ID UBC7_CAEEL STANDARD; PRT; 164 AA. AC P34477; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE PROBABLE UBIQUITIN-CONJUGATING ENZYME E2-19 KDA (EC 6.3.2.19) DE (UBIQUITIN-PROTEIN LIGASE) (UBIQUITIN CARRIER PROTEIN). GN F58A4.10. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RX MEDLINE; 94150718. 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 Waterson 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). CC -!- FUNCTION: CATALYZES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC PROTEINS (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC PYROPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: SECOND STEP IN UBIQUITIN CONJUGATION. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR CC UBIQUITIN-THIOLESTER FORMATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE UBIQUITIN-CONJUGATING ENZYME FAMILY. CC STRONGEST, TO YEAST UBC1. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR PIR; S40982; S40982. DR HSSP; Q02159; 2UCZ. DR WORMPEP; F58A4.10; CE00216. DR INTERPRO; IPR000608; -. DR PFAM; PF00179; UQ_con; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. KW Ubiquitin conjugation; Ligase. FT BINDING 88 88 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 164 AA; 18938 MW; 62580D9F3F8FD968 CRC64; MEQSSLLLKK QLADMRRVPV DGFSAGLVDD NDIYKWEVLV IGPPDTLYEG GFFKAILDFP RDYPQKPPKM KFISEIWHPN IDKEGNVCIS ILHDPGDDKW GYERPEERWL PVHTVETILL SVISMLTDPN FESPANVDAA KMQRENYAEF KKKVAQCVRR SQEE //