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Database: UniProt
Entry: B2WH69_PYRTR
LinkDB: B2WH69_PYRTR
Original site: B2WH69_PYRTR 
ID   B2WH69_PYRTR            Unreviewed;       641 AA.
AC   B2WH69;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=HRD1, HRD ubiquitin ligase complex, ER membrane component {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PTRG_09328 {ECO:0000313|EMBL:EDU42379.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU42379.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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DR   EMBL; DS231625; EDU42379.1; -; Genomic_DNA.
DR   RefSeq; XP_001939660.1; XM_001939625.1.
DR   AlphaFoldDB; B2WH69; -.
DR   EnsemblFungi; EDU42379; EDU42379; PTRG_09328.
DR   GeneID; 6347618; -.
DR   eggNOG; KOG0825; Eukaryota.
DR   HOGENOM; CLU_026721_0_0_1; -.
DR   InParanoid; B2WH69; -.
DR   OMA; DERRAWG; -.
DR   OrthoDB; 5490909at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR047157; PHRF1-like.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12618; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR12618:SF20; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          5..88
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          137..186
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          282..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  70967 MW;  6EA472A1FF70601C CRC64;
     MAETCIVCLG DLVHHDVGPT ATASPLATYP LEHGADVPHE HHAKDNKATV DSTNDDEMVA
     HLLPCGHDLH NDCLKPWVER ANSCPICRAS FNMVELSARV GGPKISEYAV QDKQQVAEID
     PSMIIEDDYI LEDDGSYDAC MVCDEFGDSS QLMYCHSCEQ LCHVFCAGLD RMPTRGPWYC
     QGCVENPALL GAASRRRPAI RGPAAWINGR SRVPRHNQAP DEWVGVWQSV WDRLQFDIEF
     PFDEEEQSEN QSDITRREDR RWEERMRVAR RAGAGNRFQI AADNVVTNRR RNSNLTARTT
     NRTLHREPPK TPKDPESQEE LRAWNQFEKA REQLAQTDAQ PAPSVASTSS RRGRKRKSVD
     YSPSDNEPCE QKPERKLKRP RTRMLIDPGE SSSAAARRNT ATHAPAAASS PTAAQNGEAS
     APAPGFLQSL LQEVEVDRFA ERDKEIAAPQ PRRIIVERAC SPPHSSPGLS PVYQQPRGMT
     TPPPLNLTRT ASPAALKDQQ PSPTYSPYSP ADDDRPSRRR LAHRSAAGLS SPPRSKDSSP
     TRPALSYSTK AELQRMVTAV LKPLYLKKEV TKQEYTDVNR DVSRLLYEKV GEAGADALAD
     QDTREKWQKM ASNEVDAAVK GLRTAGAALS PAADDSASSS S
//
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