UBC_ASFWA
ID UBC_ASFWA Reviewed; 221 AA.
AC P0C8G5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
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=War-154;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561444;
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 [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.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P25869, ECO:0000250|UniProtKB:P27949}.
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. Note=Accumulates
CC in the perinuclear cytoplasmic viral factories. Faintly detected in the
CC nucleus. {ECO:0000250|UniProtKB:P27949}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000250|UniProtKB:P25869}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C8G5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000858; 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 3: Inferred from homology;
KW ATP-binding; Early protein; Host cytoplasm; Host nucleus; Late protein;
KW Nucleotide-binding; Transferase; Ubl conjugation pathway; Virion.
FT CHAIN 1..221
FT /note="Ubiquitin-conjugating enzyme E2"
FT /id="PRO_0000355070"
FT DOMAIN 1..160
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 200..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 221 AA; 25521 MW; FB8CEABD8A1AC66D CRC64;
MVSRFLMAEY RHLIENPSEN FKISVNENDM TEWDVILRGP PDTLYEGGLF KAKVAFPPEY
PYAPPRLTFT SEMWHPNIYP DGKLCISILH GDNAEEQGMT WSPAQKIDTI LLSVISLLNE
PNPDSPANVD AAKSYRKLMH KEDLESYPME VKRTVKKSLD ECSPEDIEYF KNAVSNVPAI
PSDAYEDECE EMEDDTYILT YDDEDEEEED EEEEDEEMDD E
