PRIM_HHV6U
ID PRIM_HHV6U Reviewed; 860 AA.
AC P52467;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 02-JUN-2021, entry version 65.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN Name=U43;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(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}.
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DR EMBL; X83413; CAA58377.1; -; Genomic_DNA.
DR EMBL; X92436; CAA63169.1; -; Genomic_DNA.
DR RefSeq; NP_042936.1; NC_001664.2.
DR PRIDE; P52467; -.
DR DNASU; 1487921; -.
DR GeneID; 1487921; -.
DR KEGG; vg:1487921; -.
DR Proteomes; UP000009295; 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..860
FT /note="DNA primase"
FT /id="PRO_0000116108"
FT ZN_FING 804..842
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 492
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 494
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ SEQUENCE 860 AA; 100080 MW; 660E8AE30B4674F6 CRC64;
MTIVVFATEY DAANVIFSIL CRSPSEHLIF PIIVKYKPSN NVSFCLQTQK CKNSKRIDTV
FVCHAEKLNL SHYIQTASPI KAEDVANSLN DKETESLYVD MILSQTGKER EDVEFKYMAY
FHKSLIIKYL TGKFLLPTSP FWFLSTYGQT EGMLLLTMFY YLFEEQKSTI TTTKNYVQCF
TENTGNMVFT YSSMSEFINI TLKSKFRKLF ADFSTYARQK NLRDKEEFKH LDTQINLFRK
SSHLTNTFRV HYIYIAYNTA LETTKFVNYC NLTSYDSNLP IGQQCQRNLH ILGNSLHENL
LCIMKQYFNA DCYFKTYIDI KRLKNPNLNV TEYEYALVSK KKTIQALTSE QITRAIAKCN
KNGEGLFSPV KPGLQGLLEI SASDRYVQIQ DKRIYRRQHL HKDYHRPFPV FRVQLLHKNI
FCFGNSEDWY ENMGFNRILQ YLPDEYISDE ALTRAIWLQD THFLCDDVEK QFYTTRHEIF
NERIPVTNYI GDLDLPLQDT ATITEETFFS MCRLIRLTLI NAWKKIFPSI DTDTHPIFFF
KTQCDTTNDT LDYTEDPTEI KQFCVCRKKI GLRISIPLPN GTAIAGGEPL KQLSKILNHV
MCLDQELSQI LNSITFPGEC FDIGIYHTGH CIRIGYMYKT DMDKGKMLHG RLTPIFIVPE
GYRNSCKTFI QMQMDLNNLL HHGTKKAPIE ELIYNITDKG CPKENLSFMD LKSRQLWNKV
NIATETLITK YLNTHGFNNN ATSADDSLLS FIRLIGWPII KTQLITHYET RIAQQFSQVT
FIKIDSKNLQ IKKTQFGRVS DFSCLNRQHR GNRDNVLVYI QLKADGNRLI LILWSTCFAT
KCQSNSKQVH CSIALEQLKN