UBC7_WHEAT
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 03-AUG-2022, entry version 102.
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.Traes_3B_6707B51E1.1; -.
DR PRIDE; P25868; -.
DR eggNOG; KOG0425; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P25868; baseline.
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; -; 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; 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
