ID   UBC2_MIMIV              Reviewed;         388 AA.
AC   Q5UQ57;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   02-JUN-2021, entry version 76.
DE   RecName: Full=Probable ubiquitin-conjugating enzyme E2 L709;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme L709;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   OrderedLocusNames=MIMI_L709;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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:0000255|PROSITE-ProRule:PRU00388};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AY653733; AAV50969.1; -; Genomic_DNA.
DR   RefSeq; YP_003987237.1; NC_014649.1.
DR   SMR; Q5UQ57; -.
DR   GeneID; 9925362; -.
DR   KEGG; vg:9925362; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..388
FT                   /note="Probable ubiquitin-conjugating enzyme E2 L709"
FT                   /id="PRO_0000243981"
FT   DOMAIN          3..162
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          195..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..294
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   388 AA;  42724 MW;  9329EB6E7F020B78 CRC64;
     MQNVHKRVIK DINDGMKNLK QEFGIYLAPE EDDFYKVHFI LQGPEGTPFE GGLYHGMIRL
     NNDHPFRPPN LHMITPSGRF EAEKYPISPN SRGICTTATS FHPESWTSMN NLETVLKGFV
     SLMCDPYDGG VGAVKSTDTQ VKKLAQDSLT HIGNDLMVQK LFPDLYKAVN NGTFKPVKLA
     ELSKIVYKEP TKPIVEEKSA KTSKSSTKTS VKSKKNQKSD SEEEENSDDD NTDSDSESDD
     FRDLDDVVDD SDQESDDESD SSSESENESG GSDDESDDGS DDESDDETSE SDSESEEEKP
     VKKSTRKISK TTTKSSSTKP VKSIKSSKST TTKPTKPTKS TKTTKSTKST KSTKSTKPTE
     STKSSRSVKT TESSKSSKSS KSSKTGKK