UniProt: A0A0L6WCU7

Database: UniProt
Entry: A0A0L6WCU7_9AGAR

LinkDB:  A0A0L6WCU7_9AGAR 
Original site:  A0A0L6WCU7_9AGAR

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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   A0A0L6WCU7_9AGAR        Unreviewed;       641 AA.
AC   A0A0L6WCU7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=J132_01896 {ECO:0000313|EMBL:KNZ72904.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ72904.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) 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; KQ412828; KNZ72904.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WCU7; -.
DR   STRING; 1306850.A0A0L6WCU7; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053712; 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:UP000053712};
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          587..625
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          155..196
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          268..323
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          386..437
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   641 AA;  73019 MW;  1FAA9C7945CED71B CRC64;
     MAKEEFDADN LELFRKEAIY RRMKHYSREN ERCQSLIEDL EKRKQSCEVG LAAMTACWNH
     LIKTIRLLVR SDDSDEVAEQ MFDFTVRIQE DKAPDITKTL EVNLKATENL VTRLFEAGGN
     TQTPLPAGST LHHCQKEISD VSPAQHNGIG VPKEVDILRA QVASREARIS ELEQDVASAT
     LKRMMLEAEL KQMSHERIVE NPHYKSLLEH AGVLQASLTA SRAEITRLSE ESNHLRASRI
     EWEENLINAA NQANQELKIM LGKRDAENSR LREQREQQAA ELVERRQQDN VKTSSLREMK
     ALNDSRLERI ATLESEVARA KARLAANMGD EDLMKFFLEG QTHEAEYFTS LKERAVVAEQ
     RASILEQSLS KYQDAHPDIA EHLKAEADAL QRLADVQAQL EKYKRVYGDA SGLPPDTSAL
     AEQLRRKEEE VHKLRLQDTQ HTQAETSLYT ELEKLSTAWE SLERQVKEKV FDLGNLENQL
     KKATSEKAKS DNKYYAAMRD KDAVSAETTR LQRNVEKQNK VVERLVDAEK NLTAQKLNSA
     KHVELRKMED GIIRTRKELD AKIKQQESAA SQSGGSENAK LLRLLKCSAC EVEFRDTVIT
     KCLHTFCRPC IDARISTRQR KCPACGLGFA QSDVLYGLYF Q
//

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