LEF3_NPVAC
ID LEF3_NPVAC Reviewed; 385 AA.
AC P41453;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Late expression factor 3;
DE Short=LEF-3;
DE AltName: Full=Single-stranded DNA-binding protein;
DE Short=SSB;
GN Name=LEF-3;
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=L1;
RX PubMed=8350397; DOI=10.1128/jvi.67.9.5260-5268.1993;
RA Li Y., Passarelli A.L., Miller L.K.;
RT "Identification, sequence, and transcriptional mapping of lef-3, a
RT baculovirus gene involved in late and very late gene expression.";
RL J. Virol. 67:5260-5268(1993).
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 FUNCTION.
RX PubMed=7745748; DOI=10.1128/jvi.69.6.3924-3928.1995;
RA Hang X., Dong W., Guarino L.A.;
RT "The lef-3 gene of Autographa californica nuclear polyhedrosis virus
RT encodes a single-stranded DNA-binding protein.";
RL J. Virol. 69:3924-3928(1995).
RN [4]
RP SUBUNIT.
RX PubMed=9094629; DOI=10.1128/jvi.71.5.3574-3579.1997;
RA Evans J.T., Rohrmann G.F.;
RT "The baculovirus single-stranded DNA binding protein, LEF-3, forms a
RT homotrimer in solution.";
RL J. Virol. 71:3574-3579(1997).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9683569; DOI=10.1006/viro.1998.9235;
RA Wu Y., Carstens E.B.;
RT "A baculovirus single-stranded DNA binding protein, LEF-3, mediates the
RT nuclear localization of the putative helicase P143.";
RL Virology 247:32-40(1998).
RN [6]
RP INTERACTION WITH ALKALINE NUCLEASE.
RC STRAIN=E2;
RX PubMed=12551981; DOI=10.1128/jvi.77.4.2436-2444.2003;
RA Mikhailov V.S., Okano K., Rohrmann G.F.;
RT "Baculovirus alkaline nuclease possesses a 5'-->3' exonuclease activity and
RT associates with the DNA-binding protein LEF-3.";
RL J. Virol. 77:2436-2444(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH HELI 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 [8]
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).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH HELI, AND NUCLEAR LOCALIZATION
RP SIGNAL.
RX PubMed=19073335; DOI=10.1016/j.virol.2008.10.051;
RA Au V., Yu M., Carstens E.B.;
RT "Characterization of a baculovirus nuclear localization signal domain in
RT the late expression factor 3 protein.";
RL Virology 385:209-217(2009).
CC -!- FUNCTION: Single-stranded DNA-binding protein that plays a role in
CC viral DNA replication. Forms a stable complex with the alkaline
CC nuclease and mediates the transport of the helicase to the host
CC nucleus. {ECO:0000269|PubMed:15518813, ECO:0000269|PubMed:16103143,
CC ECO:0000269|PubMed:7745748, ECO:0000269|PubMed:8350397,
CC ECO:0000269|PubMed:9683569}.
CC -!- SUBUNIT: Homotrimer. Interacts with alkaline nuclease. Interacts with
CC HELI and IE1. {ECO:0000269|PubMed:12551981,
CC ECO:0000269|PubMed:15518813, ECO:0000269|PubMed:19073335,
CC ECO:0000269|PubMed:9094629}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16103143,
CC ECO:0000269|PubMed:19073335, ECO:0000269|PubMed:9683569}.
CC -!- SIMILARITY: Belongs to the baculoviridae LEF-3 family. {ECO:0000305}.
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DR EMBL; L18873; AAA02964.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66697.1; -; Genomic_DNA.
DR PIR; D72858; D72858.
DR RefSeq; NP_054097.1; NC_001623.1.
DR PRIDE; P41453; -.
DR GeneID; 1403900; -.
DR KEGG; vg:1403900; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0039715; C:nuclear viral factory; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019079; P:viral genome replication; IDA:UniProtKB.
DR InterPro; IPR008415; Baculo_LEF-3.
DR Pfam; PF05847; Baculo_LEF-3; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Early protein; Host nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..385
FT /note="Late expression factor 3"
FT /id="PRO_0000132822"
FT REGION 26..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:19073335"
SQ SEQUENCE 385 AA; 44551 MW; 9A25ECD7BA7FBDF1 CRC64;
MATKRSLSGE SSGEPLIKRM AMASSPKKIR ENYKRISGKL MSKMTLSIDN EYHYTFRIMS
DNKIQEYYGD SQSFKDMEEG KCYDISLNYV KTKFSQMIQI NEYKECEMEI ETATPMSDYL
TNKHFENEDG VNIIVKYKFI YKKINSGLYK VVFEVVYKNL NDDPDVVQVE CSVNAKTLIN
LFKNNIKGSD DINEVFKYLK DNENQIFTIY SIKCQQIFNG SNVYMNWNVV NSTRIELCEA
KESEAYSNLQ NCTNAKINIS RSNKHVASYN VNVLKSELEE NDMGDNKFIV QFKSDELNIA
DSDDCSTSSD LGKWNKSVFY VNTNKKTEAD SLQKLCADFN QISMLLEDNL IKVTIYVTVE
NGENHNMNVL GLLKYDEDEN EYKFL
