ID UBC21_CAEEL Reviewed; 229 AA. AC P52484; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 2. DT 16-JUN-2009, entry version 59. DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 21; DE EC=6.3.2.19; DE AltName: Full=Ubiquitin-protein ligase 21; DE AltName: Full=Ubiquitin carrier protein 21; GN Name=ubc-21; ORFNames=C06E2.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC -!- SIMILARITY: Contains 1 UBA domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U39674; AAA80415.2; -; Genomic_DNA. DR PIR; T15432; T15432. DR RefSeq; NP_509502.2; -. DR UniGene; Cel.25724; -. DR HSSP; P21734; 1FZY. DR Ensembl; C06E2.3; Caenorhabditis elegans. DR GeneID; 182321; -. DR KEGG; cel:C06E2.3; -. DR WormBase; WBGene00006716; ubc-21. DR WormPep; C06E2.3; CE40013. DR OMA; P52484; CKEVANA. DR BRENDA; 6.3.2.19; 672. DR NextBio; 917164; -. DR ArrayExpress; P52484; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC. DR GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW. DR GO; GO:0043687; P:post-translational protein modification; IEA:InterPro. DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro. DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk. DR InterPro; IPR016135; UBQ-conjugat/RWD-like. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS50030; UBA; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 2: Evidence at transcript level; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Ubl conjugation pathway. FT CHAIN 1 229 Probable ubiquitin-conjugating enzyme E2 FT 21. FT /FTId=PRO_0000082518. FT DOMAIN 187 229 UBA. FT ACT_SITE 121 121 Glycyl thioester intermediate (By FT similarity). SQ SEQUENCE 229 AA; 26065 MW; 7FBE05784F66386C CRC64; MSVSKLNKMQ FSDKMSNLAL ARVTRKCKEV ANASDITEAG IHVEIKENNL MDIKGFIKGP EGTPYAGGTF EIKVDIPEHY PFEPPKVTEI IFHIRAFEYI QAKFVTRIWH PNISSQTGTI CLDILKDKWT ASLTLRTVLL SLQAMLCSPE PSDPQDAVVA KQFINNYPMF TATAVYWTSY FANSKKDVEP DFNRKVGRLI EMGIRETEAI VYLSCNNWKL EQALQFIFD //