IE2_NPVAC
ID IE2_NPVAC Reviewed; 408 AA.
AC P24647;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 29-SEP-2021, entry version 96.
DE RecName: Full=E3 ubiquitin-protein ligase IE2;
DE EC=2.3.2.27;
DE AltName: Full=Immediate-early protein IE2;
DE AltName: Full=RING-type E3 ubiquitin transferase IE2 {ECO:0000305};
GN Name=IE2; ORFNames=ORF151;
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].
RC STRAIN=E2;
RX PubMed=2024466; DOI=10.1016/0042-6822(91)90671-w;
RA Carson D.D., Summers M.D., Guarino L.A.;
RT "Molecular analysis of a baculovirus regulatory gene.";
RL Virology 182:279-286(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 SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=8009830; DOI=10.1006/viro.1994.1332;
RA Yoo S., Guarino L.A.;
RT "Functional dissection of the ie2 gene product of the baculovirus
RT Autographa californica nuclear polyhedrosis virus.";
RL Virology 202:164-172(1994).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11262179; DOI=10.1006/excr.2000.5081;
RA Murges D., Quadt I., Schroeer J., Knebel-Moersdorf D.;
RT "Dynamic nuclear localization of the baculovirus proteins IE2 and PE38
RT during the infection cycle: the promyelocytic leukemia protein colocalizes
RT with IE2.";
RL Exp. Cell Res. 264:219-232(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11967334; DOI=10.1128/jvi.76.10.5198-5207.2002;
RA Mainz D., Quadt I., Knebel-Moersdorf D.;
RT "Nuclear IE2 structures are related to viral DNA replication sites during
RT baculovirus infection.";
RL J. Virol. 76:5198-5207(2002).
CC -!- FUNCTION: RING-finger E3 ubiquitin ligase that plays an important
CC regulatory role during the initial stages of infection. Migrates to
CC specific nuclear foci early in infection supposely to prepare the sites
CC for viral transcription and replication by targeting and ubiquitinating
CC host proteins. Acts as a transcriptional activator and activates a
CC number of viral promoters including itself, IE1 and the promoter of 39K
CC gene. {ECO:0000250|UniProtKB:O92503, ECO:0000269|PubMed:11967334,
CC ECO:0000269|PubMed:8009830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:O92503}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:11262179,
CC ECO:0000269|PubMed:11967334, ECO:0000269|PubMed:8009830}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O92503}.
CC -!- SIMILARITY: Belongs to the alphabaculovirus IE2 protein family.
CC {ECO:0000305}.
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DR EMBL; M59422; AAA46701.1; -; Genomic_DNA.
DR EMBL; L22858; AAA66781.1; -; Genomic_DNA.
DR PIR; A39150; WMNVIA.
DR PIR; A72869; A72869.
DR RefSeq; NP_054182.1; NC_001623.1.
DR SMR; P24647; -.
DR GeneID; 1403984; -.
DR KEGG; vg:1403984; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0046782; P:regulation of viral transcription; IDA:UniProtKB.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Early protein; Host nucleus;
KW Host-virus interaction; Metal-binding;
KW Modulation of host ubiquitin pathway by viral E3 ligase;
KW Modulation of host ubiquitin pathway by virus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..408
FT /note="E3 ubiquitin-protein ligase IE2"
FT /id="PRO_0000056350"
FT REPEAT 34..41
FT /note="1-1"
FT REPEAT 42..49
FT /note="1-2"
FT REPEAT 51..54
FT /note="2-1"
FT REPEAT 55..58
FT /note="2-2"
FT ZN_FING 207..255
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..49
FT /note="2 X 8 AA tandem repeats of Q-P-S-S-S-S-R-S"
FT REGION 51..58
FT /note="2 X 4 AA tandem repeats of R-R-Q-E"
FT REGION 176..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 138
FT /note="A -> R (in Ref. 1; AAA46701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 47007 MW; DDB6F4862CCD8553 CRC64;
MSRQINAATP SSSRRHRLSL SRRRINFTTS PEAQPSSSSR SQPSSSSRSH RRQERRQEQR
VSEENVQIIG NVNEPLTRTY HRQGVTYYVH GQVNISNDDP LLSQEDDVIL INSENVDRER
FPDITAQQYQ DNIASETAAQ RALQRGLDLE AQLMNEIAPR SPTYSPSYSP NYVIPQSPDL
FASPQSPQPQ QQQQQQSEPE EEVEVSCNIC FTTFKDTKNV NSSFVTSIHC NHAVCFKCYV
KIIMDNSVYK CFCSATSSDC RVYNKHGYVE FMPINVTRNQ DSIKQHWREL LENNTVNNHT
TDLNYVEQLQ KELSELRAKT SQVEHKMTML NSDYIMLKHK HAVAELDLQK ANYDLQESTK
KSEELQSTVN NLQEQLRKQV AESQAKFSEF ERSNSDLVSK LQTVMSRR
