ID   UBC7_WHEAT              Reviewed;         168 AA.
AC   P25868;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 7;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 7;
DE   AltName: Full=Ubiquitin carrier protein 7;
DE   AltName: Full=Ubiquitin-protein ligase 7;
GN   Name=UBC7;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Augusta;
RX   PubMed=1658801; DOI=10.1073/pnas.88.22.10297;
RA   van Nocker S., Vierstra R.D.;
RT   "Cloning and characterization of a 20-kDa ubiquitin carrier protein from
RT   wheat that catalyzes multiubiquitin chain formation in vitro.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10297-10301(1991).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins so as to signal them for selective protein degradation.
CC       Involved in the formation of multiubiquitin chains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:1658801}.
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; M74077; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A41547; A41547.
DR   AlphaFoldDB; P25868; -.
DR   SMR; P25868; -.
DR   STRING; 4565.P25868; -.
DR   PaxDb; 4565-Traes_3B_6707B51E1-1; -.
DR   eggNOG; KOG0425; Eukaryota.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P25868; baseline and differential.
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: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:SF3; UBIQUITIN-CONJUGATING ENZYME E2 G1; 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   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..168
FT                   /note="Ubiquitin-conjugating enzyme E2 7"
FT                   /id="PRO_0000082585"
FT   DOMAIN          6..166
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        92
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   168 AA;  18897 MW;  6ED5127DCAB415E2 CRC64;
     MATAPARRAS SSRSSSEISR TTPSMGFQLG FVDDSNVFEW QVTIIGPPET LYDGGYFNAI
     MSFPQNYPNS PPTVRFTSEM WHPNVYPDGR VCISIHPPGD DPNGYELASE RWTPVHTVES
     IVLSIISMLS SPNDESPANI EAAKDWREKQ DEFKKKVRRA VRKSQEML
//