UniProt: A0A1B7N5G5

Database: UniProt
Entry: A0A1B7N5G5_9AGAM

LinkDB:  A0A1B7N5G5_9AGAM 
Original site:  A0A1B7N5G5_9AGAM

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
   SMART (1)   
All databases (17)   

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ID   A0A1B7N5G5_9AGAM        Unreviewed;       412 AA.
AC   A0A1B7N5G5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=K503DRAFT_24999 {ECO:0000313|EMBL:OAX40088.1};
OS   Rhizopogon vinicolor AM-OR11-026.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX40088.1, ECO:0000313|Proteomes:UP000092154};
RN   [1] {ECO:0000313|EMBL:OAX40088.1, ECO:0000313|Proteomes:UP000092154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX40088.1,
RC   ECO:0000313|Proteomes:UP000092154};
RG   DOE Joint Genome Institute;
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (JUN-2016) 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; KV448224; OAX40088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7N5G5; -.
DR   STRING; 1314800.A0A1B7N5G5; -.
DR   InParanoid; A0A1B7N5G5; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000092154; 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:UP000092154};
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          359..398
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          184..281
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          310..337
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   412 AA;  47203 MW;  DCA1400793CF189E CRC64;
     MQISHASATN SSRELKTLAE SRAERIIQLE SEVRRHKAKL AAHAGNEDLM RHFWEGKADE
     LEYVDGLRRK LLETETKLTA IQQSMFTLQE EQPDIARYIA SETSAREELA ANAVELLRYR
     SLLGEGSSPD LARQLQVKED ELQKLRLLAE QHQQAEDAIY AEVERLSGAW ETLDEQLKSK
     VFSLTAAEER VAKSAHEKAK ADNKYFAAMR DRESVDIERK NVIRNLEKQA KVIERLADSE
     KNLQQQIGQL ETVNQRLHRM VDEAETRIDA LDANAVMYKK QAESTDEMMM NVRKLANDKY
     GNIHSLKGSL FKREEELARM KVEMDKLRAQ TKKLKYASAS EKEAELAEEV ASVWRLIKCS
     TCKENMRGVT LTKCSHTFCK QCVDARLSTR QRRCPHCNSG FAQSEVVNIL FQ
//

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