UniProt: A0A3M6VW17

Database: UniProt
Entry: A0A3M6VW17_9STRA

LinkDB:  A0A3M6VW17_9STRA 
Original site:  A0A3M6VW17_9STRA

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
   SMART (1)   
All databases (19)   

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ID   A0A3M6VW17_9STRA        Unreviewed;      1205 AA.
AC   A0A3M6VW17;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=DD238_000063 {ECO:0000313|EMBL:RMX70316.1};
OS   Peronospora effusa.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Peronospora.
OX   NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX70316.1, ECO:0000313|Proteomes:UP000282087};
RN   [1] {ECO:0000313|EMBL:RMX70316.1, ECO:0000313|Proteomes:UP000282087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R14 {ECO:0000313|EMBL:RMX70316.1,
RC   ECO:0000313|Proteomes:UP000282087};
RA   Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA   Reyes Chin-Wo S., Mou B., Michelmore R.;
RT   "Comparative genomics of downy mildews reveals potential adaptations to
RT   biotrophy.";
RL   Submitted (JUN-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMX70316.1}.
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DR   EMBL; QLLG01000003; RMX70316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6VW17; -.
DR   STRING; 542832.A0A3M6VW17; -.
DR   VEuPathDB; FungiDB:DD237_000654; -.
DR   VEuPathDB; FungiDB:DD237_000655; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000282087; 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:0070042; F:rRNA (uridine-N3-)-methyltransferase activity; IEA:InterPro.
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   GO; GO:0070475; P:rRNA base methylation; IEA:InterPro.
DR   CDD; cd16499; RING-HC_Bre1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019446; BMT5-like.
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; PF10354; BMT5-like; 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:UP000282087};
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          808..847
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          244..271
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          382..416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          477..601
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          693..720
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          751..785
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1205 AA;  139196 MW;  95BB1D78C141CC4F CRC64;
     MADTEAHTQE NGVSHRKRRE TLLESESAPK KIKLEDDTPP EANPNTIEAV REKNKALEID
     RNEKNRRIAY LTKKCEALYR SREIKSASFR CLRRQWFQLQ DELLAAVKTV DPSAVSDEKL
     KESWLAALNA VDDFGKVRVR AEELVLNLPE WFVTVAKYTE EEEEPDADVS LPTDDDVNDD
     ALVKMDDLSH MEKEVHDQLK RKSQNMKELL QKLLALVGSI AQDKTKSIEY AHIVQEKRAA
     VAETLDLKGQ LQTCKRRIAE LERDVEYKET ERHRACRDYD RLSAFVKQQG GVNTDRIDDS
     DTKSEQVIDT EKPSEKTMSG PSSAEIVKQE ALAEKEKEHN KIVATLRENM GILSTKLYQE
     RQKFDSMRRE LEKFKALEVA WKNDETALVQ DHEEKLKQLR DEKAHVDEEY KKLLHKSKDL
     EHHMTEKWEK KITKIQAEMS TIKSQMDGLN LKNVSLREKI SNASTYRDQL SEVKPELESV
     KRENAKLKAQ IKCARSREDR AQMSADNHEI QILTQKVNLL TKEKLELQQT YDMLKNAEMY
     ESSLRWLVFG GLTNLLSLNR KNACEKLSEA LERLSEVQHK LEQERKKHHE CSTDREKLRA
     KIEDMKAWSE ASREENDALL LEIDTITKDV NSLRHGRKKF IQQIEEKRNA NKKLHTLLAR
     EEQAKSHCFE ELAAVRLQVS SLSTVHKHQK TFIESSKESL QAKELELEKM KKYVKTIEEE
     REASDVEKRK VLRDAEVAKK ICETAEKSQR EQQLQQEKQK HCEKCESFRK KIEDVERQLQ
     HSKMATSTGE LTDLERFELR DLQKLVNCSV CQDGRKDVII SKCFHMFCKE CIENNLKSRN
     RKCPTCKKMF GQDDVKTVWF TMARKKNDIS SQKRRLTGSR LGSNTKRQRQ DIQKKTLTQV
     YAPDDAVLVL GDGDFSFSRG LIKHRGTGRG VLATSFDSEN EVRRKYPNAQ ECIAAVQAAH
     GLVLHDVDAT KLLELPRHLK IGTGMKTVPD FFQYIIFNFP HSGQQRVHIN RALLLNFFES
     ARDRLLVHGE AHVTLKTRPP YSNWFIEDQA KKAGFVMKDR RKFDVRLFPG YRHRTTDPQA
     KTFEPNLCVT YVFVVHRSKY PFQNSRAALN AAGAEIAATQ ASEQHDLATA IVNIANAQAA
     ANKNKNVKTR GVAVRTEEPT MPRKRPIAIV VCPEKQATKT RRIAQVTPHV SWKPLHRHLG
     GTCFW
//

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