ID   A0A1D6GUP7_MAIZE        Unreviewed;       777 AA.
AC   A0A1D6GUP7;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=ZEAMMB73_Zm00001d014640 {ECO:0000313|EMBL:AQK66696.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK66696.1};
RN   [1] {ECO:0000313|EMBL:AQK66696.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK66696.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; CM000781; AQK66696.1; -; Genomic_DNA.
DR   EMBL; CM000781; AQK66708.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6GUP7; -.
DR   UniPathway; UPA00143; -.
DR   ExpressionAtlas; A0A1D6GUP7; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
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   SUPFAM; SSF57997; Tropomyosin; 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   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          725..763
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          188..222
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          315..342
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   777 AA;  88890 MW;  4B201804B7DAD71C CRC64;
     MCLIFSFYPS YTCTSYFSDG ICFHLETDFL NGLLEAGATE SSGSPNCQLG NDVSSEQSTT
     IDILQKLFLP SSGPWHVNNE FVSAALMKLP ENEHSRQLHN ATSDVLSKLH VVMRTVDNLH
     LKHRQLAANY QKQRDSSAWN RAEQKRLKEE LTSVVAKLEG SKQKLAVLKA QGDNKQATPI
     LVPTLGNKNM TAEKVRDKQT ELQDLEATHK ELMELISKRL EEIRRLHTER IEILNKLATF
     QNILTDFKSI HSSKAFQLVN DQLQKSQAEL DDHQTLLEKL QVEMDTFVWR ERQFNQKVDL
     AEIPQKVSAY CVSRIADLEK DVQKLCNEKN MLVLKLEEAS REPGRNQVIS EFKALVSSLP
     REMGAVQSEL SKHKDASLQL HSLRAEVHSL SSIQTRKEQE IEEMSFRSAH AGSDISQLQS
     LVRELRENTQ ELKLFVELYK HESTDSRQLM ESRDRELAEW ARVHILKYSL SESKLEQRVI
     SANEAEAISQ QRLATAEAEI AELGQKLETS RRDLVKQSDI LKSKHEECEA YVVEIESIGH
     AYEDIMSQNQ QLLQQIIERD DHNTKLFMEG VKSKQSHDAL HLEVRSLQRN LQHASTLMDL
     CNQKTIRLED QLRGWSERLR RLSEDGMQQS ISLGNYQKKL SGMHGEAPKL RQSMDVLQAK
     AGSNRLEIAE LLIELENERF GKKRLEDDLD LMSSKANSLR EKTDNSAVLQ KLLHEAKEYR
     GILKCGICHD RQKEVVIAKC YHLFCSQCIQ KPLGSRQKRC PSCGLSFGVN DVKPIYI
//