ID   UBE2S_LITCT             Reviewed;         211 AA.
AC   C1C3R6;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 40.
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;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Helbing C.C., Veldhoen N., Leong J., Koop B.F.;
RT   "Rana catesbeiana ESTs and full-length cDNAs.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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       'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme
CC       ube2c/ubch10 on APC/C substrates, enhancing 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: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; BT081495; ACO51626.1; -; mRNA.
DR   AlphaFoldDB; C1C3R6; -.
DR   SMR; C1C3R6; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
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   GO; GO:0010994; P:free ubiquitin chain polymerization; ISS:UniProtKB.
DR   GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; 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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Nucleotide-binding; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..211
FT                   /note="Ubiquitin-conjugating enzyme E2 S"
FT                   /id="PRO_0000390430"
FT   DOMAIN          11..157
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          157..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   211 AA;  23252 MW;  334EE1DC6CB0827F CRC64;
     MNSNVENLPP HVIRQVYKEV STLTPDPPEG IKIIPNEEDI TDVQVSIEGP EGTPYAGGIF
     RMKLILGKDF PAAPPKGYFL TKIFHPNVSS NGEICVNVLK KDWKAELGIR HVLLTIKCLL
     IHPNPESALN EEAGRLLLEN YEEYASRARL MTEIHAHSSS LRGKDPTDPC SSASVTGALG
     DGPMAKKHAG DRDKKLAAKK KTDKKRALRR L