ID UBC2_MEDSA Reviewed; 152 AA. AC P35130; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Ubiquitin-conjugating enzyme E2 2; DE EC=2.3.2.23; DE AltName: Full=E2 ubiquitin-conjugating enzyme 2; DE AltName: Full=Ubiquitin carrier protein 2; DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 2; DE AltName: Full=Ubiquitin-protein ligase 2; GN Name=UBC2; OS Medicago sativa (Alfalfa). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3879; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Excalibur; TISSUE=Cotyledon; RX PubMed=8278526; DOI=10.1104/pp.102.3.1049; RA Pramanik S.K., Bewley J.D.; RT "A ubiquitin carrier protein cDNA from developing alfalfa embryos."; RL Plant Physiol. 102:1049-1050(1993). 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, ECO:0000255|PROSITE- CC ProRule:PRU10133}; 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}. 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; L06967; AAA18528.1; -; mRNA. DR AlphaFoldDB; P35130; -. DR SMR; P35130; -. DR UniPathway; UPA00143; -. 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 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:SF301; UBIQUITIN-CONJUGATING ENZYME E2 2; 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 2: Evidence at transcript level; KW ATP-binding; Nucleotide-binding; Transferase; Ubl conjugation pathway. FT CHAIN 1..152 FT /note="Ubiquitin-conjugating enzyme E2 2" FT /id="PRO_0000082574" FT DOMAIN 4..150 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT ACT_SITE 88 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133" SQ SEQUENCE 152 AA; 17315 MW; 3951D40CF5CE8E24 CRC64; MSTPARKRLM RDFKRLQHDP PAGISGAPQD NNIMLWNAVI FGPDDTPWDG GTFKLSLQFS EDYPNKPPTV RFVSRMFHPN IYADGSICLD ILQNQWSPIY DVAAILTSIQ SLLCDPNPNS PANSEAARMF SENKREYNRR VREVVEQSWT AD //