ID   IAP3_NPVOP              Reviewed;         268 AA.
AC   P41437;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=E3 ubiquitin-protein ligase IAP-3;
DE            EC=2.3.2.27;
DE   AltName: Full=IAP-3;
DE   AltName: Full=RING-type E3 ubiquitin transferase IAP-3 {ECO:0000305};
GN   Name=IAP3; Synonyms=IAP; ORFNames=ORF35;
OS   Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=262177;
OH   NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8139034; DOI=10.1128/jvi.68.4.2521-2528.1994;
RA   Birnbaum M.J., Clem R.J., Miller L.K.;
RT   "An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a
RT   polypeptide with Cys/His sequence motifs.";
RL   J. Virol. 68:2521-2528(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA   Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT   "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT   polyhedrosis virus genome.";
RL   Virology 229:381-399(1997).
RN   [3]
RP   FUNCTION.
RX   PubMed=15325084; DOI=10.1016/j.virusres.2004.04.017;
RA   Green M.C., Monser K.P., Clem R.J.;
RT   "Ubiquitin protein ligase activity of the anti-apoptotic baculovirus
RT   protein Op-IAP3.";
RL   Virus Res. 105:89-96(2004).
CC   -!- FUNCTION: RING-finger E3 ubiquitin ligase required to prevent cellular
CC       apoptosis in infected cells. Ubiquitinates and subsequently targets
CC       host pro-apoptotic cellular proteins such as HID for degradation by the
CC       proteasome. {ECO:0000269|PubMed:15325084}.
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   -!- PTM: Auto-ubiquitinated.
CC   -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR   EMBL; L22564; AAB02610.1; -; Genomic_DNA.
DR   EMBL; U75930; AAC59034.1; -; Genomic_DNA.
DR   PIR; A53989; A53989.
DR   RefSeq; NP_046191.1; NC_001875.2.
DR   SMR; P41437; -.
DR   MEROPS; I32.010; -.
DR   GeneID; 912041; -.
DR   KEGG; vg:912041; -.
DR   Proteomes; UP000009248; Genome.
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   CDD; cd00022; BIR; 2.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001370; BIR_rpt.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00653; BIR; 2.
DR   SMART; SM00238; BIR; 2.
DR   PROSITE; PS01282; BIR_REPEAT_1; 2.
DR   PROSITE; PS50143; BIR_REPEAT_2; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Host-virus interaction; Metal-binding;
KW   Modulation of host ubiquitin pathway by viral E3 ligase;
KW   Modulation of host ubiquitin pathway by virus; Repeat; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..268
FT                   /note="E3 ubiquitin-protein ligase IAP-3"
FT                   /id="PRO_0000122371"
FT   REPEAT          18..84
FT                   /note="BIR 1"
FT   REPEAT          111..178
FT                   /note="BIR 2"
FT   ZN_FING         221..256
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
SQ   SEQUENCE   268 AA;  30076 MW;  DF89175FDE85A708 CRC64;
     MSSRAIGAPQ EGADMKNKAA RLGTYTNWPV QFLEPSRMAA SGFYYLGRGD EVRCAFCKVE
     ITNWVRGDDP ETDHKRWAPQ CPFVRNNAHD TPHDRAPPAR SAAAHPQYAT EAARLRTFAE
     WPRGLKQRPE ELAEAGFFYT GQGDKTRCFC CDGGLKDWEP DDAPWQQHAR WYDRCEYVLL
     VKGRDFVQRV MTEACVVRDA DNEPHIERPA VEAEVADDRL CKICLGAEKT VCFVPCGHVV
     ACGKCAAGVT TCPVCRGQLD KAVRMYQV