PRIM_VZVD
ID PRIM_VZVD Reviewed; 1083 AA.
AC P09270;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN ORFNames=ORF6;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27889.1; -; Genomic_DNA.
DR PIR; F27212; WZBE6.
DR PRIDE; P09270; -.
DR Proteomes; UP000002602; 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..1083
FT /note="DNA primase"
FT /id="PRO_0000116112"
FT ZN_FING 1022..1061
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 669
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 671
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ SEQUENCE 1083 AA; 122547 MW; F9F2FF57A77EE225 CRC64;
MDKSSKPTIR LLFATKGCAI SHSLLLLTGQ ISTEPLYVVS YTWTPDLDDV FVKNGREEIT
QVIPTKRPRE VTENDEENQI MHLFCSRDVN VIFYLIGGFS TGDVRSRVWP IFFCCFKTQT
DFKALYKALW YGAPLNPHII SDTLCISETF DIHSEVIQTL MVTTHHLNRK GLSDNGLCIT
EATLCKLVKK SVGRQELTSL YAHYERQVLA AYRRLYWGYG CSPFWYIVRF GPSEKTLVLA
TRYYLLQTDT SYNTLETPLY DLQAIKDLFL TYQVPALPNC SGYNISDLLS FDKLSMFCCS
STYTRGLTAK NALSYILQRI HTDTTEIHAV SEYITNDRKG LKVPDREFVD YIYLAHFECF
NRKQIADHLQ AVTYSDFVNK PVLLKSSNLG KRATANFFNH VRSRLNMRDY IKKNVICDVT
ELGPEIGHKY TITKTYTLSL TYAAKPSKFI GVCDLATTLT RRVENIEKQF SPYGWSSTIP
SNPPGFDELS NFEDSGVSAE ALRAANFAND TPNQSGRTGF DTSPGITKLL LFFSAATGIA
THDVSILSYK TPLEALIGHS EVTGPMPVYR VALPHGAQAF AVIANDTWSS ITNRYTLPHE
ARLIAEDLKQ INPCNFVAAS LRDMQLTLLL STSVKNVSKI SSNIPKDQLY INRNELFNTN
LIITNLILDV DFHIRKPIPL GILHAGMRAF RHGILTAMQL LFPKAVVNPN KDPCYFYKTA
CPEPTVEVLD DDNLLDITSH SDIDFYIENG ELYTCVEENY TEDVWFFDTQ TTSEVHTHAD
VSNNENLHET LPCNCKEKIG FRVCVPIPNP YALVGSSTLK GFAQILQQAV LLEREFVEYI
GPYLRDFSFI DTGVYSHGHS LRLPFFSKVT TTGTAVGQLL PFYVVPEQCI DILAFVTSHR
NPANFHFHSR PQSNVPVQFI LHNLGGEYAE FFERKVARNK QIFSSPQISL TKALKERGVT
CLDAFTLEAF VDSTILESIV EHIAVHFPGR DREYTLTSSK CIAIKRDWVL FQLICGTKGF
TCLRYPHRGG RTAPRTFVSL RVDHHNRLCI SLAQQCFATK CDSNRMHTIF TLEVPNYPNL
TSS