ID B2VWQ2_PYRTR Unreviewed; 1195 AA.
AC B2VWQ2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Ubiquitin-protein ligase E3A {ECO:0000313|EMBL:EDU41052.1};
GN ORFNames=PTRG_01614 {ECO:0000313|EMBL:EDU41052.1};
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:EDU41052.1, 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; DS231615; EDU41052.1; -; Genomic_DNA.
DR RefSeq; XP_001931947.1; XM_001931912.1.
DR AlphaFoldDB; B2VWQ2; -.
DR STRING; 426418.B2VWQ2; -.
DR EnsemblFungi; EDU41052; EDU41052; PTRG_01614.
DR GeneID; 6339388; -.
DR eggNOG; KOG0941; Eukaryota.
DR HOGENOM; CLU_001858_0_0_1; -.
DR InParanoid; B2VWQ2; -.
DR OMA; PEDFHTP; -.
DR OrthoDB; 1820836at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF16558; AZUL; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EDU41052.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 840..1195
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1163
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1195 AA; 134625 MW; 9555D51A7659AB2D CRC64;
MSASKETERP RDAQYSVTDS SSASREPRVI EVHDTNRILE CSQIEKQQRF QHLVRQYLSQ
ILHGCTSAHC DTPTCLSSHQ RNASKPYRPP THLTATSLAH YLASQDNPNR GLCLNELKVA
PASFEISASL AQDPNDGIGE DYAVYPSVWQ LAQQYGHAHA GSGKSGGASG QENDSNVDIT
DAIKERQQPR KDTKALGQNL YDSFTVIYNY TKQIPTPASV LASLRTNHDA VGPDTSPTER
SAVPATRTVA ETITNGASDA ARDRKLTRRH SQSKYTAYED SRTGNSAVET LGSGQQVHKI
PYHPPRSGQR SLTTDTGTPD DDSTSAMLSI SKTGKKSFTI GGTSPCVNKT PKPSVAAGHD
STQVPETLGV PVITNLNCDI LDQFKELVCR RTDWSRHSDY VVDYDSRRRT RRTKPMVNRS
LFYTLSDAET LLASFHETDQ AFKDSPLPHL DSSHLANSFQ DWNRLNGALM FDALCLALEA
LLTSPPELAV HKSPRLRPSR KGASADSSLE QSPGSQKKTT ATKRYLSTHE AAHIVMICIH
ALTSLVPIGW PNTWAQIRKF RSWGIFVPSG ALDSDAFTDP YMEITDELEY EPALRLTERL
LRAIGTRTCY EHILSTLKDE DLYHGEEEPA NSDETLIDVV VHHLIVVERV ALAKKQKMTS
NLDPSADPGW TVTATFMEWL RTVIIKRWDT KAEINKWGTV GTAVMTLAEF HSKYASLNLL
PKMFEMRIFN ERLDTVTEPV KFLSWKNQPN KLHLLQYPFF FLPRQLVGYF RIINFTEMMK
HYDHTLHTTH MRRSLGLFHG QFHVDVLADR LNVTLSEQLI LDVSRENPLK DTLDQLWGQD
KRMLLKPLKV RMGREEGEVG QDHGGVTYEF FRVVLGEAFQ PENGMFTIDP ETRMMWFQPY
SLEPCWKFEM LGILFSLAVY NGITLPVTFP LAFYNYLWTN GYTVSNPMTL TERISFISDG
WPTLAKGFEQ LLTWPDPNVE DIFSLDSVFP YQVYGQRYAH NLAHFFTHSA TPPPEDNLPN
LDAAPVTNEN REEYIDNYIT TLTHASISPQ LSAFNKGFRT CISPPSLSLF TPTSLRNLIE
GNTHISLTDL KRCVRYEDGY TPTHSTIRMF WDIVERYDQD DARRLLEFVT ASDRVPVTGY
ESITFAIHKI GGAPRSLPSS STCFGKLYLP EYESREGMEG KLGLAIRNSR GFGVV
//
