ID A0A420Y1F0_9PEZI Unreviewed; 632 AA.
AC A0A420Y1F0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN Name=BRE1_1 {ECO:0000313|EMBL:RKU41752.1};
GN ORFNames=DL546_001743 {ECO:0000313|EMBL:RKU41752.1};
OS Coniochaeta pulveracea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU41752.1, ECO:0000313|Proteomes:UP000275385};
RN [1] {ECO:0000313|EMBL:RKU41752.1, ECO:0000313|Proteomes:UP000275385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAB683 {ECO:0000313|EMBL:RKU41752.1,
RC ECO:0000313|Proteomes:UP000275385};
RA Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL Submitted (AUG-2018) 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|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:RKU41752.1}.
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DR EMBL; QVQW01000068; RKU41752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420Y1F0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000275385; 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:UP000275385};
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 173..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..28
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 121..155
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 205..309
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 466..581
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 173..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 71352 MW; 9328465483C3837E CRC64;
MLEYKREKNN LEARLQELEN KADDHDEHIR IIDAWWLQLL QEVEILVDGA VSSTSTSPDT
PFPTSLDFKD VRDFQKHFSE VGKALKSRID ALVKRLASAG GQVKHDTAEL EAQLKSSLAS
EKEYMIKCAK LKDDKEKLQE KLSSEILRAV KAERKLDRAK SSAVTKLENQ ALANAGVPTK
TEQNGSSGEH SGDFDALQLK YQEAIAAVTK QKEQLSAALA EAKSLQEDNS TLRSQKGTIS
DEEYARSDVF KQFRAQNEDL IRRINNLEAT NRQLRQEAEQ LQAERTSFRD QLEREAQAVT
VDLEDQVQAK EGDLTRVRSA RDELFAENTS LKQMTAKEKN ALEHLTELVS ATSDRVQQLE
LELERLRPGE DTTMSESRED LEALALQELK EKYLKLERDF DSINKEMPLL EKSYKKTMAL
ASKKVMDFTA LEERVALLLA EKSKADQKYF AARKDADVRN GEIRSLRVAN NKSSEIIAQL
KDAELQSRVL ISNLEKQLVD LKQANSKLVA ENKKLEAAST EAMRQANSVT GRITELTNLV
KSRDAEAHHL KTKAMEQETE VEKYKARIDH ITKDRDNWKA KSMSNSSSEE DMLRVSLPTV
SSCIRGFGPV TDIVCRTLSF ARFAASTSKT PS
//
