UniProt: A0A1Y2V2R3

Database: UniProt
Entry: A0A1Y2V2R3_9PEZI

LinkDB:  A0A1Y2V2R3_9PEZI 
Original site:  A0A1Y2V2R3_9PEZI

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   A0A1Y2V2R3_9PEZI        Unreviewed;       653 AA.
AC   A0A1Y2V2R3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=M434DRAFT_337350 {ECO:0000313|EMBL:OTA91831.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA91831.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA91831.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA91831.1,
RC   ECO:0000313|Proteomes:UP000194361};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112493; OTA91831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2V2R3; -.
DR   STRING; 1001938.A0A1Y2V2R3; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000194361; 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; IPR027370; Znf-RING_euk.
DR   InterPro; IPR013087; Znf_C2H2_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; PF13445; zf-RING_UBOX; 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.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_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:UP000194361};
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:PRU00042}.
FT   DOMAIN          601..639
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          634..653
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   COILED          127..161
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          197..323
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          493..583
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   653 AA;  74312 MW;  BEC06725030FC2E4 CRC64;
     MLEYKREKNT LEAQLDEAQK KSIHHDDHIR IIDNWWLQLL QEVELLVEGT IPFQGSDGQP
     FPTHTSFKDL EEFESHLSEK ASSIKKMVEA ILSRLSGGRS QVAPDISHLE QQIGALLAQQ
     KEFLVKLDRL ATDKDSLSEQ LNTATLRYMK AERRLDRAKS AQVQKLEQQA LNHVAARPTM
     GVDQENGMAA EENNTNNEAL QLALREANAV AEKQKQQLES ALTQNKTLQE ELTAVQTRLT
     NLTDEDYSRT EVFKMFKSQM EDLVRKINSL EADNKSLRAS AEKLEAERES SRRKVESEAQ
     ALIAELEDQL QQADTTLARV RSARDELHAD VTMLRASKEQ DRTALEHMKE FVSAEEDRIT
     ALESEVRRLQ PSEDVDMTER PDIDALSLEE IREKYKKLMK DYNSIESELP GMTNAVKKYQ
     ALAHKKVMDH VAMEERVALT IAEKSKADQK YFTARKDGDL KAEVIQKLRT QNSKSSEIIS
     QLKEVEAHNR TLVTNLDKQL SDLKQTNASV TAENKKLEAS SNEMLRRFDA LKQQVAELSN
     LAKSKDSTTA AAKERAATLE SDVEKLKVRL ESVSKDRDKW RAKCLSNSSE EEEMLRTMAT
     CSVCKKDFKN TIIRTCGHIF CRGCIDDRIA NRMRKCPTCG RAFDKSDTMA IHL
//

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