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   04-MAR-2015, entry version 107.
DE   RecName: Full=Probable ubiquitin-conjugating enzyme E2 7;
DE            EC=6.3.2.19;
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: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine. {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}.
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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.F58A4.10.1; -.
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; COG5078; -.
DR   GeneTree; ENSGT00730000110436; -.
DR   HOGENOM; HOG000233454; -.
DR   InParanoid; P34477; -.
DR   KO; K10575; -.
DR   OMA; FGYEKPE; -.
DR   PhylomeDB; P34477; -.
DR   UniPathway; UPA00143; -.
DR   EvolutionaryTrace; P34477; -.
DR   NextBio; 892258; -.
DR   PRO; PR:P34477; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019787; F:small conjugating protein transferase activity; IBA:GO_Central.
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; Ligase;
KW   Nucleotide-binding; Reference proteome; 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
//