ID K4A5S6_SETIT Unreviewed; 854 AA.
AC K4A5S6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN Name=101765941 {ECO:0000313|EnsemblPlants:KQK88626};
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|EnsemblPlants:KQK88626, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EnsemblPlants:KQK88626, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK88626,
RC ECO:0000313|Proteomes:UP000004995};
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|EnsemblPlants:KQK88626}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK88626};
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; AGNK02005555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012698290.1; XM_012842836.1.
DR RefSeq; XP_012698291.1; XM_012842837.1.
DR RefSeq; XP_012698292.1; XM_012842838.1.
DR RefSeq; XP_012698293.1; XM_012842839.1.
DR RefSeq; XP_012698294.1; XM_012842840.1.
DR AlphaFoldDB; K4A5S6; -.
DR STRING; 4555.K4A5S6; -.
DR EnsemblPlants; KQK88626; KQK88626; SETIT_034230mg.
DR GeneID; 101765941; -.
DR Gramene; KQK88626; KQK88626; SETIT_034230mg.
DR KEGG; sita:101765941; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR InParanoid; K4A5S6; -.
DR OMA; AISRQWK; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000004995; Chromosome IX.
DR ExpressionAtlas; K4A5S6; baseline.
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:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
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:UP000004995};
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 802..840
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 218..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 668..702
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 854 AA; 97813 MW; B60D1875D45BADBA CRC64;
MSTCLHIQGP GKIAMSRPLD FAVLKYKNQR LAEQLEVHKF EYRTLEGRFN DLKEKQRTHN
ETLVLVKSHW ERLLADLDLV SVCKNESLHS SCGTGQNNVQ KERDFLNRLL EAGATESSGC
SPSYHLGNGV APEQSSTVNV LQKAFLPSSD LWHVNNDLVY VALTKLPENE HSRQLHSATS
NIFSKLHKVI HAIDNLHLEH RQLAGNYQKQ RDSSAWNRAE QKRLKEELTS AVAKLEESKH
KLAALKAQGD NKHGTPVLVP KLGNKDVSAE KVRDKQRELQ DLEATHKELM ELISKRLEEI
RRLHMERIEI LNKLATFQDI LTGFRNIRSS KAFELVNDQL QKSQAELDDH QTLLKKLQVD
TDSFVWQERQ FNQKVDLAEI PQKVSAYCVS RIADLEKDVL KLCNEKNMLV LKLEEASREP
GRNQVISEFK ALVSSLPREM GAVQSELSKH KDASLQLHSL RAEVSSLSSI LTRKEQEIEQ
TSCRSAHAGS DISQLQSLVL DLKENIKELK LFVELYKHES TDSRQLIEYR DRELSEWARV
HVLKYSLNES KLEQRVIAAN EAEAMSQQRL ATSEAKIAEL GQKLETSRRD LVRLSHILKS
KYEECEAYVV EIESIGNAYE DIMSQNQQLL QQIIERDDHN TKLFMEGVKA KQSHDALHLE
VSSLKRNLQH ASMLMDLYNK KIVRLEDQLR GWSERVRRLS EDGMQQSISL GNSQRKLAGL
HGEAPKLMQS MDELQAKVGS NRLEVAELLT ELEKERFSKK RIEDDLDLMS SKANSLREKK
DNSAVLQKLH HEVKEYRGIL KCGVCHERQK EIVIAKCYHL FCNQCIQKSL GSRQKRCPSC
GLSFGVNDVK PIYI
//
