ID   UBC_ASFM2               Reviewed;         213 AA.
AC   P25869;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2;
DE            EC=2.3.2.23 {ECO:0000250|UniProtKB:P27949};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme;
DE   AltName: Full=UBCv1 {ECO:0000250|UniProtKB:P27949};
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
DE   AltName: Full=pI215L {ECO:0000250|UniProtKB:P27949};
GN   Name=UBC; OrderedLocusNames=Mal-151;
OS   African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10500;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1310934; DOI=10.1002/j.1460-2075.1992.tb05058.x;
RA   Hingamp P.M., Arnold J.E., Mayer R.J., Dixon L.K.;
RT   "A ubiquitin conjugating enzyme encoded by African swine fever virus.";
RL   EMBO J. 11:361-366(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
RX   PubMed=7853518; DOI=10.1128/jvi.69.3.1785-1793.1995;
RA   Hingamp P.M., Leyland M.L., Webb J., Twigger S., Mayer R.J., Dixon L.K.;
RT   "Characterization of a ubiquitinated protein which is externally located in
RT   African swine fever virions.";
RL   J. Virol. 69:1785-1793(1995).
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins (By similarity). Performs the
CC       second step in the ubiquitination reaction that targets specifically a
CC       protein for degradation via the proteasome (By similarity). By
CC       controlling the ubiquitination status of specific host proteins, the
CC       virus may target them to degradation and thereby optimize the viral
CC       replication (By similarity). May be implicated in the shutoff of
CC       protein synthesis through its interactions with components of the host
CC       translation machinery (By similarity). Blocks p65 nuclear translocation
CC       upon cytokine stimulation, thereby impairing NF-kappa-B signaling (By
CC       similarity). Inhibits type I IFN production and 'Lys-63'-linked
CC       polyubiquitination of host TBK1 through binding to host RNF138. This
CC       binding enhances the interaction between RNF138 and RNF128 and promotes
CC       RNF138-mediated degradation of RNF128. Also inhibits the activation of
CC       AP-1 transcription factor (By similarity). Monoubiquitinates the viral
CC       protein P15/PIG1 in vitro (PubMed:7853518).
CC       {ECO:0000250|UniProtKB:P27949, ECO:0000269|PubMed:7853518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000250|UniProtKB:P27949};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P27949};
CC       Note=Binds Mn2+ ion which is required for highest activity. Can also
CC       utilize Mg2+ ions. {ECO:0000250|UniProtKB:P27949};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:P27949, ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with host 40S ribosomal protein RPS23 (By
CC       similarity). Interacts with host translation initiation factor EIF4E
CC       (By similarity). Interacts with host E3 ubiquitin ligase CUL4B (By
CC       similarity). Interacts with host RNF138 (By similarity).
CC       {ECO:0000250|UniProtKB:P27949}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P27949}.
CC       Host nucleus {ECO:0000250|UniProtKB:P27949}. Virion
CC       {ECO:0000269|PubMed:7853518}. Note=Accumulates in the perinuclear
CC       cytoplasmic viral factories. Faintly detected in the nucleus.
CC       {ECO:0000250|UniProtKB:P27949}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000305|PubMed:7853518}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; X62440; CAA44305.1; -; Genomic_DNA.
DR   EMBL; X71982; CAA50851.1; -; Genomic_DNA.
DR   EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S19158; S19158.
DR   SMR; P25869; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000860; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Early protein; Host cytoplasm; Host nucleus; Late protein;
KW   Nucleotide-binding; Transferase; Ubl conjugation pathway; Virion.
FT   CHAIN           1..213
FT                   /note="Ubiquitin-conjugating enzyme E2"
FT                   /id="PRO_0000082592"
FT   DOMAIN          1..160
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   213 AA;  24468 MW;  F9671BC7385D6DCE CRC64;
     MVSSFLLAEY KNLIVNPSEH FKISVNEDNL TEWDVILKGP PDTLYEGGLF KAKIVFPPKY
     PYEPPRLTFT SEMWHPNIYS DGKLCISILH GDNAEEQGMT WSPAQKIDTV LLSVISLLNE
     PNPDSPANVD AAKSYRKYLY KEDLESYPME VKKTVKKSLD ECSAEDIEYF KNVPVNVLPV
     PSDDYEDEEM EDGTYILTYD DEDEEEDEEM DDE