UBC7_CAEEL
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 03-AUG-2022, entry version 145.
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 Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC 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., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., 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 investigating
RT 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:
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}.
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DR EMBL; Z22179; CAA80166.1; -; Genomic_DNA.
DR PIR; S40982; S40982.
DR RefSeq; NP_499133.1; NM_066732.4.
DR PDB; 1PZV; X-ray; 2.52 A; A=1-164.
DR PDBsum; 1PZV; -.
DR AlphaFoldDB; P34477; -.
DR SMR; P34477; -.
DR BioGRID; 41558; 4.
DR STRING; 6239.F58A4.10; -.
DR EPD; P34477; -.
DR PaxDb; P34477; -.
DR PeptideAtlas; P34477; -.
DR EnsemblMetazoa; F58A4.10.1; F58A4.10.1; 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 GeneTree; ENSGT00940000155228; -.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; P34477; -.
DR OMA; RKVTRCV; -.
DR OrthoDB; 1317014at2759; -.
DR PhylomeDB; P34477; -.
DR Reactome; R-CEL-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P34477; -.
DR PRO; PR:P34477; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006704; Expressed in embryo and 4 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; 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 CDD; cd00195; UBCc; 1.
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; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..164
FT /note="Probable ubiquitin-conjugating enzyme E2 7"
FT /id="PRO_0000082516"
FT DOMAIN 3..163
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"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:1PZV"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1PZV"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1PZV"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1PZV"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1PZV"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1PZV"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1PZV"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1PZV"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:1PZV"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:1PZV"
FT HELIX 147..161
FT /evidence="ECO:0007829|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
