ID E5ACQ9_LEPMJ Unreviewed; 563 AA.
AC E5ACQ9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=UBR-type domain-containing protein {ECO:0000259|PROSITE:PS51157};
GN ORFNames=LEMA_P010480.1 {ECO:0000313|EMBL:CBY02261.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY02261.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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DR EMBL; FP929139; CBY02261.1; -; Genomic_DNA.
DR RefSeq; XP_003845740.1; XM_003845692.1.
DR AlphaFoldDB; E5ACQ9; -.
DR STRING; 985895.E5ACQ9; -.
DR EnsemblFungi; CBY02261; CBY02261; LEMA_P010480.1.
DR GeneID; 13289441; -.
DR eggNOG; KOG2752; Eukaryota.
DR HOGENOM; CLU_025221_1_0_1; -.
DR InParanoid; E5ACQ9; -.
DR OMA; GAMVYNH; -.
DR OrthoDB; 11436at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19677; UBR-box_UBR7; 1.
DR InterPro; IPR040204; UBR7.
DR InterPro; IPR047506; UBR7-like_UBR-box.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR13513; E3 UBIQUITIN-PROTEIN LIGASE UBR7; 1.
DR PANTHER; PTHR13513:SF9; E3 UBIQUITIN-PROTEIN LIGASE UBR7-RELATED; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 43..121
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 43..121
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 202..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 60791 MW; 5768D51C00C4E3EE CRC64;
MASKPRTSSM SQASESSQTA AEFIKEQLSL EAEAREALPY QFDTCTRDLG PLRQSLYACL
TCNPPPASPA QVHIPAGVCY SCSISCHGEH TLVELFNKRD FICDCGTNRI PETTPCTLRI
NSTTGQKGDV SGEEPATSNK YNQNFQNRFC GCGEEYDAQQ EKGTMFQCLG LGTCEEGGCG
EDWWHPECLV GLSREQYRKM IEKPKTDKNN GTAQTAAAGK PTEKLASDNT TTETEPPSAT
TITTAVGNGN GVDGHDVEAG AEEQDEDDDP PLPPGFPAED DFDHFLCYKC VAAHPWIKKY
AGSTGFLPPV YFDASIAISN AEKVQSGNPE FSTVESKKRK ASEENENEQI ASTATLEAPA
PAKRQKSEDP KNALASLAED TVNLPITPKK QEEPSVPKHT LLPPLPETAL TTPFSLFLKP
DFRDHLCRCP DCFPLLKPHP QLLEEEDTYE PPVSESGDEN PQSVGTGSLL DRGEVAFNNM
DRVRAIQGAM AYAHLKDKVA AFLKPFAESG QAVGAEDVKA YFEKLRGDEQ GIQEAAGGAR
QSRDGDGEGG AGGGAGRTEQ SGY
//