ID A0A428QE01_9HYPO Unreviewed; 718 AA.
AC A0A428QE01;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=CEP54_005222 {ECO:0000313|EMBL:RSL63449.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL63449.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL63449.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL63449.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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}.
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:RSL63449.1}.
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DR EMBL; NKCI01000039; RSL63449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428QE01; -.
DR STRING; 1325734.A0A428QE01; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000288168; 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 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; 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; PF08647; BRE1; 1.
DR Pfam; PF13920; zf-C3HC4_3; 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:UP000288168};
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 666..705
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 189..223
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 270..367
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 411..473
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 547..585
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 621..648
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 100..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 81586 MW; 109912771871D6C0 CRC64;
MEDRKRPAIS SADDLAPPSK RVAVNGSKAK DDSLEMKEES WIEAYTKGAI YRQMQEYSRK
AATYESRLEE LHKRSVHHDD HLRIIDAWWR QVLEEIELLA DSDTTSSNPS GMNPTTPHRT
SADSVAEPPY LSGVSFKDLH DFQKHLQDKG KSIKSKAESL LAHLAASRGS IDPSVSKLES
KVSGLLAAQK EYLFKLDRLS SEKDQLSEQL NAATLRYFKA EKKLDRAKSS QVQKLEQQAF
ANATRPSASG DAGAESGETN GNSGEILLKY EEATAAATKQ KEQLDAILAE IKTLQDENST
LKAKRDTLTD EDFIRTDVFK QFKNQNEDLI KRINTLEATN KQLREEAEKL QAERSAFRSQ
LEADANQVTQ ELEAEIMSRD QDLARVRSAR DELLAENTQS KARLEQERGS MEQIKELASA
KDDRITALEL ELSRLKSSED QEKFNPDDEN LTVDELRLKY RKLQQDFDSI NLELPAIEKA
YKKMKELAHR KAMDSSAMEE RMTILIAEKS KADQKYFAAR KDADTRNNEI RSLRHQNSKS
SEIIAQLKEL EMQNRTLLSN LEKQLADLKQ ANASLVTENK KAEATSLEAV RRTDSLSKQV
SDLTNLVKSK DAASAVVRER NTMQETEVEK LKVRIEHVQK DRDSWKNKAL SNSSEEEEML
RTFALCTICR NNFKNTALKT CGHLFCNQCV DDRISNRMRK CPTCSRAFDK MDVMSVHH
//
