ID M5CC92_THACB Unreviewed; 458 AA.
AC M5CC92;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=E3 ubiquitin-protein ligase DMA2 {ECO:0000313|EMBL:CCO37066.1};
DE EC=6.3.2.- {ECO:0000313|EMBL:CCO37066.1};
GN ORFNames=BN14_11217 {ECO:0000313|EMBL:CCO37066.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO37066.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO37066.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
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:CCO37066.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAOJ01016719; CCO37066.1; -; Genomic_DNA.
DR AlphaFoldDB; M5CC92; -.
DR HOGENOM; CLU_023195_0_0_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR PANTHER; PTHR15067:SF8; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 9..60
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 126..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49284 MW; 1631F2498FBC7FC8 CRC64;
MPIRCSSLVA ASRQSDSTKI AFKSKVVSRA HAEIWCAPNG KFMIRDTRSS SGTFLNHTRL
SAPNIESRPT ELHDGDIVQL GVDYQGGNEE IYRCVKIRVE VGREWQREAN EFNTGALKQL
QTLQGRGTDG VKEKAKEKPR TSTPSIIAGP SNSRKTSVAD CCICLFPVGI LQSLFIAPCS
HCFHYKCIRP LLVKTFADLE EDVEQEYAPS AAPSIRAPSV YAPSVHEAEA VVGLIEAAAA
ANAHRECVDV CVGTSPEHGT KELPPVPNDE ASGSGSMTRQ STLDAGSDRL RPESTHSGPP
HNSDGGSTPR GSSEDLRAAQ RGLFDTTLVS DEPEDDMVRV PGGIIVPRSP EREHDIFNSA
TPLNNQFLTL TALNGIGSGL PSIPSVGDIP ALRHTSEYES SVDLAAPYRS EDTESAKHIL
VDDEEEDGED EALVIAGMKR MSVATETEAG PSSQLKTI
//
