ID UBC7_CAEEL Reviewed; 164 AA. AC P34477; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 07-SEP-2016, entry version 119. DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 7; DE EC=2.3.2.23; DE AltName: Full=E2 ubiquitin-conjugating enzyme 7; DE AltName: Full=Ubiquitin carrier protein 7; DE AltName: Full=Ubiquitin-protein ligase 7; GN Name=ubc-7; ORFNames=F58A4.10; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=7906398; DOI=10.1038/368032a0; RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., RA Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., RA Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., RA Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M., RA Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., RA Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., RA Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., RA Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., RA Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., RA Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J., RA Wohldman P.; RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. RT elegans."; RL Nature 368:32-38(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX 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. {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine CC = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 CC ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE- CC ProRule:PRU00388, ECO:0000255|PROSITE-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; Z22179; CAA80166.1; -; Genomic_DNA. DR PIR; S40982; S40982. DR RefSeq; NP_499133.1; NM_066732.4. DR UniGene; Cel.18114; -. DR PDB; 1PZV; X-ray; 2.52 A; A=1-164. DR PDBsum; 1PZV; -. DR ProteinModelPortal; P34477; -. DR SMR; P34477; 4-164. DR STRING; 6239.F58A4.10.2; -. DR EPD; P34477; -. DR PaxDb; P34477; -. DR EnsemblMetazoa; F58A4.10; F58A4.10; WBGene00006704. DR GeneID; 176363; -. DR KEGG; cel:CELE_F58A4.10; -. DR UCSC; F58A4.10.1; c. elegans. DR CTD; 176363; -. DR WormBase; F58A4.10; CE00216; WBGene00006704; ubc-7. DR eggNOG; KOG0425; Eukaryota. DR eggNOG; COG5078; LUCA. DR GeneTree; ENSGT00730000110436; -. DR HOGENOM; HOG000233454; -. DR InParanoid; P34477; -. DR KO; K10575; -. DR OMA; KEWREEY; -. DR OrthoDB; EOG091G0O9F; -. DR PhylomeDB; P34477; -. DR UniPathway; UPA00143; -. DR EvolutionaryTrace; P34477; -. DR PRO; PR:P34477; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00006704; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central. DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. 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; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transferase; Ubl conjugation pathway. FT CHAIN 1 164 Probable ubiquitin-conjugating enzyme E2 FT 7. FT /FTId=PRO_0000082516. FT ACT_SITE 88 88 Glycyl thioester intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133}. FT HELIX 5 17 {ECO:0000244|PDB:1PZV}. FT STRAND 23 29 {ECO:0000244|PDB:1PZV}. FT STRAND 35 41 {ECO:0000244|PDB:1PZV}. FT STRAND 52 58 {ECO:0000244|PDB:1PZV}. FT HELIX 63 65 {ECO:0000244|PDB:1PZV}. FT STRAND 69 72 {ECO:0000244|PDB:1PZV}. FT STRAND 85 87 {ECO:0000244|PDB:1PZV}. FT HELIX 90 92 {ECO:0000244|PDB:1PZV}. FT HELIX 115 127 {ECO:0000244|PDB:1PZV}. FT HELIX 137 144 {ECO:0000244|PDB:1PZV}. FT HELIX 147 161 {ECO:0000244|PDB:1PZV}. SQ SEQUENCE 164 AA; 18939 MW; 62580D9F3F8FD968 CRC64; MEQSSLLLKK QLADMRRVPV DGFSAGLVDD NDIYKWEVLV IGPPDTLYEG GFFKAILDFP RDYPQKPPKM KFISEIWHPN IDKEGNVCIS ILHDPGDDKW GYERPEERWL PVHTVETILL SVISMLTDPN FESPANVDAA KMQRENYAEF KKKVAQCVRR SQEE //