ID A7F4U5_SCLS1 Unreviewed; 684 AA.
AC A7F4U5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=SS1G_12620 {ECO:0000313|EMBL:EDN97766.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN97766.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476641; EDN97766.1; -; Genomic_DNA.
DR RefSeq; XP_001586633.1; XM_001586583.1.
DR AlphaFoldDB; A7F4U5; -.
DR STRING; 665079.A7F4U5; -.
DR EnsemblFungi; EDN97766; EDN97766; SS1G_12620.
DR GeneID; 5482636; -.
DR KEGG; ssl:SS1G_12620; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_2_0_1; -.
DR InParanoid; A7F4U5; -.
DR OMA; YRQMQEY; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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 Reference proteome {ECO:0000313|Proteomes:UP000001312};
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 632..670
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..76
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 175..216
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 252..359
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 545..614
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 77633 MW; 4289800EDE23A682 CRC64;
MEDRKRAAGQ SNDDLAPPTK RQAVNGSGKA SSDSDNTAPW SEDIEKYQKD AIYRQMLEYK
REKATLESQL KNIQKKSTDH DDHLRIIDAW WTQLLEEVTL LAENDIPNIE KTEPSFPTSL
QFHGIKGFSD HLASKGREIK SKLHTIFNNV AATRGKPSSD LQDLQSKVTK MLASQKEYLV
TVDRLRNEKE ELNERLESAS LRYIKAEKRL DRLRSDTVRK EEAKALFHST ANGVKADNSM
DTEMTNGIAE DKEANQTAYK EAQAVVEKQK EQLEAMAAEN KSLTEQITSA SIKQVPSDDD
YARTELFKQF QKLQAERTAY RIQIENEAEA TAGELESQLQ RLDADLTRIR SARDELLADL
SVRKATQEQD HAGIEHLKEL VGAKDDRITS LELEVERLRQ IAEQSCQPTP GPEIDSLSLE
ELRVKYDLLQ QGYDSINKEL PALQSAYKRV QALTSKKVMD FTALEEKVSV LAAEKSKADQ
KYFAARKDMD IRLAEVRSLK NQNAKSSEII SQLKDVETSD RTLLSNMEKQ LSDMRQSNTS
IMAENKKLEA SSREATSKCE ILKNQAAELT NLLKSKDSAN SGTKQKIHAV ELENEQLRVR
CEQAQKDRDT WKQKSLSNQS GEEEMLRTLA LCTVCRANFK NTVLKTCGHL FCNQCVDDRI
ANRMRKCPNC AKPFDKFDVM TAHM
//
