PRIM_MUHVS
ID PRIM_MUHVS Reviewed; 964 AA.
AC Q69153;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 65.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN Name=UL70;
OS Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Muromegalovirus.
OX NCBI_TaxID=10367;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7483291; DOI=10.1007/bf01724298;
RA Messerle M., Rapp M., Lucin P., Koszinowski U.H.;
RT "Characterization of a conserved gene block in the murine cytomegalovirus
RT genome.";
RL Virus Genes 10:73-80(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8971012; DOI=10.1128/jvi.70.12.8833-8849.1996;
RA Rawlinson W.D., Farrell H.E., Barrell B.G.;
RT "Analysis of the complete DNA sequence of murine cytomegalovirus.";
RL J. Virol. 70:8833-8849(1996).
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; L07319; AAA96665.1; -; Genomic_DNA.
DR EMBL; U68299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Proteomes; UP000008774; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
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 DNA replication; Host nucleus; Metal-binding; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..964
FT /note="DNA primase"
FT /id="PRO_0000116116"
FT REGION 807..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 527
FT /note="Essential for primase activity"
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"
SQ SEQUENCE 964 AA; 109704 MW; 70605300E1D85864 CRC64;
MTVVLFATEY DTPNIVVNML SETPTEHHLF PLMIKYKPSN RIEFVLQTQR CPDSTRVRPV
FICDARRLSL SEYVSTNTPL PARVICAGID ADATRELYEH LFDRKKDETG HDEENGSAAR
HLFSNLTSTL KCLVHYNRSA ILRYLNNTFL SPTFPSWFLS TYGTHEGTLI LTMSYYLFER
TYSTIQTTRD YTKCFTADPG RNLFTYINMR DFMATMNGSR FRKQTVLFAV FAKARNARDR
CELEYVDAKI NAFREESRLA ADSCVYYVYL AYRTALCREK FLQYCEHTAY DKNLPDDQQC
AAEENYLGRS LDAELISIMN TYFSVEGYFG SYIHVDRAKL SPPHSYRGYD WNTEADTMVG
YSSTATNLAI SLRKLNSTCE SLFSPLPPTL MGLLKLCASD RYVPRAEKSR KRTSGGREKE
DETRVCRRNY LLNDTSRPIG PMPVFRVEMP EKRHVFCAVS AENWTRRLLP KDLMKNLPSE
YVSDECLTDA VWLREDIAAL CEVGEQLYRT RHEMFNENLP VFNFVGDVDL KLREDLQGLS
RQEVFDLCRA LRRTLIGAWR HLFPEVDPDS HPVFFFKSAC PQNAAGAADE AMLYGGGGYD
EDDDPRPEHA AAMVDYGDAV RRPPFCVCRR KLGLRVIIPF PPRTAAIGAQ TLKRLAGILD
HTLCLDRDLV CKLNAISHPG ECFDTGIYSH GRSIRMPLMY KLDEASGLIL HSRLNPIFIV
PAGYRDRPAE FVLQQLCPQN LTHHGRPPQR DGSADQLTEV VLHITDRACA DSDGNFLQSR
ARRAMSSGRL PLGPLLRAHL SLESGQSAPS LPTLVGRGGG GEGGASSDYE EERAVGSDEE
EDDDDVENLQ AFARRIAWPA LLRHTRNHYR EEVQQQLEAA TVFTAVGRTC VAVKRGLYGR
ARDFSCLARE TYTRQETVQV FLDIRGDQRR NVWATLWSRC FTRRCNSNAK QTHLSLKISL
PSQY