DR PIR; I36800; WZBEE6.
DR Proteomes; UP000001189; 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..716
FT /note="DNA helicase/primase complex-associated protein"
FT /id="PRO_0000115859"
SQ SEQUENCE 716 AA; 77773 MW; 62AB49A671C6B5F1 CRC64;
MLCRRGSDYT AEFCHVPVSG ELLKRGARDA SLVTPARVAS AAQTAAVPGC WPLAPLGNAM
LWKSVYGGIT AALKRAVGSF AFYQPLVLGI NTQTGLLVTL RPAASAGEGG GDHVSPRAAI
VNVSVEVDLD PAGIEASAAS STGSSLARAR LCTLRDGYFL SKRDIALEVE IATKEVSFYR
KYDSVQQPAN KRRGDMADLF VVHERTLLLG GCKRMGVKVL LPRTFDCLVA SSQSVSGLAA
MALYKQWHAT LFSVELPDTV VQIFAYLGPE LNPCGEEVDY CCFVGFPGLP TLKASSSTTE
AVRDAMAAYR LSDGLWPALG MSAFHFLAPW DPEDRWPGES EAKRVEGAVH RLQLGTEDDW
GAGRVSCILE SDAVMQGPWF AKFDFSAFFP TLYLLLFPAN ERLAEVVRLR ARGQHPTLKL
ALVSFFGGLQ HINPVAYRSI IALSNGISKR LEHEVNQRGF AICTYVKDGF WGAAGNLPSD
SVSYADALVY AEELRSAAQK AALGHVSEMG FSLPEGVHLN LRLEGLFTDA ISWSTHCYWL
YNRFTKMEDF VGFPAKSGAG RAAKASLSAL LPLVAAVCDS SDMSTLHQSV RGACEQLVAG
AFAERNNPQF WSTRTGIESS TLLPPAVYRN GSLLDRDCGQ REIVLTRKHD CESPSPVPWT
LFPPPLVLGR IDCMVYLTSI FKTYLSMLNR AISASCDADE SMNVDFPISD YAFLFT