ID   P28_ECTVM               Reviewed;         241 AA.
AC   Q85318;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 87.
DE   RecName: Full=E3 ubiquitin-protein ligase p28;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase p28-like {ECO:0000305};
GN   Name=p28; OrderedLocusNames=EVM1012;
OS   Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265874;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Chen N., Danila M.I., Feng Z., Buller M.L., Wang C., Han X., Lefkowitz E.,
RA   Upton C.;
RT   "The genomic sequence of ectromelia virus, the causative agent of
RT   mousepox.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=10725436; DOI=10.1099/0022-1317-81-4-1087;
RA   Brick D.J., Burke R.D., Minkley A.A., Upton C.;
RT   "Ectromelia virus virulence factor p28 acts upstream of caspase-3 in
RT   response to UV light-induced apoptosis.";
RL   J. Gen. Virol. 81:1087-1097(2000).
RN   [3]
RP   FUNCTION.
RX   PubMed=15496420; DOI=10.1074/jbc.m410583200;
RA   Huang J., Huang Q., Zhou X., Shen M.M., Yen A., Yu S.X., Dong G., Qu K.,
RA   Huang P., Anderson E.M., Daniel-Issakani S., Buller R.M., Payan D.G.,
RA   Lu H.H.;
RT   "The poxvirus p28 virulence factor is an E3 ubiquitin ligase.";
RL   J. Biol. Chem. 279:54110-54116(2004).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15596852; DOI=10.1128/jvi.79.1.597-601.2005;
RA   Nerenberg B.T., Taylor J., Bartee E., Gouveia K., Barry M., Fruh K.;
RT   "The poxviral RING protein p28 is a ubiquitin ligase that targets ubiquitin
RT   to viral replication factories.";
RL   J. Virol. 79:597-601(2005).
CC   -!- FUNCTION: RING-finger E3 ubiquitin ligase which catalyzes the formation
CC       of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Plays an
CC       important role in virulence by acting as an anti-apoptotic factor.
CC       {ECO:0000269|PubMed:10725436, ECO:0000269|PubMed:15496420,
CC       ECO:0000269|PubMed:15596852}.
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   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:15596852}.
CC       Note=Localizes to viral factories, the sites of virus replication.
CC   -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the poxviridae p28 protein family.
CC       {ECO:0000305}.
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DR   EMBL; U01161; AAA16258.1; -; Unassigned_DNA.
DR   EMBL; AF012825; AAM92318.1; -; Genomic_DNA.
DR   PIR; B49276; B49276.
DR   RefSeq; NP_671530.1; NC_004105.1.
DR   SMR; Q85318; -.
DR   GeneID; 1494459; -.
DR   KEGG; vg:1494459; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR016398; E3_ubiquitin-prot_ligase_p28.
DR   InterPro; IPR017880; KilA_N.
DR   InterPro; IPR018004; KilA_N/APSES_HTH.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11224; PTHR11224; 1.
DR   Pfam; PF04383; KilA-N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   PIRSF; PIRSF003775; E3_ubiquit_lig_p28; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS51301; KILA_N; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host-virus interaction; Metal-binding;
KW   Modulation of host cell apoptosis by virus;
KW   Modulation of host ubiquitin pathway by viral E3 ligase;
KW   Modulation of host ubiquitin pathway by virus; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..241
FT                   /note="E3 ubiquitin-protein ligase p28"
FT                   /id="PRO_0000395986"
FT   DOMAIN          21..131
FT                   /note="KilA-N"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00631"
FT   ZN_FING         172..225
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   241 AA;  28383 MW;  A19CBF2622A32E54 CRC64;
     MEFDPAKINT SSIDHVTILQ YIDEPNDIRL PVCIIRNINN ITYFINITKI NPDLANQFRA
     WKKRIAGRDY MTNLSRDTGI QQSKLTETIR NCQKNRNIYG LYIHYNLVIN VVIDWITDVI
     VQSILRGLVN WYIANNTYNP NTPNSTTISE LDIIKILDKY EDVYRVSKEK ECGICYEVVY
     SKRLENDRYF GLLDSCNHIF CITCINIWHR TRRETGASDN CPICRTRFRN ITMSKFYKLV
     N