ID H0EJX1_GLAL7 Unreviewed; 627 AA.
AC H0EJX1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, 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=M7I_2855 {ECO:0000313|EMBL:EHL01162.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL01162.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHL01162.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family.
CC {ECO:0000256|RuleBase:RU365038}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHL01162.1}.
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DR EMBL; AGUE01000060; EHL01162.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EJX1; -.
DR HOGENOM; CLU_019713_2_0_1; -.
DR InParanoid; H0EJX1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005446; Unassembled WGS sequence.
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 InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF08647; BRE1; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|RuleBase:RU365038, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|RuleBase:RU365038};
KW Nucleus {ECO:0000256|RuleBase:RU365038};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|RuleBase:RU365038}.
FT REGION 114..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..99
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 142..169
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 198..268
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 328..355
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 433..523
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 627 AA; 70982 MW; 3229A15BFF308F10 CRC64;
MVERSGGSED FQSHLASKAK EIKAKLQAIF TNLTSVRGIP SSDVHDLQAK LTKLLSAQKE
YMVKVDRLRV EKEELGERLE TASLRYIKAE KRLDRAKSSA VAKLEQQAIA NSSGTGIGSA
VNGDTEMTNG MSEDSKASQT AYEEASAVVA KQKEQLEAIA AENKSLTEQF TVATIRLSNL
TEDDYARTEL FKQFRVQHED VIRRINHLEA TNLQLQKEAE KYQAERTAYR AQIENESEIV
TGELESQLAR MDADLTRIRS ARDELTAEIG VQKASQEHDQ AAKEHLKQLV AAKDGQISAL
ELETERLKTQ IKESCDPTLR PDIDSLDLTQ LRQKYEALAQ EYESLNKEMP ALQTAYKRVQ
ALSTKRVMDF TAMEERISIL QVEKSKADQK YFAARKDMDT RILEVRSLRA QNSKSSEIIT
QLKDVETSNR ALLSNLEKQL SDMRQANTSI TAENKKMETT SRDATSKLDT LKNQVAELSA
LLKSKDAANA STKQKAYALE TELEQLRVKY EHAQKERDTW KTKSLSNQSG EEEMLRNYYL
QEVVVSDFHL YCPPDTQLPL QLPFQTRIPV ANSHYFSNSH TYFSSPDTEV EDPTHHHQDL
HLQAHHPILH PRNQVVVSLP VALHEVP
//
