ID   A0A0D1YKN5_9EURO        Unreviewed;       705 AA.
AC   A0A0D1YKN5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=PV08_05584 {ECO:0000313|EMBL:KIW15536.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW15536.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW15536.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW15536.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-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; KN847495; KIW15536.1; -; Genomic_DNA.
DR   RefSeq; XP_016235752.1; XM_016379925.1.
DR   AlphaFoldDB; A0A0D1YKN5; -.
DR   STRING; 91928.A0A0D1YKN5; -.
DR   GeneID; 27332667; -.
DR   VEuPathDB; FungiDB:PV08_05584; -.
DR   HOGENOM; CLU_019713_2_0_1; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053328; 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; PF13923; zf-C3HC4_2; 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:UP000053328};
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          653..691
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          49..76
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          170..211
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          249..574
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          610..637
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   705 AA;  80447 MW;  C333B4E0F857FDA8 CRC64;
     MEERKRPSPY DQVDSAPPSK KLATSANGAS KSHKDDDMPW KDDLETYQKD AILRRMQEYK
     REKNTLESQL KEMRKKARYH DDHLRIIDSW FQQVIDEVKL IAQGDDDVDM ESSSLPSSLL
     FTDQEHFQEH LQSRSKEIKA VISKLFGSKN PASPDITQMQ SRISRLLAAE KGHVVELSRL
     QSEKEDLEAR LENASLRYMV AEKKIDRAKS VTVAKFEKQA LMGATKTQTE DGSSVKREDS
     VVNGTTDHAE ELAEVETQLN KKAAAFEKQK DQLEKLEEEN ARLNAQITEL TTKSVILTDD
     DYAKTELFKQ LKSQHEDVIK RINNLEAVNT ELKEEATKLR SERTTFQLHL ENERRVALQE
     KESLLAASEA NLARIRHNRD ELLADQAVKK ATLEQDQEAL RKMKELSSAL EDQIRALESK
     NERLSESNAM AVDDVALEGL SLEELRGKYT ELERKYNLLN VELSSMSTAF QKTSKIATQK
     VSDFAAMEEK VLRLSAEKAK ADQKFFAAMK SKETRDSEVR TLRLQNSKSA EAVSQLKEAE
     NASRALLVTM EKQLAEMKDA LTQKINEHRN VQQQNITQGL EVSRLNSQVT ELKNQLTAKD
     TTLAQTSSVC RAAEVEAEEL KASLKDCRRN LEMWKSKSGQ HEQYEILRQF AYCNVCKKNL
     KNTVMKNCGH TFCNECVEER MTSRSRKCPN CGKAFGSNDH MRITL
//