ID   P28_VACC8               Reviewed;         239 AA.
AC   P0C775;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   23-FEB-2022, entry version 34.
DE   RecName: Full=E3 ubiquitin-protein ligase p28-like;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase p28-like {ECO:0000305};
GN   Name=p28; ORFNames=m8008R;
OS   Vaccinia virus (strain LC16m8) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10248;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16140764; DOI=10.1128/jvi.79.18.11873-11891.2005;
RA   Morikawa S., Sakiyama T., Hasegawa H., Saijo M., Maeda A., Kurane I.,
RA   Maeno G., Kimura J., Hirama C., Yoshida T., Asahi-Ozaki Y., Sata T.,
RA   Kurata T., Kojima A.;
RT   "An attenuated LC16m8 smallpox vaccine: analysis of full-genome sequence
RT   and induction of immune protection.";
RL   J. Virol. 79:11873-11891(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:0000250}.
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. Note=Localizes to viral
CC       factories, the sites of virus replication. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The vaccinia strains LC16m0 and LC16m8 encode a full-
CC       length E3 ubiquitin ligase p28 unlike the majority of the vaccinia
CC       strains.
CC   -!- SIMILARITY: Belongs to the poxviridae p28 protein family.
CC       {ECO:0000305}.
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DR   EMBL; AY678275; AAW23401.1; -; Genomic_DNA.
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..239
FT                   /note="E3 ubiquitin-protein ligase p28-like"
FT                   /id="PRO_0000395992"
FT   DOMAIN          21..131
FT                   /note="KilA-N"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00631"
FT   ZN_FING         170..223
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   239 AA;  28185 MW;  69076053856E9BC4 CRC64;
     MEFDPAKINT SSIDHVTILQ YIDEPNDIRL TVCIIRNINN ITYYINITKI NTHLANQFRA
     WKKRIAGRDY ITNLSRDTGI QQSKLTETIR NCQKNRNIYG LYIHYNLVIN VVIDWITDVI
     VQSILRGLVN WYIANNTYTP NNTTTISELD IIKILDKYED VYRVSKEKEC GICYEVVYSK
     RLENDRYFGL LDSCNHIFCI TCINIWHKTR RETGASDNCP ICRTRFRNIT MSKFYKLVN