ID G2XWE0_BOTF4 Unreviewed; 1014 AA.
AC G2XWE0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Ring finger domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BofuT4_P051590.1 {ECO:0000313|EMBL:CCD44810.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD44810.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
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 -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR EMBL; FQ790272; CCD44810.1; -; Genomic_DNA.
DR AlphaFoldDB; G2XWE0; -.
DR STRING; 999810.G2XWE0; -.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_005224_1_0_1; -.
DR InParanoid; G2XWE0; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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 InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 18..74
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 948..1009
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 154..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 113587 MW; 13D7241278C375FD CRC64;
MDSGSENRGL DLEKELTCSI CTEVLYQPLT LLDCLHTFCG SCLKEWFSWQ LVSVNNAQTL
IPPGGTPYTC PSCRAPVRDT KHSSTIATLL EMFLARSPEK GRTADEKEEI AAKYKSGDEV
LPKWEQRDRS SRERRLEDED RRLMEEVRDL SLREVGVESS EARRERRRRE RDAERSHSSR
HHPSRDHSRN TDDADRRRRR EEHHERRRAR QGTSALRPEP DRSDSEGRRR GYSETESIRR
HEETSRSAAR QIEHQSSLRS LISSSDIDSR EMEEEILRQI REEGLLDGID LENIDVNQED
QISERIAEAF RRRQEERSRP ESSRRSESDT ADRRRRSPRA SLTDSGRETS GDDAPRTTRR
RRNQSSSPRS GSLSNEQSRP PPSISAVHAS HLDVGLNSGG RRRQRTLSAP RSSTAPGPVI
TPETRPAARS QTDLSTIPRT SFVQTSQPFR AHARRSTDSN VRRLSESSTS RELQPQTGST
TRTSNSTLVA SPSESTPRTS SNSLLERSHS DDMPELPDIP AMPAPLSIRA NAPADIFVAS
AVPASVPYMD ESLIPAPLSP HTPTHLALFD KAAALASGSR PSSSHSVGSR PRTQLYPEPS
ILCRRCQKTH IEYEVHYNCS SCLRGNYNIC LSCYRSGAGC LHWFGFGYSA WSNWEIQMQA
GKIPQGADRP HMLTANRYLA PKMAAGGADG RKTLTTEDPQ KRLQSGAFCA SCLAWTNECY
WRCDICNHGD WGFCNLCVNQ GRSCTHSLLP LTYKPSESYT PPLSPMHDQH LPPSATILQG
PGVADVGNFK PLTFSTNCDI CRYPIQPSST RYHCYSCTSA VPDTQPGDYD ICTTCYPKLV
TSRRISVENG HNGWRRCLQG HRMVIVGFED DRGGQRRVIV HDLVGGHSLD IEPMLYPSAD
HAAPELQKWS WGQDNDTFVR LVTTDPSKVA PTSVPGLMIE RSFPPDGGIG MSTLAIWSWW
PAEGASDELM FPKGAEVREC KDVNGDWFWG CYMGAKGLFP APYVRVLEDG ITGI
//
