ID UBC_ASFB7 Reviewed; 215 AA. AC P27949; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 08-NOV-2023, entry version 110. DE RecName: Full=Ubiquitin-conjugating enzyme E2; DE EC=2.3.2.23 {ECO:0000269|PubMed:29472632}; DE AltName: Full=E2 ubiquitin-conjugating enzyme; DE AltName: Full=UBCv1 {ECO:0000303|PubMed:33384682}; DE AltName: Full=Ubiquitin carrier protein; DE AltName: Full=Ubiquitin-protein ligase; DE AltName: Full=pI215L {ECO:0000303|PubMed:29472632}; GN Name=UBC; OrderedLocusNames=BA71V-144; ORFNames=I215L; OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) OS (ASFV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Asfuvirales; Asfarviridae; Asfivirus; African swine fever virus. OX NCBI_TaxID=10498; OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RX PubMed=1309282; DOI=10.1016/0042-6822(92)90059-x; RA Rodriguez J.M., Salas M.L., Vinuela E.; RT "Genes homologous to ubiquitin-conjugating proteins and eukaryotic RT transcription factor SII in African swine fever virus."; RL Virology 186:40-52(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11831707; DOI=10.1006/viro.1995.1149; RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C., RA Rodriguez J.F., Vinuela E.; RT "Analysis of the complete nucleotide sequence of African swine fever RT virus."; RL Virology 208:249-278(1995). RN [3] RP 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). RN [4] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, COFACTOR, RP MUTAGENESIS OF CYS-85; CYS-162 AND CYS-189, INDUCTION, DISRUPTION RP PHENOTYPE, CATALYTIC ACTIVITY, AND ACTIVE SITE. RX PubMed=29472632; DOI=10.1038/s41598-018-21872-2; RA Freitas F.B., Frouco G., Martins C., Ferreira F.; RT "African swine fever virus encodes for an E2-ubiquitin conjugating enzyme RT that is mono- and di-ubiquitinated and required for viral replication RT cycle."; RL Sci. Rep. 8:3471-3471(2018). RN [5] RP INDUCTION. RX PubMed=32075923; DOI=10.1128/jvi.00119-20; RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J., RA Dixon L., Werner F.; RT "The African Swine Fever Virus Transcriptome."; RL J. Virol. 94:0-0(2020). RN [6] RP FUNCTION, INTERACTION WITH HOST RPS23, INTERACTION WITH HOST EIF4E, RP INTERACTION WITH HOST CUL4B, AND INDUCTION. RX PubMed=33384682; DOI=10.3389/fmicb.2020.622907; RA Barrado-Gil L., Del Puerto A., Munoz-Moreno R., Galindo I., RA Cuesta-Geijo M.A., Urquiza J., Nistal-Villan E., Maluquer de Motes C., RA Alonso C.; RT "African Swine Fever Virus Ubiquitin-Conjugating Enzyme Interacts With Host RT Translation Machinery to Regulate the Host Protein Synthesis."; RL Front. Microbiol. 11:622907-622907(2020). RN [7] RP FUNCTION, AND MUTAGENESIS OF CYS-85. RX PubMed=34204411; DOI=10.3390/v13061160; RA Barrado-Gil L., Del Puerto A., Galindo I., Cuesta-Geijo M.A., RA Garcia-Dorival I., de Motes C.M., Alonso C.; RT "African Swine Fever Virus Ubiquitin-Conjugating Enzyme Is an RT Immunomodulator Targeting NF-kappaB Activation."; RL Viruses 13:0-0(2021). RN [8] RP FUNCTION, INTERACTION WITH HOST RNF138, AND MUTAGENESIS OF CYS-85. RX PubMed=34759016; DOI=10.4049/jimmunol.2100320; RA Huang L., Xu W., Liu H., Xue M., Liu X., Zhang K., Hu L., Li J., Liu X., RA Xiang Z., Zheng J., Li C., Chen W., Bu Z., Xiong T., Weng C.; RT "African Swine Fever Virus pI215L Negatively Regulates cGAS-STING Signaling RT Pathway through Recruiting RNF138 to Inhibit K63-Linked Ubiquitination of RT TBK1."; RL J. Immunol. 207:2754-2769(2021). CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its CC covalent attachment to other proteins (PubMed:29472632). Performs the CC second step in the ubiquitination reaction that targets specifically a CC protein for degradation via the proteasome (PubMed:29472632). 