ID K4A5U0_SETIT Unreviewed; 843 AA.
AC K4A5U0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN Name=101767187 {ECO:0000313|EnsemblPlants:KQK90442};
GN ORFNames=SETIT_9G367100v2 {ECO:0000313|EMBL:RCV44359.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV44359.1};
RN [1] {ECO:0000313|EMBL:RCV44359.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK90442,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV44359.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV44359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV44359.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK90442}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK90442};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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}.
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DR EMBL; AGNK02005935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003536; RCV44358.1; -; Genomic_DNA.
DR EMBL; CM003536; RCV44359.1; -; Genomic_DNA.
DR RefSeq; XP_004984043.1; XM_004983986.1.
DR AlphaFoldDB; K4A5U0; -.
DR STRING; 4555.K4A5U0; -.
DR EnsemblPlants; KQK90442; KQK90442; SETIT_034244mg.
DR GeneID; 101767187; -.
DR Gramene; KQK90442; KQK90442; SETIT_034244mg.
DR KEGG; sita:101767187; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR InParanoid; K4A5U0; -.
DR OMA; YSNIDTR; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000004995; Chromosome IX.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:EnsemblPlants.
DR GO; GO:0009965; P:leaf morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
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; IPR018247; EF_Hand_1_Ca_BS.
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:SF7; E3 UBIQUITIN-PROTEIN LIGASE BRE1-LIKE 2; 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; PS00018; EF_HAND_1; 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:UP000004995};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 791..829
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 3..37
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 209..239
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 323..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 475..509
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 553..594
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 728..788
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 843 AA; 96232 MW; 019947CAE06322BF CRC64;
MDSAALQYEN QKLLQQLEAQ KSEMHALEVK FKELKDEQCS YDKTLISLNK MWNQLIDDLV
LLGVRVGGDL GNLQALDHEE LSEESFESCP SEEIFLLRLL KSSSFKNNKD NSLLEFVEEA
LACHHLATVT LMKSLQEAIS SHQARSESLT LALNGQKSNE DVLIALQHHN DHLKEVVENA
SQAVSIINEK HKRYLDEIET FKSNHSKELQ EIKRISGELE ESMAELEESR RKLVVLQLQK
HGSVMDASGV NAVNGGISTD KSSDQSMSWQ DLKDAVDAAK TLAGNRLLEL HQTQEDNLIL
SKELGDLEGQ LKDENYVLAS KPYAILNDQL QHLNAEIERY RGLVEVLQND KDQLMQKDKE
ICAKAESFDS IKQTITIYET KIEELENQIK IFMSEKNDLE TKVEEALQDS GKKDFKNEIH
VMAAALSNEL RMMENQLSRS KDAASEALAL REKAESLTSL VAKKIEEQKE ISDKYNSQLI
EIKSLKALVE ELEKEKQELQ FIADMYTKEC SESRTIADIE ESENRAHSQV EYLRSSLEEH
SLELRVKAAS EAEAACQQRL SFAEAELEEL RAKVDASERD VVELKEAIRI KEAEGDAYIS
DIETIGQAYE DMQTQNQHLL EQLADREDFN IKLVSDSVKM KQACSSLFSE KLMLEKQLQQ
VNTSLESSKL KISRGEEQMK TCVAQAIKTS AENRHLTISL ERTALDMSNT EKELKWLRSS
VGSSEKEHDQ TQQKISELRI LLEHERSERR RLEEQYEEVK NEIMELTSET EETTIQKLQD
EIKECKAILK CGVCFDRPKE VVITKCFHLF CSPCIQRNLE IRHRKCPGCG TPFGQNDVRE
VKI
//
