PRIM_HHV2H
ID PRIM_HHV2H Reviewed; 1066 AA.
AC P89471;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 23-FEB-2022, entry version 70.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN ORFNames=UL52;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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; Z86099; CAB06739.1; -; Genomic_DNA.
DR ChEMBL; CHEMBL4630722; -.
DR PRIDE; P89471; -.
DR Proteomes; UP000001874; 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..1066
FT /note="DNA primase"
FT /id="PRO_0000385149"
FT ZN_FING 995..1035
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT REGION 694..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 631
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 633
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ SEQUENCE 1066 AA; 114654 MW; A6BD223DED54C17F CRC64;
MGTEDCDHEG RSVAAPVEVT ALYATDGCVI TSSLALLTNC LLGAEPLYIF SYDAYRSDAP
NGPTGAPTEQ ERFEGSRALY RDAGGLNGDS FRVTFCLLGT EVGVTHHPKG RTRPMFVCRF
ERADDVAVLQ DALGRGTPLL PAHVTATLDL EATFALHANI IMALTVAIVH NAPARIGSGS
TAPLYEPGES MRSVVGRMSL GQRGLTTLFV HHEARVLGAY RRAYYGSAQS PFWFLSKFGP
DEKSLVLAAR YYLLQAPRLG GAGATYDLQA VKDICATYAI PHDPRPDTLS AASLTSFAAI
TRFCCTSQYS RGAAAAGFPL YVERRIAADV RETGALEKFI AHDRSCLRVS DREFITYIYL
AHFECFSPPR LATHLRAVTT HDPSPAASTE QPSPLGREAV EQFFRHVRAQ LNIREYVKQN
VTPRETALAG DAAAAYLRAR TYAPAALTPA PAYCGVADSS TKMMGRLAEA ERLLVPHGWP
AFAPTTPGDD AGGGTAAPQT CGIVKRLLKL AATEQQGTTP PAIAALMQDA SVQTPLPVYR
ITMSPTGQAF AAAARDDWAR VTRDARPPEA TVVADAAAAP EPGALGRRLT RRICARGPAL
PPGGLAVGGQ MYVNRNEIFN AALAVTNIIL DLDIALKEPV PFPRLHEALG HFRRGALAAV
QLLFPAARVD PDAYPCYFFK SACRPRAPPV CAGDGPSAGG DDGDGDWFPD AGGPGDEEWE
EDTDPMDTTH GPLPDDEAAY LDLLHEQIPA ATPSEPDSVV CSCADKIGLR VCLPVPAPYV
VHGSLTMRGV ARVIQQAVLL DRDFVEAVGS HVKNFLLIDT GVYAHGHSLR LPYFAKIGPD
GSACGRLLPV FVIPPACEDV PAFVAAHADP RRFHFHAPPM FSAAPREIRV LHSLGGDYVS
FFEKKASRNA LEHFGRRETL TEVLGRYDVR PDAGETVEGF ASELLGRIVA CIEAHFPEHA
REYQAVSVRR AVIKDDWVLL QLIPGRGALN QSLSCLRFKH GRASRATART FLALSVGTNN
RLCASLCQQC FATKCDNNRL HTLFTVDAGT PCSRSAPSST SRPSSS