ID A0A094BCG8_9PEZI Unreviewed; 664 AA.
AC A0A094BCG8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=V494_04797 {ECO:0000313|EMBL:KFY37323.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY37323.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY37323.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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}.
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:KFY37323.1}.
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DR EMBL; JPJW01001624; KFY37323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BCG8; -.
DR STRING; 1420907.A0A094BCG8; -.
DR HOGENOM; CLU_019713_2_0_1; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000029288; 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; 1.10.287.1490; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; PF08647; BRE1; 1.
DR Pfam; PF13920; zf-C3HC4_3; 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:UP000029288};
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 612..651
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 99..161
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 220..419
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 560..594
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 664 AA; 75135 MW; FD6521D730E09C73 CRC64;
MTEYKREKAL LESELRDVRK RSVDHDDHLR VVDAWWSQLL DEVTLLTKNS TPSTFNIDAP
FPTATDFENS VVFSDHLASK AKQIKEMVAN IMANLDTSSE KRTDEVQDLQ QKLNKLLASH
KDEMVKYDRM RVENEQAKER LESASLRALK LERKLERSKS STVAKLEQQA IAGTGNSAGS
GIGSVENGFD TRAEVANGSK DNEAKVEASQ VALKEAVAVS DKQKQQLEEL FTENKSITEQ
LTAANARLAN LTEDDYARTE LFKNFKSQHE EVIKRINHLE ATNIQLREEA EKLQAERTAY
RTQLQNEADA VNGELESQLQ RLDSDLARVR STRDELLADQ TMRKANQDQE RTAIGQMKEL
VSAKEDRVTS LESEVQRLKS LVEGSCEATP KSEIEGLDLA ELQRKYVTLE QSFSSVNNEL
PAMEKAYKRA VATASKKVMD FAALEEKVSI LIAEKSKADQ KYFAARKDMD TRIGEVRALR
AQNSKSSEII TQLKEVESSN RTIVTGLERQ LSDLRQLNNS VTLDHKKLQS TSSESASKLE
SLRSQVSELT NMLRSKDTAL STTKQRAQSV ETELEQVRAR YEQSEKEKET WKAKSLSNQS
GEEEMLRMLA LCTICRKDFK NTALKTCGHL FCNHCVENRL ANRMRKCPNC SKAFDKMDVM
AVHM
//
