ID   PRIM_ELHVK              Reviewed;         975 AA.
AC   Q18LF7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   23-FEB-2022, entry version 42.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF322977; ABG36562.1; -; Genomic_DNA.
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; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..975
FT                   /note="DNA primase"
FT                   /id="PRO_0000408166"
FT   ZN_FING         919..958
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            624
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            626
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ   SEQUENCE   975 AA;  112193 MW;  046E105324EBFD32 CRC64;
     MTIQVLFATE YDSANIVISL LCGVEVDHDL YPILYKRINY NNGASNNDGS RSGAINFDDR
     VNDEDSRLNA PVDDTIEFCL QTQSCEDSIR IRPVFYCHAH ALNFETRYRT HEVLGSATLL
     QCLDESRTLT MYRRILSEII TEPSSASEKR NPAPTNLRHL VYFHRDVLVK YLTENFIMPT
     SPAWFISVFG SYEASLVLTM HYYLLERQYS TVQTTQHYAK CFTGDMGKPL VSCYSMKDFM
     IMIQSSAFLG KTAKFTHYCK LKNDRDLQEL MAIDASINAF RQNVCLTEAE HVHFMYLAFG
     TALAKTKFLD YTLKTSLLSN NDDQTNNCND YIVDNCAVDN HCQNDIDEII IPRSSTNRTF
     AISEVSYDRS NSTSSSGVYS MDSCDESRGS EDSAMCSLYE SRYLSHNLKK ELLNIMELYF
     TPTSYLNIYV KVHKHESKSP LFEGYSIDTC SEKGTVFSGT STSMADRLRK GNKMFEGLFE
     ETDSEGVSSV LNIIASNRHA ILPRCEDDDS CGKSTSGMPN RICKREIVFP GLTRPAPMYR
     TDGFNNMQIC RYFSVVSKEN WFSNSNLTDV LNMVPDEYVS DERLTESVWV PDVKVSSPRL
     SEQLYRSRHE MFNDRLPVYN FVGDVDLKVT GPVSKDWMFS FCRTLRRIIL ETFEHLFEKI
     DHGEHPVYFF KSGCEPENGS FCACSEKIGL RVITPFPRNT CILGGKTMKH LCEIINHILF
     LDKEMFSLVN VTVVDKNCFD YGIYSHGKSV RLPMMSKVDE NLGFLQNRLL PLFIVPDSYR
     HGGRHKVFVR DQLNISNWLH HNASGTAYDP CKTISYVLSI DDVGRAQDVS FIDHKLNKLL
     KKEYVHIDTI IELFKSKYDI SETRYFIEKI VWPQFLRTIK TNYHSAAGNQ FNNVCFDDTS
     WPCVQLFKIH QGTRRNFSCI QHDHRDGREN VQFFLDFRPE SATTIWTTLW SRCFSRKCKS
     NAKNVHVSHK LTIQQ