ID   P28_VAR67               Reviewed;         242 AA.
AC   Q76R05;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=E3 ubiquitin-protein ligase p28-like;
DE            EC=2.3.2.27;
DE   AltName: Full=D4R protein;
DE   AltName: Full=RING-type E3 ubiquitin transferase p28-like {ECO:0000305};
GN   Name=p28; ORFNames=D4R;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=India-1967;
RX   PubMed=8384129; DOI=10.1016/0014-5793(93)80041-r;
RA   Shchelkunov S.N., Blinov V.M., Sandakhchiev L.S.;
RT   "Genes of variola and vaccinia viruses necessary to overcome the host
RT   protective mechanisms.";
RL   FEBS Lett. 319:80-83(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=India-1967;
RX   PubMed=7856312; DOI=10.1016/0168-1702(94)90125-2;
RA   Shchelkunov S.N., Blinov V.M., Resenchuk S.M., Totmenin A.V., Olenina L.V.,
RA   Chirikova G.B., Sandakhchiev L.S.;
RT   "Analysis of the nucleotide sequence of 53 kbp from the right terminus of
RT   the genome of variola major virus strain India-1967.";
RL   Virus Res. 34:207-236(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=India-1967;
RX   PubMed=8725113; DOI=10.1016/0168-1702(95)01269-9;
RA   Shchelkunov S.N., Totmenin A.V., Sandakhchiev L.S.;
RT   "Analysis of the nucleotide sequence of 23.8 kbp from the left terminus of
RT   the genome of variola major virus strain India-1967.";
RL   Virus Res. 40:169-183(1996).
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}.
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DR   EMBL; X69198; CAA48945.1; -; Genomic_DNA.
DR   RefSeq; NP_042048.1; NC_001611.1.
DR   GeneID; 1486399; -.
DR   KEGG; vg:1486399; -.
DR   Proteomes; UP000002060; 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; Reference proteome;
KW   Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..242
FT                   /note="E3 ubiquitin-protein ligase p28-like"
FT                   /id="PRO_0000395990"
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;  28556 MW;  07A0D10D5B96740A CRC64;
     MEFDPTKINI SSIDHVTILQ YIDEPNDIRL TVCIIQNINN ITYYINITKI NPHLANQFRA
     WKKRIAGRDY MTNLSRDTGI QQSNLTETIR NCQKNRNIYG LYIHYNLVIN VVIDWITDVI
     VQSILRGLVN WYIDNNTYTP NTPNNTTTIS ELDIIKILDK YEDVYKVSKE KECGICYEVV
     YSKRLENDRY FGLLDSCNHI FCITCINIWH RTRRETGASD NCPICRTRFR NITMSKFYKL
     VN