HELI_NPVAC
ID HELI_NPVAC Reviewed; 1221 AA.
AC P24307;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA replication helicase;
DE EC=3.6.4.12;
DE AltName: Full=P143;
GN Name=HELI; ORFNames=ORF95;
OS Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46015;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=HR3;
RX PubMed=1994581; DOI=10.1016/0042-6822(91)90500-b;
RA Lu A., Carstens E.B.;
RT "Nucleotide sequence of a gene essential for viral DNA replication in the
RT baculovirus Autographa californica nuclear polyhedrosis virus.";
RL Virology 181:336-347(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6;
RX PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT virus.";
RL Virology 202:586-605(1994).
RN [3]
RP MUTAGENESIS OF VAL-934, AND FUNCTION.
RX PubMed=9887325; DOI=10.1006/viro.1998.9485;
RA Liu G., Carstens E.B.;
RT "Site-directed mutagenesis of the AcMNPV p143 gene: effects on baculovirus
RT DNA replication.";
RL Virology 253:125-136(1999).
RN [4]
RP INTERACTION WITH LEF-3 AND IE1.
RX PubMed=15518813; DOI=10.1016/j.virol.2004.08.035;
RA Ito E., Sahri D., Knippers R., Carstens E.B.;
RT "Baculovirus proteins IE-1, LEF-3, and P143 interact with DNA in vivo: a
RT formaldehyde cross-linking study.";
RL Virology 329:337-347(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16103143; DOI=10.1128/jvi.79.17.10915-10922.2005;
RA Chen Z., Carstens E.B.;
RT "Identification of domains in Autographa californica multiple
RT nucleopolyhedrovirus late expression factor 3 required for nuclear
RT transport of P143.";
RL J. Virol. 79:10915-10922(2005).
CC -!- FUNCTION: Essential for initiation of viral DNA replication, it may
CC contribute to other functions such as controlling the switch to the
CC late phase and leading to the inhibition of host protein synthesis.
CC Required for late and very late gene expression.
CC {ECO:0000269|PubMed:16103143, ECO:0000269|PubMed:1994581,
CC ECO:0000269|PubMed:9887325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with IE1 and LEF-3. {ECO:0000269|PubMed:15518813}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16103143}.
CC Note=LEF-3 is responsible for transporting the helicase to the host
CC nucleus. {ECO:0000269|PubMed:16103143}.
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DR EMBL; M57687; AAA67907.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66725.1; -; Genomic_DNA.
DR PIR; A38499; HJNVAV.
DR RefSeq; NP_054125.1; NC_001623.1.
DR PRIDE; P24307; -.
DR GeneID; 1403928; -.
DR KEGG; vg:1403928; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0039715; C:nuclear viral factory; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0019079; P:viral genome replication; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006824; DNA_helicase_Baculovir.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04735; Baculo_helicase; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Early protein; Helicase;
KW Host nucleus; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1221
FT /note="DNA replication helicase"
FT /id="PRO_0000132853"
FT DNA_BIND 967..981
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT MOTIF 692..701
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 917..924
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 934
FT /note="V->M: Defective in the synthesis of viral DNA, late
FT protein synthesis and the shutoff of host protein synthesis
FT at the nonpermissive temperature (mutant ts8)."
FT /evidence="ECO:0000269|PubMed:9887325"
FT CONFLICT 126
FT /note="F -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="F -> L (in Ref. 1; AAA67907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1221 AA; 143214 MW; 090E199855882D1B CRC64;
MIDNILQFFL KNVPQDKTYE INNLQDANHL IIRNTRTGTR RLFEYVNNFQ QFLNTIRNNF
NGPCAKHDMG ASCEDTEEPA EKHAAQTLDG HDWVLESNDF CIFVKPFILK KHYDIIQKYI
NFEDFFKSTD PGYINKCVQA GDYYYWPNWP KKQAFSFNGW QLFLNIKFGI VIEPTIPIIH
NKKLGPVDLF VFDPKCFLNV ELSLRTNHDP PQTLFVNGKT KFDDSHEDLF ILKMADGTVA
TCKVNGELVN SDKNFFNYIR DDINLEECIT VPKYKHIVNV NLKSLRVFEN NNFDKNDVDL
SDTRSRKPRI VPIISASSEN ADYIQTQINL GLIAIHENMV KVLATHERAN DPNLLQQYFE
KSKFKNFDFL IYVLWKILTK NENFSYRETD IKLFLELLCE SLFACDKEAL NEALKRCEPY
KKQEKIVFNR ACNHWFDFDD TKLCVSLGYY FGIHYMIYLT QSAKNEILDH DELWAYTYEN
VMALNLPPDI VCKGFFRKLE NVVTGVNLVF NGKHYQIVKK EDDLFKLTKS NCYKLSNIKF
NNWKYLYLTT HGVYNVFTNS FHSSCPFLLG TTLPQTFKKP TDEKYLPEDA FNYMLSTSAD
ELSIYRTYHI AKMCRDVKML KTNTAIVNYM GNCNTCQADM RVALNNLFRD LWNLDDENLI
TLALYVNKNR VSDMLHNLKC KPCRSTVSGS RPKCKCYKKI KINRKALKVC LMADMFGNDA
ELSELIWMLI FTNKTYVSTT LIRTNSEFVN QHGEFFSKEH NKIIQYLYRT IHKIEYVDML
MDKFNDKRLF LTELRDDVAR EPDVQFEESD NISKFYTHHA DALMILKKYN VWWDKIILAR
STDDLPTWLT RFYMRIIMSK VDLKEYSYNY LKKIVEGYLY FKRFTNFNHA NAIMLMHFAA
SLAIPVDYGK KAIYMPGEPG SGKSSFFELL DYLVLMHKFD DDNHSGESNK ETSDKEVSKL
NSQLYTINEL KQCSESYFKK HADSSKSDSK SRKYQGLLKY EANYKMLIVN NKPLYVDDYD
DGVQDRFLIV YTNHKFVDSV KFAGSVYEHI KSKQFPIESM YYESLVTPVR LFLSHVLMYR
RDPKTGFVVY KTLLSNDPMH KHNLMCLSTN NSPLYALIYI LNIKTVRSAT ITIGEDKMEE
MIGIAVQHFK NFLHPSFVQY NYKKNINASS SKSFVFNEQV LLQQIKNKFK NNYNKTTNVF
YNMTMALNRN DLNTSVPNFV C