ID A0A0M9VQA0_9BASI Unreviewed; 750 AA.
AC A0A0M9VQA0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=Malapachy_2461 {ECO:0000313|EMBL:KOS15313.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15313.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS15313.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15313.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-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}.
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:KOS15313.1}.
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DR EMBL; LGAV01000002; KOS15313.1; -; Genomic_DNA.
DR RefSeq; XP_017992945.1; XM_018136950.1.
DR AlphaFoldDB; A0A0M9VQA0; -.
DR STRING; 77020.A0A0M9VQA0; -.
DR GeneID; 28728825; -.
DR VEuPathDB; FungiDB:Malapachy_2461; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000037751; 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; 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; PF08647; BRE1; 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:UP000037751};
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 697..735
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 202..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..74
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 439..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 202..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 84166 MW; 28D115B060640E25 CRC64;
MERKRDHVEV AAGHEAAGAA TKRLHLDLMA GEEETNPDYQ RLEQYRKEAI YRRMREAQRD
AKRTKDEAVA LQGTLVRTQQ QVLAVNQFWD ALAEYMAHYQ VDERALGEDT LKRMERIVPL
TLLQGSNEQI AALQERQSLL QHIVAVLAKS AAGSGSSISQ PALQEVQDRC ASLAGEVSAL
RQALEATKAQ LHLSQERVET LEEQLRQAER RADRAQSDVV RNMEDPKHEK QAQASAQPAS
NQGTPTPTPA DHKESAQGSE SHAEAAQGTM AATAEKAAAM EEELSSLRDV AHSRQRLLDE
ARAELLEAKQ SVAALQLQMQ AVPDERVHAH SVYQALQAEM VFMQQEAERL RSAHAALEQE
NNDMREFRFE FQRQTTTQAQ THSEELQKQI KARDADIVRL RGQRDELNAE LLERRARESV
RFTYVDEAKA LLAPKDERLA AFEAQVQRLQ AELAAAKNDA AGVEAALGDG ATEASLSTDV
AQLQLQLKAA NAASMTLCDE VDRLSSAYDQ LDKQTSARIA NVERLEDKML RVTTEKAKAD
NKYFAAMRAK DALEVEKRAL ARSAERQAKV IERYTEAEKG LQTQVAQAEK EISALRRSLQ
THTSKLAEAD RDVAVWRRRH ADAERARAAA EASVSKHLAT AEQETSARHK AEERMMALDR
DVGRLRRRLA ESSTSSRRRE SSDADTHLEY LNSLLRCSSC KERYRDRIIT RCFHTFCEAC
INARLQTRQR KCPHCGLAFA SSDVQALYLQ
//
