ID E5A6U7_LEPMJ Unreviewed; 743 AA.
AC E5A6U7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=LEMA_P085810.1 {ECO:0000313|EMBL:CBX99342.1};
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:CBX99342.1, 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).
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
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DR EMBL; FP929135; CBX99342.1; -; Genomic_DNA.
DR RefSeq; XP_003842821.1; XM_003842773.1.
DR AlphaFoldDB; E5A6U7; -.
DR STRING; 985895.E5A6U7; -.
DR EnsemblFungi; CBX99342; CBX99342; LEMA_P085810.1.
DR GeneID; 13288894; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_3_3_1; -.
DR InParanoid; E5A6U7; -.
DR OMA; XCEPVEL; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 219..437
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 41..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 82281 MW; 71A1EEDC1F1C484A CRC64;
MTKAQKEAKA KNELRLKQML EVGEAKVAGL EEPEVKKKPI YDDRKKRKKQ IETQKEKEAR
EAEEAAKKLA ELKLAEEQAA AAAAAAEKAR LDAETKKGDD DDAAEDWEAE ADELDGVKDS
WDIDTDEEEE RKATAKKAKE EKMAAEKAAA EKEPQFKDTK AKSDFDSDSD SEEDSEDDSS
EDEQGTATQR AEAARKAAAA ERRKQAHEEA LAARSKDNLR SPICCILGHV DTGKTKLLDK
IRQTNVQEGE AGGITQQIGA TYFPVEALEK KVAVVNKDKS FVFNVPGLLV IDTPGHESFT
NLRSRGSSLC NIAILVIDIM HGLEPQTIES MKLLRDRKTP FIVALNKIDR LFGWKKIDNN
GFEDSFNLQK QAVQSEFEER WTFVRTQLQE QGFNSELFFK NKNMAKYVSV CPTSAHTGEG
IPDMIKLIVR LTQERLTNNL MYLSEVECTV LEVKVIEGLG TTIDVILSNG VLHEGDRIVL
CGNPEPIVTN IRALLTPAEM KELRVKSQYV HNKEVKAAMG IKIAADGLDQ AIAGSRLLVV
GPNDDEEDLM DEVMGDLAHL LSKVSKTGRG VSVQASTLGS LEALLEFLRV SKIPVATISI
GPVFKKDVLR AGVMLEKAKE YAVMLCFDVK VDKDAKAYAE EIGVKIFEAD IIYHLFDKFT
AHMKQLEEQR KEESKMLAVF PCVLRPVAVF NKKDPIVIGV DVTDGNLKIT TPICAVKKNP
ATGVKEIIQL GRVYVPTSAL PII
//
