ID A0A1Y1W5M4_9FUNG Unreviewed; 856 AA.
AC A0A1Y1W5M4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=DL89DRAFT_268363 {ECO:0000313|EMBL:ORX68536.1};
OS Linderina pennispora.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX68536.1, ECO:0000313|Proteomes:UP000193922};
RN [1] {ECO:0000313|EMBL:ORX68536.1, ECO:0000313|Proteomes:UP000193922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX68536.1,
RC ECO:0000313|Proteomes:UP000193922};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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}.
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:ORX68536.1}.
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DR EMBL; MCFD01000009; ORX68536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1W5M4; -.
DR STRING; 61395.A0A1Y1W5M4; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000193922; 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:UP000193922};
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 804..843
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..241
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 321..351
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 380..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 504..617
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 723..785
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 252..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 97740 MW; 420204F9F6F1DF31 CRC64;
MTERKRRSDE SRDLEGQPQA TLAKKRHTSK ETDFQALSAE FDENAQMLDL FQKEAIWRQM
QEYKRDARRS QQRASDLERR QEQWTMRIGR LCHAWDQAVA QLDTIINSDT SDGSLSSAHP
SAVDSWLGML LPTKIAETAD DGMATADSNS AVEKSDVVQT SLQRFNRAVQ TILRQLESKS
TSPVDWQSAI ERLSRMRTSE KEVADLRSQV AQFSRQIAEE REQLEASQTE LRRALKKLDR
SVCPTVQALD VETQPHQQNS GSSPHSHAPP NTTAIANGAV YSRAGSPSAA GSPAQQQTAQ
QQQQLQQPQQ PQEANDKTDY RELAERRLSE IEEKVRENAE IQKQLDALRL QISNIPDHII
AETSLFKQAE ASREYYNAES LRLQAEVDRL FKEVAELKSS RTEFDMSLQA AANSQRQILE
AELQRLQTDL VRVRNHRDQV QRELESRRAQ DTVEDQKSTE LKLLSDVRRE RMNSLISENK
RLLACIAVLK GDRSAFETYT DEELSKTTAV ADELRAKLDQ ALRREKQLSA QLAASSQPDA
SQLAADLTRA QETADSLQKR LAKYESILGG ACVDEHGQML AELPDKAGEL AQKQRQVDEM
ILQRDSLQRT SEMMERELQT ICDSFTKLEK QNTSKVWELA SKEQHISRVV AEKCKYEEKF
IGLNKDREAQ KQANQALRHQ NQKQLEHIKT IEERDRAMAQ ELSLASAETQ QATLAWQGCQ
TNLQESQRRT QELEEQVRAL EEKHRVATQM LDERTDSLSR AEHERRRAEE ALELASKRVS
EAEKITDQSG LAQMCADYKA LLKCPTCQTH FKSHVLLRCM HVFCKECIDS RIETRQRKCP
SCSEPFGAKD VRQIYL
//
