ID   L2FSC1_COLFN            Unreviewed;       685 AA.
AC   L2FSC1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=CGGC5_10808 {ECO:0000313|EMBL:ELA28623.1};
OS   Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS   (Colletotrichum gloeosporioides (strain Nara gc5)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA28623.1};
RN   [1] {ECO:0000313|EMBL:ELA28623.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA28623.1};
RA   Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   fructicola.";
RL   Submitted (AUG-2012) 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; KB020913; ELA28623.1; -; Genomic_DNA.
DR   RefSeq; XP_007282326.1; XM_007282264.1.
DR   AlphaFoldDB; L2FSC1; -.
DR   STRING; 1213859.L2FSC1; -.
DR   EnsemblFungi; ELA28623; ELA28623; CGGC5_10808.
DR   HOGENOM; CLU_019713_2_0_1; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
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; 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   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          633..672
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          55..82
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          168..209
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          242..326
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          420..482
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          518..552
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   685 AA;  78585 MW;  D20D35BEDC9361D8 CRC64;
     MEDRKRPPIS TAEDLAPPSK RHQTVNGSKS KGDSGDTAEE HWIENYQKGA IYRQLQETKR
     EKADFESRVE QLQKNLNHRE DHIRIIEAWW KQVLEEMEQL VDPALPPPSG PTSPPYITST
     HFKDNEEFQR HLGDTTADIR KRAEAVINRI ASARGEITPN IADLETRVNS LLAQQKDYLV
     KLDRANQENE QLSEDLNKAS LRFFKAEKRM DRLKSAQVQK LEQQFIASAK PTAAGGENGS
     DNAEANGNAA EALIKFEEAS AEENSALKAR REGLTDEDFI RTDVFKQFKS QNEDLIKRVN
     HLEATNKQLK EEAEKLQAER TAFRTKLHDE AQGMVIELER QVEERDADLT RIRAARDEWY
     AKANMLETRE REEKQAHQHL KELTGSQQDR ITSMELELQR LKPEDQQMAD PDPELDTLPA
     EELLAKYKKL QQDFESINKE LPALQQAYKR SMTLAQKKVM DFTALEERVA AALAEKQKAD
     QKYFAVKKDA DMRDRELGVL RSQHRKSSEI VSQLKEVEAQ HRVLISNLEK QLSDLKQANA
     AMAAEHKKME ATSSDAARRA DSYKNQINEL SGLVKSRDAA VAAARERTTT QEAEVERLKV
     RADMVQKDKD EWKRKALSNS SEEEEMLRTF ALCTVCRNNF KDTALKTCGH LFCHQCVDDR
     ISNRMRKCPN CSRAFDRLDV MSVHH
//