PRIM_ALHV1
ID PRIM_ALHV1 Reviewed; 837 AA.
AC O36406;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 02-DEC-2020, entry version 60.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN Name=56;
OS Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX NCBI_TaxID=654901;
OH NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA Ensser A., Pflanz R., Fleckenstein B.;
RT "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL J. Virol. 71:6517-6525(1997).
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; AF005370; AAC58103.1; -; Genomic_DNA.
DR PIR; T03151; T03151.
DR RefSeq; NP_065555.1; NC_002531.1.
DR GeneID; 911780; -.
DR KEGG; vg:911780; -.
DR Proteomes; UP000000941; 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..837
FT /note="DNA primase"
FT /id="PRO_0000405742"
FT ZN_FING 782..821
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 498
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 500
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ SEQUENCE 837 AA; 95341 MW; 620255A61104016A CRC64;
MTRVVKALFA ADTDCAELLA DILTGQNNSG SLYCLLHNCR PEDVSWEVTR LSLCLPVRRP
GGAEGRCAEV FKIKLPTEEA GQFLFNCGSL SAKQVYESYS KRAAYETFQP ILEVLGLSGD
EYSIKNAVTW GRGKFVASLR KYFKLTTSPH WFINTFGAFE NHFVLVSSCY YFFPVSVSTV
DTLCHLAMLY SSKKGCPLSS ITTLRELGAV ATQSPALDRV ENFYLYVCDK LARDTLECEA
VDRCINEFRG QLMLSDQDLV HYIYLSFFQC FNNQKFLAYS QCTNPCNLNT TMLREPMLVA
NIDSDFKHKM ATYYNKNTYL SNYVLLRGIH LHPVVGYGQE CLRSAHATGG HSIWWGESHQ
VSDMLKTINV EYPDICLHEE FRGLMDLAAI TDRCSIFGNP IHYLTDCATS GAIPIYRSEL
SHRHYFLAVF SDDIEYFWKK TIFLPPESFC LGAQDTMLTR AITYTEMHCS MSSVAEQIHV
SRHEYFNPKL PVFNWVLDLD LPISEGNLHI DSIYSLCLLI RESVLDILKL LGPVEPDHEV
FFFKSACINL CDPGEASWRP STFCTCTEKL GMRVVTRFPP GICLKGSEPL TQLTKILNRV
IKLGCGSLLN LSAFQLSNGP FDVGIYGRGR SIRLPHTYKV GKCGQLERLL KLFVCHPEAT
DKFPYLQNSL KLNRLLHHAQ SQDPRGPLKI IYRVEDINED FLYKHTQKQL PVKHEAVIPS
IERLLDTSLN CFLLSKVWPK CFGTIRSYMS EEKLQQFSRV VFHPTNHCIV QVRPDRGNNF
KCLRYNHRGS SKSVRVFLIL HLKEETKLIV TFMSQCFANK CQSNKAMAHF SVFVDLS