ID   UBE2S_DICDI             Reviewed;         215 AA.
AC   Q54I43;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 S;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme S;
DE   AltName: Full=Ubiquitin carrier protein S;
DE   AltName: Full=Ubiquitin-protein ligase S;
GN   Name=ube2s; ORFNames=DDB_G0289021;
OS   Dictyostelium discoideum (Social amoeba).
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 specifically elongating
CC       polyubiquitin chains initiated by the E2 enzyme ubch10 on APC/C
CC       substrates, enhancing the degradation of APC/C substrates by the
CC       proteasome and promoting mitotic exit. {ECO:0000255|PROSITE-
CC       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; AAFI02000129; EAL62926.1; -; Genomic_DNA.
DR   RefSeq; XP_636428.1; XM_631336.1.
DR   AlphaFoldDB; Q54I43; -.
DR   SMR; Q54I43; -.
DR   STRING; 44689.Q54I43; -.
DR   PaxDb; 44689-DDB0305006; -.
DR   EnsemblProtists; EAL62926; EAL62926; DDB_G0289021.
DR   GeneID; 8626920; -.
DR   KEGG; ddi:DDB_G0289021; -.
DR   dictyBase; DDB_G0289021; ube2s.
DR   eggNOG; KOG0423; Eukaryota.
DR   HOGENOM; CLU_030988_5_3_1; -.
DR   InParanoid; Q54I43; -.
DR   OMA; QPAKCGA; -.
DR   PhylomeDB; Q54I43; -.
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:Q54I43; -.
DR   Proteomes; UP000002195; Chromosome 5.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF154; UBIQUITIN-CONJUGATING ENZYME E2 G2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..215
FT                   /note="Ubiquitin-conjugating enzyme E2 S"
FT                   /id="PRO_0000327752"
FT   DOMAIN          9..155
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          159..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        93
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   215 AA;  23617 MW;  8D79DBBEBAD4519C CRC64;
     MSSENLPPDV IKRVVKELKE LNSSTLEGIT LLPCEEDITN IEAVVTGPAG TPYEGGYFKA
     RLILSSDFPR SPPKANFITK IFHPNVSKKG EICVNTLKKD WTEDLGLKHI LLTIKCLLIV
     PNAESSLNED ASRLLLENYD DYCKHAKLFT SIHASKPIID SNNNNENSTT TPTTTTTATT
     PSTNTASISS PVKKKTETTN STTTKVQPKK SLKRL
//