ID A7F5S9_SCLS1 Unreviewed; 757 AA.
AC A7F5S9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS51873};
GN ORFNames=SS1G_12957 {ECO:0000313|EMBL:EDN98100.1};
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:EDN98100.1, 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).
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DR EMBL; CH476643; EDN98100.1; -; Genomic_DNA.
DR RefSeq; XP_001585865.1; XM_001585815.1.
DR AlphaFoldDB; A7F5S9; -.
DR EnsemblFungi; EDN98100; EDN98100; SS1G_12957.
DR GeneID; 5482091; -.
DR KEGG; ssl:SS1G_12957; -.
DR VEuPathDB; FungiDB:sscle_02g022150; -.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_015887_1_0_1; -.
DR InParanoid; A7F5S9; -.
DR OMA; PWFNYET; -.
DR OrthoDB; 251172at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR11685:SF404; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01485; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 304..504
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 84841 MW; 6C799451EB85685C CRC64;
MAGSNDIHKV RRRPKFTNGE LEDEKVHKSR PGRHEGEVVT SVEPDISEVR RKRLEKLEGN
STNRSTRNSA ATENMPAEPS MTVDATKSSS SHRRRRRHHT SEDGAGHHSR SKTNEREEKP
RSDYVYAATR EGDSKTKPHG ISVTERRRRE EEDDSSDESE DEDKSPLESM DSKLKKKTKD
VVREQPKRSN STSSRMKKED KDKLSTKGSA DTGTLGSKST SRKPKVTTGD SVSRPPLSRS
ATTWITTEPR PALRRNSMTD KPKVPPSIAN TSTSHTSQRR SSFLGSFFSS GPPPPPPPPP
EPEKLVECLT CLSDDIPKSK CAKLRCGHRM CHSCLRRIFK LSVKDPAHMP PKCCTAEHIP
LKHVEKLFDI PFKKLWNKKY HEYTTKNRIY CPAKRCGEWI KPENIHKENG RKYGICGSCK
TKVCALCNGK WHGSKECPKD EETNKLLETA KQAGWQRCYN CRTMVELKEG CNHMTCHCTA
QFCMICGLKW KSCHCPWFNY EPLEADQLND MQVPQPVAGR NPTPPVRGAR DRARRQPPID
FDEEINQRRR QEREDERLAR QLQNWGFEDT PRNDRDTDYN GGIGDVEGVG NGAGHFMNQD
YIREASNVLA HPGGVMNFGL GVTNFLTGVL RPRGASVANP TVGEMSAVPP VAPMDEPQPS
VPGLIRRHTT RDATRANGPT RRASDIVVPR RTRTDYAVEA AIHAPDSRSP SSTSKTKKEK
EKKTKSSILA GLGSGKNRVD AWRSYVAPGA PPAEPVS
//
