P28_MONPZ
ID P28_MONPZ Reviewed; 242 AA.
AC Q8V571;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=E3 ubiquitin-protein ligase p28-like;
DE EC=2.3.2.27;
DE AltName: Full=Protein D5R;
DE AltName: Full=RING-type E3 ubiquitin transferase p28-like {ECO:0000305};
GN Name=p28; ORFNames=D5R;
OS Monkeypox virus (strain Zaire-96-I-16) (MPX).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=619591;
OH NCBI_TaxID=45479; Cynomys gunnisoni (Gunnison's prairie dog).
OH NCBI_TaxID=99825; Cynomys leucurus (White-tailed prairie dog).
OH NCBI_TaxID=45480; Cynomys ludovicianus (Black-tailed prairie dog).
OH NCBI_TaxID=99826; Cynomys mexicanus (Mexican prairie dog).
OH NCBI_TaxID=99827; Cynomys parvidens (Utah prairie dog).
OH NCBI_TaxID=30650; Gliridae (dormice).
OH NCBI_TaxID=226685; Heliosciurus ruwenzorii (Ruwenzori sun squirrel).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zaire-96-I-16;
RX PubMed=11734207; DOI=10.1016/s0014-5793(01)03144-1;
RA Shchelkunov S.N., Totmenin A.V., Babkin I.V., Safronov P.F.,
RA Ryazankina O.I., Petrov N.A., Gutorov V.V., Uvarova E.A., Mikheev M.V.,
RA Sisler J.R., Esposito J.J., Jahrling P.B., Moss B., Sandakhchiev L.S.;
RT "Human monkeypox and smallpox viruses: genomic comparison.";
RL FEBS Lett. 509:66-70(2001).
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; AF380138; AAL40466.1; -; Genomic_DNA.
DR RefSeq; NP_536435.1; NC_003310.1.
DR GeneID; 928906; -.
DR KEGG; vg:928906; -.
DR Proteomes; UP000101269; 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_0000395988"
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; 28640 MW; F5203CE384205BDC CRC64;
MEFDPVKINT SSIDHVTILQ YIDEPNDIRL TVCIIRNINN ITYYINITKI NPHLANRFRA
WKKRIAGRDY MTNLSRDTGI QQSKLTETIR NCQKNKNIYG LYIHYNLVIN VVIDWITDVI
VQSILRGLVN WYIANNTYTP NTPNNTTTIS ELDIIKILDK YEDMYRVSKE KECGICYEVV
YSKRLENDRY FGLLDSCNHI FCITCINIWH RTRRETGALD NCPICRTRFR KITMSKFYKL
VN