ID A0A0A0L2Z2_CUCSA Unreviewed; 878 AA.
AC A0A0A0L2Z2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=Csa_3G118000 {ECO:0000313|EMBL:KGN56365.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN56365.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN56365.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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; CM002924; KGN56365.1; -; Genomic_DNA.
DR RefSeq; XP_004133777.1; XM_004133729.2.
DR RefSeq; XP_011650646.1; XM_011652344.1.
DR AlphaFoldDB; A0A0A0L2Z2; -.
DR STRING; 3659.A0A0A0L2Z2; -.
DR EnsemblPlants; KGN56365; KGN56365; Csa_3G118000.
DR GeneID; 101221425; -.
DR Gramene; KGN56365; KGN56365; Csa_3G118000.
DR KEGG; csv:101221425; -.
DR eggNOG; KOG0978; Eukaryota.
DR OMA; THIEIMT; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000029981; Chromosome 3.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:EnsemblPlants.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR GO; GO:0045087; P:innate immune response; IEA:EnsemblPlants.
DR GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:EnsemblPlants.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:EnsemblPlants.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblPlants.
DR GO; GO:0010162; P:seed dormancy process; IEA:EnsemblPlants.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR CDD; cd16499; RING-HC_Bre1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 826..865
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 137..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..74
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 252..323
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 357..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 481..536
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 587..621
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 678..726
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 769..803
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 100944 MW; 64E1A4275B219AA8 CRC64;
MGSTVESDRK RRHFSTISPT AATAKKAPFL PVSEDKKLDV AVLQYQNQKL IQKLEVQKVE
YKSLQNKYAQ LKEKQEPYDT TVAVVKNCWE ELVNGLETSS VRMRRWRSKR DGEHTIAGVD
GSSSSFEDAV LSRLAETGAT QSSSTYSSSK HMEEETESPC EKTKTIERSI ETSIENLWYL
KDGLHATLLN ELPKDDSFRK RTSGDLVKEV RNMRLRVKDF LFKQKVLAQE LEKHRDLDAK
TKAELKVLKV ELGSAVAELE ESNSKLTKLR AEHDAAKKAG FPVLNLTGKH SASGKVRDKQ
KDLRDMESSL KELKDQAVDR LAELNSLHEG RLKMLRRLSD IQNTMKSVKT ISSSKPYLLL
RDRIEKLKLE VNEQQALFEK LQVEKDNIMW KEKELNIKNN ILDVLRRSST VSDTRINDLE
ILIQKQKDGK QSIENKLVEV LKEPGRKKIV SEFRALVSSF PEAMGSMQSQ LHKYKEAASD
VHSVRADLQS LSSIIDRMEK ECENLSSRSK DQQAEIQKLQ ATVQDLTEVN RELKLIIDMY
SRESTESREV LEARDLEYKA WARVQSLKSS LDERNLESRV KTANEAEAIS QQRLAAAEAE
IARLRQKLEA SKRDLTRLSD VLKSKGDENV AYLSEIETIG QAYDDMQTQN QHLLQQITER
DDYNIKLVLE GVRARQLQEI MLIEKQALEN EVQQANASLV LYEMKAARIE DQLRGCSDHI
QKIEEDKLRD TDTLENTRKR LLEIRIASQQ TRESLDECQS KVERSRTTQA ELQIELEKER
FEKKRIEEEL EVIGRKASRL EAQMESSSVI EKLHEELGEY EKIVNCKICV NSRKQVVITK
CFHLFCNPCV QDILKSQHRK CPRCSASFGP NDVKQVFF
//
