PRIM_SUHVK
ID PRIM_SUHVK Reviewed; 962 AA.
AC Q85228;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 51.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN Name=UL52;
OS Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS Kaplan)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=33703;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7637001; DOI=10.1128/jvi.69.9.5560-5567.1995;
RA Baumeister J., Klupp B.G., Mettenleiter T.C.;
RT "Pseudorabies virus and equine herpesvirus 1 share a nonessential gene
RT which is absent in other herpesviruses and located adjacent to a highly
RT conserved gene cluster.";
RL J. Virol. 69:5560-5567(1995).
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 -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X87246; CAA60690.1; -; Genomic_DNA.
DR IntAct; Q85228; 1.
DR PRIDE; Q85228; -.
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; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..962
FT /note="DNA primase"
FT /id="PRO_0000116114"
FT ZN_FING 894..932
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 534
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 536
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ SEQUENCE 962 AA; 103329 MW; 5175209AD4AAC840 CRC64;
MPPSMIRVLY ATDGCAITYS LMLLTGQEPS GAVYVVSYAW DGAGLDEAFS LPGERAEAEL
LARRPGVTFC LTGHVASVRV RPVFVAAATP AVVRALCRGE PLAARDVLEA MDEAATFALH
DGLIAALTMV LEQVRPRTGN AEYAPERPLR SIAVGRRGLT SLFVHHETQT LAAFRRLYGN
HNTPFWYVAR FGPEEKTLVL ATRLHLFHPR PAYDLRALKD LLLTYNPRVD PNPSGLDPAG
LLSFAALSRF CCLSGYARGP AAAHAARYVD ERVRADRAEM GVLRDYISHD RGSLKLPDRE
FVTYVYLAHF ESFNRARLRE HLDAVNVTDP AAPVGRSPLG ERAAAAFFRH VRAQLNIRDY
VAQNVTPSVA RLAPAMGAGY VEDRTYAALA ADAPRGLCDA AAGLARRVTA VEERLAPHGW
VRAPDEEQQQ PGADGAVLRR LLELAAAPGG GRARTALGAL LGLPDACPPA PVYRVELAHR
RQAFAVLAGD AWGRATARRD AAPEMAAHEP AAQMYVSRHE VFNARLAVTN IVLDVDFRLA
RPVPAGTLEA AMRGFRRAVL DALALLFPEA DGDWAAHPCY VYKSACPPGG ALAAAAGSAS
AASSDDGLEE APWDDDAALA DFGAAPGDED WADWDAGVPA EVYTCDDDEV GVGIGGAGGD
PGASALVRAP VPADERPPCG CRAKMGFRVC TPVPSPYAVA GADTVRGLAR VLQQAVLLER
DFIEPMGPYL QDFTFVDTGV YAHGRSLRLP FFAKVDGGGC HGRLLPFGDA PPGFDDPRNF
HFHARPAHAV TRVLHSLGGE YESFFERKAA RNREAFFARR TPLADMLRGL AVDAEDRRAL
EAFVADVAMA PVLRHLDAHF NGRAHEYAGA TAQRVVAKPD WVLFQLCGSA RFSCLRARHA
RSPPARTFVA LSVDAHDRLC ISLSQQCFAT KCGSNATRTI FTAEVGQSCS SAGARCTSSS
SG