ID   A0A1W5D7J6_9LECA        Unreviewed;       714 AA.
AC   A0A1W5D7J6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
OS   Lasallia pustulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC   Lasallia.
OX   NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM39011.1, ECO:0000313|Proteomes:UP000192927};
RN   [1] {ECO:0000313|Proteomes:UP000192927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma R., Thines M.;
RL   Submitted (MAR-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}.
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DR   EMBL; FWEW01003236; SLM39011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W5D7J6; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000192927; 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   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          662..701
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          168..209
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          262..374
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          410..511
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          617..644
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  80060 MW;  EE5DA39417CE9A64 CRC64;
     MEERKRPASY DHDDSAPPLK RQATSVNGGS KGHPDDMPWK DELERFQKEA IWRQMQEYKR
     ERNTLEARLN DLTKRTAYHD DHLRIIDAWF GQLLDEAKMI VGQVDNHAFV PSFPSALLTA
     DNSTFEEHLE LRSSEISSAI SQLFSRSVAP SPEVSELQGR ITHLLFTEKV HIVELEKSRS
     EKEQLEERLE SASLRYMVAE KKLERAKSAT VAKLERQATA GGRESGSGIG GGAESSGKKD
     SDGLNGVDES NDGAAEATEV TRREAVAASI KQKEQLEKLE ADNEKLTAQL TTLNIKMSRL
     SDDDCARTDL FKQLKSQHED VIKRINNLEA TNNQLREEAE KLQAERTAYR VQMENEAQAA
     LGEKEAQLTR AESDLARIRT GRDELIADNQ MRKAAQDQER GSINQVRELA AARAERISAL
     ESEIERLKIE LGHADSGSVP QTGLGNLSAE ELRTKYQNLE RQYSMLEKEV PLMVSALKRA
     STLASQKISD LSALEDKVVR LGAEKSKADQ KYFAAMKAKE ARDQEVRTLR AQNSKSSDIV
     SQLKDAEAST RALVINLEKQ LAESKEAITN ISNRNRTSQQ QLLERTTALE GSKAQVEELK
     KMLTTKDASL STVSSSYRKA EVEIEELKVR LDETKQSLKG WKNKSLATEG SEETALRMIA
     YCTVCRKNLK DTALKTCGHV FCKDCVEERL TSRSRKCPSC NKSFGTNDHM RVTL
//