ID   UBE2S_DROGR             Reviewed;         208 AA.
AC   B4JKB7;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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   ORFNames=GH12079;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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 vih/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; CH916370; EDW00020.1; -; Genomic_DNA.
DR   RefSeq; XP_001991395.1; XM_001991359.1.
DR   AlphaFoldDB; B4JKB7; -.
DR   SMR; B4JKB7; -.
DR   STRING; 7222.FBpp0145985; -.
DR   EnsemblMetazoa; FBtr0147493; FBpp0145985; FBgn0119558.
DR   GeneID; 6564572; -.
DR   KEGG; dgr:6564572; -.
DR   eggNOG; KOG0423; Eukaryota.
DR   HOGENOM; CLU_030988_5_3_1; -.
DR   InParanoid; B4JKB7; -.
DR   OMA; QPAKCGA; -.
DR   OrthoDB; 1412570at2759; -.
DR   PhylomeDB; B4JKB7; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
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; Cell cycle; Cell division; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..208
FT                   /note="Ubiquitin-conjugating enzyme E2 S"
FT                   /id="PRO_0000390439"
FT   DOMAIN          14..160
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          161..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        98
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   208 AA;  23260 MW;  8FB88248BBCD1FED CRC64;
     MSSQYSNVEN LSPQTIRQVM KELQDMESTP PEGIKVLINE SDVTDIQALI DGPAGTPYAV
     GIFRVKLTLS KDFPQTPPKA YFLTKIFHPN VASNGEICVN TLKKDWKPDL GIKHILLTIK
     CLLIVPNPES ALNEEAGKML LERYDDYSQR ARMMTEIHAQ PAKCGAGASD AKDDDGPSTK
     KHAGVDKKLQ DKKKEKLLKE KKRMLKRL