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 (PubMed:29472632). May be implicated in the shutoff of CC protein synthesis through its interactions with components of the host CC translation machinery (PubMed:33384682). Blocks host RELA nuclear CC translocation upon cytokine stimulation, thereby impairing NF-kappa-B CC signaling (PubMed:34204411). Inhibits type I IFN production and 'Lys- CC 63'-linked polyubiquitination of host TBK1 through binding to host CC RNF138. This binding enhances the interaction between RNF138 and RNF128 CC and promotes RNF138-mediated degradation of RNF128 (PubMed:34759016). CC Also inhibits the activation of AP-1 transcription factor CC (PubMed:34204411). Monoubiquitinates the viral protein P15/PIG1 in CC vitro (PubMed:7853518). {ECO:0000269|PubMed:29472632, CC ECO:0000269|PubMed:33384682, ECO:0000269|PubMed:34204411, CC ECO:0000269|PubMed:34759016, 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:0000269|PubMed:29472632}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:29472632}; CC Note=Binds Mn2+ ion which is required for highest activity. Can also CC utilize Mg2+ ions. {ECO:0000269|PubMed:29472632}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:29472632}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. CC {ECO:0000269|PubMed:29472632}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:29472632}. CC -!- SUBUNIT: Interacts with host 40S ribosomal protein RPS23 CC (PubMed:33384682). Interacts with host translation initiation factor CC EIF4E (PubMed:33384682). Interacts with host E3 ubiquitin ligase CUL4B CC (PubMed:33384682). Interacts with host RNF138 (PubMed:34759016). CC {ECO:0000269|PubMed:33384682, ECO:0000269|PubMed:34759016}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:29472632}. CC Host nucleus {ECO:0000269|PubMed:29472632}. Virion CC {ECO:0000250|UniProtKB:P25869}. Note=Accumulates in the perinuclear CC cytoplasmic viral factories. Faintly detected in the nucleus. CC {ECO:0000269|PubMed:29472632}. CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle CC (PubMed:29472632, PubMed:32075923, PubMed:33384682). Detected at 2-4 CC hpi onwards, recruited to viral factories from 8 hpi and expressed CC until 24 hpi, increasing its concentration throughout the infection CC with a maximum at 16 hpi (PubMed:29472632, PubMed:33384682). CC {ECO:0000269|PubMed:29472632, ECO:0000269|PubMed:32075923, CC ECO:0000269|PubMed:33384682}. CC -!- DISRUPTION PHENOTYPE: Knockdown impairs viral infection, with lower CC number of synthesized viral genomes and lower viral progeny. CC {ECO:0000269|PubMed:29472632}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. 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; M77121; AAA42704.1; -; Genomic_DNA. DR EMBL; U18466; AAA65370.1; -; Genomic_DNA. DR PIR; F39448; UQXFAS. DR RefSeq; NP_042834.1; NC_001659.2. DR SMR; P27949; -. DR GeneID; 22220370; -. DR KEGG; vg:22220370; -. DR UniPathway; UPA00143; -. DR Proteomes; UP000000624; Segment. 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:0044423; C:virion component; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW. DR CDD; cd00195; UBCc; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR PANTHER; PTHR24067:SF3; UBIQUITIN-CONJUGATING ENZYME E2 G1; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS00183; UBC_1; 1. DR PROSITE; PS50127; UBC_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Early protein; Host cytoplasm; Host nucleus; KW Host-virus interaction; Inhibition of host NF-kappa-B by virus; KW Late protein; Nucleotide-binding; Reference proteome; Transferase; KW Ubl conjugation pathway; Virion. FT CHAIN 1..215 FT /note="Ubiquitin-conjugating enzyme E2" FT /id="PRO_0000082591" 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, FT ECO:0000255|PROSITE-ProRule:PRU10133, FT ECO:0000269|PubMed:29472632" FT MUTAGEN 85 FT /note="C->A: Complete loss of thioester bond with FT ubiquitin. No effect on the NF-kappa-B and iNF inhibitory FT function." FT /evidence="ECO:0000269|PubMed:29472632, FT ECO:0000269|PubMed:34204411, ECO:0000269|PubMed:34759016" FT MUTAGEN 162 FT /note="C->A: No effet on the formation of the thioester FT bond with ubiquitin." FT /evidence="ECO:0000269|PubMed:29472632" FT MUTAGEN 189 FT /note="C->A: No effet on the formation of the thioester FT bond with ubiquitin." FT /evidence="ECO:0000269|PubMed:29472632" SQ SEQUENCE 215 AA; 24737 MW; 3488BEC687E67727 CRC64; MVSRFLIAEY RHLIENPSEN FKISVNENNI TEWDVILRGP PDTLYEGGLF KAKVAFPPEY PYAPPKLTFT SEMWHPNIYP DGRLCISILH GDNAEEQGMT WSPAQKIDTI LLSVISLLNE PNPDSPANVD AAKSYRKYVY KEDLESYPME VKKTVKKSLD ECSPEDIEYF KNAASNVPPI PSDAYEDECE EMEDDTYILT YDDDEEEEDE EMDDE //