ID E3RJJ0_PYRTT Unreviewed; 1009 AA.
AC E3RJJ0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=EF1G-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PTT_08317 {ECO:0000313|EMBL:EFQ94101.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ94101.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94101.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; GL533501; EFQ94101.1; -; Genomic_DNA.
DR RefSeq; XP_003297795.1; XM_003297747.1.
DR AlphaFoldDB; E3RJJ0; -.
DR STRING; 861557.E3RJJ0; -.
DR EnsemblFungi; EFQ94101; EFQ94101; PTT_08317.
DR KEGG; pte:PTT_08317; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR HOGENOM; CLU_011637_0_0_1; -.
DR OrthoDB; 159792at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:InterPro.
DR CDD; cd07735; class_II_PDE_MBL-fold; 1.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR000396; Pdiesterase2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR PANTHER; PTHR43986:SF13; GLUTATHIONE S-TRANSFERASE AN1595-RELATED; 1.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR Pfam; PF02112; PDEase_II; 2.
DR PRINTS; PR00388; PDIESTERASE2.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW ProRule:PRU00519};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 87..212
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 252..413
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 219..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 110413 MW; AB9A7CB41839177D CRC64;
MSFGKLYSYS GNPRTTSLLA VAKENGLDIE FVETEPAKGV STEYLKLNKL GKVPTFEGAD
GFVLSECIAI AVYLASQNEK TSLLGKTKQD YATILRWMSF ANTEVLSPLG GWFRPILGRD
PYNKKNVEES QKAALKAVHV IEEHLLTHTY LVGERLTLAD IFAASILARG FQFFFDKQWR
DSNPNVTRWY ETIYNQSSYS AVAPKFEFIT EALKNVAPKK EGGEKKKETP KAAPKPKEEA
EEEEEAAPAP KPKHPLEALP KATFVLDDWK RKYSNEETRE VALPWFWENA NFEEYSIYKV
DYKYNDELTL TFMTANLIGG FFTRLEASRK YLFGCCSVYG TANDSIIKGA FVVRGQEALP
AFDVAPDVES YEFTKLDPTK EEDREFVNDQ WSWDKPLVVG DKSYEWADGK GSGGGPSEDN
VTGFLVRSTA TQWAKNSVIA VDAGSHLASI TRILAKDFPL VSDPDPPLPP SRNDNANSNG
AYDHSESPSP GAAPVSPSDD ESEADTPNSE KELPVTITTL KHGAFAGLPF PHQSARANAL
HVVREHISTY LITHPHLDHL SGFVINTAAF HNTSRPKRLA ALPFTVNAIK THIFNNVIWP
NLTDEDGGVG LVTFQRLAEG GNIALGEGSG RGFIEVCDGL GVKGFKVSHG HCMQGPGHVH
RGSNANLLET SSAQHPTSGH QLDGQDGRSM SFSYTSQSAP GTPGLSGADT GRRASGTTVP
PPQQSSEDHC VIDSTAYFIR TESTPTTPKR EILIFGDVEP DSLSLSPRTS QIWSEAAPKI
ASGILTGIFI EVSYTNAQSD AVLFGHLAPR HLLEELCVLG DMVKERKKET EREKEEGRIR
KKRKRASNTL QLDGLGEKDR GKRLGVPKGI DSPISSTNQN ININNDDDGM SDYPTSRGET
GTHTPNPLPS SHHQRTSDPH VSHPSAPAAL NLSSVSAEHS RAILSAAFDS PLKGIKIVII
HVKDTFTDGP LVGDQILKEL REGEATLQEQ GRGLGCQFEV SVAGGSYWF
//
