PRIM_EHV2
ID PRIM_EHV2 Reviewed; 884 AA.
AC Q66658;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 68.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN Name=56;
OS Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX NCBI_TaxID=82831;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT "The DNA sequence of equine herpesvirus 2.";
RL J. Mol. Biol. 249:520-528(1995).
CC -!- FUNCTION: Essential component of the helicase/primase complex. Unwinds
CC the DNA at the replication forks and generates single-stranded DNA for
CC both leading and lagging strand synthesis. The primase initiates primer
CC synthesis and thereby produces large amount of short RNA primers on the
CC lagging strand that the polymerase elongates using dNTPs.
CC {ECO:0000255|HAMAP-Rule:MF_04011}.
CC -!- SUBUNIT: Associates with the helicase and the primase-associated factor
CC to form the helicase-primase factor. {ECO:0000255|HAMAP-Rule:MF_04011}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011}.
CC Note=Requires the presence of the primase associated factor to properly
CC localize in the host cell nucleus. {ECO:0000255|HAMAP-Rule:MF_04011}.
CC -!- SIMILARITY: Belongs to the herpesviridae DNA primase family.
CC {ECO:0000255|HAMAP-Rule:MF_04011}.
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DR EMBL; U20824; AAC13844.1; -; Genomic_DNA.
DR PIR; S55651; S55651.
DR RefSeq; NP_042653.1; NC_001650.2.
DR PRIDE; Q66658; -.
DR GeneID; 1461069; -.
DR KEGG; vg:1461069; -.
DR Proteomes; UP000007083; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04011; HSV_PRIM; 1.
DR InterPro; IPR033685; HSV_PRIM.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; Helicase; Host nucleus; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..884
FT /note="DNA primase"
FT /id="PRO_0000406066"
FT ZN_FING 825..864
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 529
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 531
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ SEQUENCE 884 AA; 98684 MW; 76833888B1825537 CRC64;
MATGRSTSTE SSEKTCQQRD PLPEYRALCG TDGDAAEILT DVLTNTDSDG VVFCLAHNCY
SYNIGGGEAL LTLCLPAKRP WGAEKCLPVI QFRCDASRAQ EFLFQGRPIP VRYIQTNLNH
RAVKKFFKPI LSVLTCSDKK GGGGEGAHAD LKSTIFWFRA KFVAAVRKTF KITASPFWMI
STFGCTEAQF VLVSSCYFFE RHECTIDTLS HLSRLFDGSR GRQLTTVNTF SDLAGMFGTS
AWLGRVPEFS AYVGKKLARD DLESAAVDEA VNAFRGQLML SNADLIHYIY LSFFQCLNKE
KFLEYSLRTN PHNIDGVPPE EPIITGFIDE GFKSKMATYY TKSSYLKNHV RVGSLYLDGV
EGYSPEAIEA GPPAAAGGGG GADRYWAGQS RDVQGLLSDI LADHPASRLS PDLHGLLDLA
ALGDSSGVAG GVKDSLFPEP LRCPVYRCQY LNKTFFAVVT RDNLARAWER AVQLPTQVTG
WEGMEDARLT ACVHYAELAF SLGHLREQLS VSRHEYFNPR LPVFNLVLDF DLPLKKPGLS
LERVYSICRS VRSDVLSVLG VLGEVDEAAH PVYFFKSACP RPEWDEPYAG RPFCTCDAKL
GLRIITPLPR GVAIVGGAPL VALAKILNRM IKMNREDLLE ICPGLPDADG PLDTGIYHRG
RCVRLPHTYK VNEACGLERL LRLFVCHPGS PDKAAYIRDA MTLRNLLHHS KSAYWEGNAR
EGVSEEAPQK TKVVYSVTDV SENFLVCQTQ QQLPRSYERP DSRIETMTGR DLVTWVTEVA
WPKVFHNIKA YIPDDKTTQF HFVKFIHTSH NIIQVKPQRG NNFVCISSNH RNKTQSVRIF
IVLYTNKKDE VTITLMSQCF AHKCNSNKPR AHFSIPLQLR GRDF