PRIM_HHV7J
ID PRIM_HHV7J Reviewed; 861 AA.
AC P52468;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 23-FEB-2022, entry version 72.
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 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=57278;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA Nicholas J.;
RT "Determination and analysis of the complete nucleotide sequence of human
RT herpesvirus.";
RL J. Virol. 70:5975-5989(1996).
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; U43400; AAC54705.1; -; Genomic_DNA.
DR PIR; T41945; T41945.
DR RefSeq; YP_073783.1; NC_001716.2.
DR GeneID; 3289501; -.
DR KEGG; vg:3289501; -.
DR Proteomes; UP000009246; 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..861
FT /note="DNA primase"
FT /id="PRO_0000116110"
FT ZN_FING 805..843
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 861 AA; 101074 MW; 706B74EB4A007EE3 CRC64;
MTITVFATEY DPAHVIVNIL CKNPSEHLIF PIIVKYKPSK NVYFCMQTQK CKFSKRIETV
FVCDAESLNF SYYVKNALPI KSEDIIHCLN TEETENLYKD FLLSHVPEGS ENIEFKSLVF
FCKTIIIKHL TNKYLLPTSP FWFLSTYGQT EGMLLLTMYY YLFEEQKSTI ATTKNYVQCF
TDKLGDMVFT YSSMSEFINI TLKSNYRKKF VSFSEYAKQK NIRDRKEFLY LDKQIDIFRN
SVHLTNSFRV HYIYIAYSTA LEKNKFIKYS QLTSYDPTRS DTSQCQENMY ILGNSLHSDL
ISIMKQYFNE DSYFQNYVEI KRMLNNKFQM QQYVYDINSN RNIMLVINSD QISKMVNKCN
KHGEGYFTPI KLGLQGFLKI LASNKSILID GKPVTRRQYL HDQFSNPIPM FRVQMSYKNL
YCFGSAESWY KNMGFDQVMQ FLPNEYISDE SLTSTFWLQD TTFLSDEIEK QFYVTRHEIF
NEYLPVTNYI GDLDLPLQDS AIITESLFFS MCKLMRNVLI NAWQKIFPFI DKDAYPIFFF
KTTCSNPENP LNHNVCYNEV ETAFCVCKKK IGLRIAIPIP QGTAIIGSEP LKQLSKIFNH
LMCLNHDLMQ ILNSVIFPGE CFDTGIYNTG RCLRLGFMYK VDEENNRFLY GRLKPIFIVP
EKMKKNFQDF VSMQLDLNNI LHHGTKDQTI TEIIYSIFDK ACPTEFSFID SRTKQLYHRK
QSSLETLCLK YLHVNGFSET SCLSRDDLLM TFTRSIAWPQ MLKKNIQHCE ARTATQFQHV
TFLKIDHKNI QLKKLQNGKL SDFSCLTRNH KGNRENVLVY LEFKVDNNRI LIILWSKCFT
TKCKSNSKQV HSSVVLDSLN M