PRIM_GAHVM
ID PRIM_GAHVM Reviewed; 1074 AA.
AC Q9E6M4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 23-FEB-2022, entry version 62.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN Name=MDV066;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14246.1; -; Genomic_DNA.
DR RefSeq; YP_001033982.1; NC_002229.3.
DR PRIDE; Q9E6M4; -.
DR GeneID; 4811527; -.
DR KEGG; vg:4811527; -.
DR Proteomes; UP000008072; 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..1074
FT /note="DNA primase"
FT /id="PRO_0000406558"
FT ZN_FING 1012..1052
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 659
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 661
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ SEQUENCE 1074 AA; 120176 MW; 82C44B0125A161CE CRC64;
MARFSSISDT LESDDSGIKV LFAVDGCAVS FSLALLTGQI PSTNSVYVIG YWDPSDRFSS
IPFLDGDPNT NERISTTVCN LEDVPSPLRV EFCLLNQMAS GMGGADLKLR TRAIFVCRFT
SWSEMNAIAN SIIYGTPIQA GVLQATISET ETFMLHDEFN LALHVFLNGL SLKGRNKKDV
CMSLNHNYIS SVSENFPRGK RGLTGLYLQH EQKVTAAYRR IYGGSTTTAF WYVSKFGPDE
KSLVLALRYY LLQAQEEVTG IATGYDLQAI KDICKTYAVS VNPNPTGFLA ADLTSFSRLS
RFCCLSYYSK GSVAIAFPSY VERRIMADIA EVDALREYIE RDRPSLKISD LEFVKYIYLA
YFECYNREQL KRHLKDVTVS LPDEDIYKKS SLGKCAVENF FTHVRSRLNV NDHIAHNVLP
EQVEMGNKLV RKFGRARMYL STTMTNESHF TGICECASVI LKRLDTLEMK LQKYGWPSDR
VDGSNLMADN QNNSTLIPYD KSRSSGMILE CSNTHSRGGP MIVKRLLALV SADSRAGGIG
PANMLMGIDS AIDGPLPVYR VGMSKGRQAF TVLMTECWER TIPSPGSAKA HLIKLNNSYG
TSTEDLISRD LFLTSEIEQL IGSTVELPEI TCGSADEQQY INRNEVFNGN LAIGNIVLDV
DIHLRNPIPL RLMHAAIRGF RSGILRALAL LLPKANIDHG SYPCYFYKSS CKKSRVMGGA
PWMLHDAELA PDYSMFENAE FDLEMGIDDP LLIDQIDESL TRWSSESSRS VDLDPDKPCG
CHDKIGLRVC IPVPSPYLLV GSKTLAGLSR IIQQAVLLER NFVETIGPYL KNYEIIDSGV
YGHGRSLRLP FFGKIDENGI VSRRLVPFFV IPDDCADMEK FIVAHFEPKN FHFHSSIPLE
KAAIILKDIG GEYAGFFERK ITVNRDIFFG TRLSLSIALR ERGVDINDCA AITTFVTDHI
LDDIITYVYE HIPDHAIEYQ NLSVSCCVVK SDWILLQLIP NKTIGYRHGF TCVRFKHARA
RRASARSYLA LNVDAHGRLC VCVIQQCFAA KCGNNKLRTL FTVDIDSKCR LEHQ