ID   P28_CWPXB               Reviewed;         242 AA.
AC   Q8QN38;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   23-FEB-2022, entry version 78.
DE   RecName: Full=E3 ubiquitin-protein ligase p28-like;
DE            EC=2.3.2.27;
DE   AltName: Full=Protein CPXV023;
DE   AltName: Full=RING-type E3 ubiquitin transferase p28-like {ECO:0000305};
GN   Name=p28; OrderedLocusNames=CPXV023;
OS   Cowpox virus (strain Brighton Red) (CPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265872;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dietrich F.S., Ray C.A., Sharma A.D., Allen A., Pickup D.J.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the poxviridae p28 protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF482758; AAM13470.1; -; Genomic_DNA.
DR   RefSeq; NP_619812.1; NC_003663.2.
DR   DNASU; 1485898; -.
DR   GeneID; 1485898; -.
DR   KEGG; vg:1485898; -.
DR   Proteomes; UP000152733; Genome.
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..242
FT                   /note="E3 ubiquitin-protein ligase p28-like"
FT                   /id="PRO_0000395989"
FT   DOMAIN          21..131
FT                   /note="KilA-N"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00631"
FT   ZN_FING         173..226
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   242 AA;  28611 MW;  BDB013606035BEB6 CRC64;
     MEFDPTKINI SSIDHVTILQ YIDEPNDIRL TVCIIQNINN ITYYINITKI NPHLANQFRT
     WKKRIAGRDY MTNLSRDTGI QQSKLTETIR NCQKNRNIYG LYIHYNLVIN VVIDWITDVI
     VQSILRGLVN WYIANNNYTP NTPNNTTTIS ELDIIKILDK YEEVYRVSKE KECGICYEVV
     YSKRLENDRY FGLLDSCNHI FCITCINIWH RTRRETGASD NCPICRTRFR NITMSKFYKL
     VN