UBC_ASFB7
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 03-AUG-2022, entry version 105.
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.
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}.
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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; 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 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; -; 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 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
