ID Q0U3A8_PHANO Unreviewed; 574 AA.
AC Q0U3A8;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_13756 {ECO:0000313|EMBL:EAT78780.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT78780.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445352; EAT78780.1; -; Genomic_DNA.
DR RefSeq; XP_001803962.1; XM_001803910.1.
DR AlphaFoldDB; Q0U3A8; -.
DR STRING; 321614.Q0U3A8; -.
DR EnsemblFungi; SNOT_13756; SNOT_13756; SNOG_13756.
DR GeneID; 5980884; -.
DR KEGG; pno:SNOG_13756; -.
DR VEuPathDB; FungiDB:JI435_137560; -.
DR eggNOG; ENOG502SBGS; Eukaryota.
DR HOGENOM; CLU_012883_1_0_1; -.
DR InParanoid; Q0U3A8; -.
DR OMA; LACQVCY; -.
DR OrthoDB; 75723at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22696; E3 UBIQUITIN-PROTEIN LIGASE RNF26; 1.
DR PANTHER; PTHR22696:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF26; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT REGION 121..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 64728 MW; 12455D8FBA992751 CRC64;
MGTLTADCPR LDDHCPHKLA TSVYIDGIGF VQRGTRWQGY CWFCKEFWTN RLAATDPPLE
LAQTRIPEIP DQTEFLERWF EFHKGYRVAK LQDGTEQHMP VIGEPFKEVS PGFLPRTLDQ
LRRGVQNDAR RPENRLRRRR LTSEEERPDE PQQSLDSALD SLLAEVEDEE TPRAPQETAP
HPEEAQQPEV LTPESLPDLV PAEQPMTEEA SQPANRPRPL NRGEARLQRA RERFARVFGT
QEDIQQDDYQ SPLSLLYNRA ENRYHQAEER RATNTTAPPP LDGLSARERR EIEEQLLWGV
MRESALDGGA EDHVWSYAPR RLQPSEGARF VRSQAMREYR VRQAQGYNRL PVRPSTGAGH
DRDLTSAQSS SSTPATSGPS QSGVTATSSP VLPTAAETSP AGMAMLLRHQ ARYEAMLAER
MAEFERAQPE AGLTAFTPGQ ARDGVEPNIE ASGENANGNG MSQIQTSIQQ ITSELHRLRL
ASEAITSARH SMHSHFQPPP ERPPQTLDNQ PGRPDAMSEE EMTKKLECQV CYQQLADVAL
LPCGHMVMCQ WCADVVIPVK HSHLPIRPRM LNMQ
//
