ID K4BVG0_SOLLC Unreviewed; 161 AA.
AC K4BVG0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
DE Flags: Fragment;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EMBL:AQT19654.1};
RN [1] {ECO:0000313|EMBL:AQT19654.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27909045; DOI=10.1104/pp.16.01190;
RA Zhou B., Mural R.V., Chen X., Oates M.E., Connor R.A., Martin G.B.,
RA Gough J., Zeng L.;
RT "A Subset of Ubiquitin-Conjugating Enzymes Is Essential for Plant
RT Immunity.";
RL Plant Physiol. 173:1371-1390(2017).
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:0000256|ARBA:ARBA00000485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating
CC enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].;
CC EC=2.3.2.25; Evidence={ECO:0000256|ARBA:ARBA00035805};
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000256|RuleBase:RU362109}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KY246910; AQT19654.1; -; mRNA.
DR RefSeq; NP_001310969.1; NM_001324040.1.
DR AlphaFoldDB; K4BVG0; -.
DR GeneID; 101243704; -.
DR KEGG; sly:101243704; -.
DR eggNOG; KOG0427; Eukaryota.
DR HOGENOM; CLU_030988_15_1_1; -.
DR OrthoDB; 452at2759; -.
DR PhylomeDB; K4BVG0; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF373; UBIQUITIN-CONJUGATING ENZYME E2 W; 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 {ECO:0000256|RuleBase:RU362109};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU362109}.
FT DOMAIN 15..161
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT ACT_SITE 99
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AQT19654.1"
SQ SEQUENCE 161 AA; 18428 MW; 0E7C028D85BC7793 CRC64;
MTSASASSRK VLSKIACNRL QKELMEWQVN PPAGFKHKVT DNLQRWIIEV NGAPGTLYAN
EMYQLQVDFP EHYPMEAPQV VFIHPAPLHP HIYSNGHICL DILYDSWSPA MTVSSICISI
LSMLSSSTVK QRPADNDRYV KNCKNGRSPK ETRWWFHDDK V
//
