ID   UBE2C_DICDI             Reviewed;         153 AA.
AC   Q54XS6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Probable ubiquitin-conjugating enzyme E2 C;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme C;
DE   AltName: Full=Ubiquitin carrier protein C;
DE   AltName: Full=Ubiquitin-protein ligase C;
GN   Name=ube2c; Synonyms=ubch10; ORFNames=DDB_G0278775;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Acts as an essential factor of the anaphase promoting
CC       complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that
CC       controls progression through mitosis. Acts by initiating polyubiquitin
CC       chains on APC/C substrates, leading to the degradation of APC/C
CC       substrates by the proteasome and promoting mitotic exit.
CC       {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:0000250|UniProtKB:O00762, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Component of the APC/C complex.
CC       {ECO:0000250|UniProtKB:O00762}.
CC   -!- PTM: Autoubiquitinated by the APC/C complex, leading to its degradation
CC       by the proteasome. {ECO:0000250|UniProtKB:O00762}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AAFI02000024; EAL67989.1; -; Genomic_DNA.
DR   RefSeq; XP_641954.1; XM_636862.1.
DR   AlphaFoldDB; Q54XS6; -.
DR   SMR; Q54XS6; -.
DR   STRING; 44689.DDB0304925; -.
DR   PaxDb; Q54XS6; -.
DR   EnsemblProtists; EAL67989; EAL67989; DDB_G0278775.
DR   GeneID; 8621686; -.
DR   KEGG; ddi:DDB_G0278775; -.
DR   dictyBase; DDB_G0278775; ube2c.
DR   eggNOG; KOG0421; Eukaryota.
DR   HOGENOM; CLU_030988_9_0_1; -.
DR   InParanoid; Q54XS6; -.
DR   OMA; HPNVDMS; -.
DR   PhylomeDB; Q54XS6; -.
DR   Reactome; R-DDI-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-DDI-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DDI-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-DDI-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-DDI-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-DDI-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-DDI-176412; Phosphorylation of the APC/C.
DR   Reactome; R-DDI-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DDI-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DDI-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q54XS6; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; 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   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..153
FT                   /note="Probable ubiquitin-conjugating enzyme E2 C"
FT                   /id="PRO_0000328509"
FT   DOMAIN          6..153
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        90
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   153 AA;  17473 MW;  4ACE8F6E07C6E6C9 CRC64;
     MSQDHSVSKR LQSELMNLMM GPSPGISAFP DGDNIFNWIG TIQGAKDTVY EQMEFKMSLK
     FPTDYPYKPP TVKFETQCFH PNVDNNGNIC LDILKDKWSP VYNVRSLLIS IQSLLGEPNN
     ESPLNSYAAS LWSNQDEYKK VLDKRYQEAT SRP