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Database: UniProt
Entry: A0A0P1B9I3_9BASI
LinkDB: A0A0P1B9I3_9BASI
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ID   A0A0P1B9I3_9BASI        Unreviewed;      1188 AA.
AC   A0A0P1B9I3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-NOV-2023, entry version 34.
DE   SubName: Full=Translation elongation factor 2 {ECO:0000313|EMBL:CEH12320.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH12320.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH12320.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCYA01000149; CEH12320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1B9I3; -.
DR   STRING; 401625.A0A0P1B9I3; -.
DR   OrthoDB; 166721at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd04096; eEF2_snRNP_like_C; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16268; EF2_II; 1.
DR   CDD; cd16261; EF2_snRNP_III; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 2.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:CEH12320.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:CEH12320.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845}.
FT   DOMAIN          9..297
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          206..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..908
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1188 AA;  130952 MW;  D45D18EC39B9EA2E CRC64;
     MSSKKFGTAN VRCATLIGHV DHGKSSYADS LLAANGIIAP RQAGKLRYLD SREDEQERGI
     TMESSAVSLS FKLRAHSTDG KVGEISDYMI NLIDTPGHID FSSEVSTASR LCDGALVIVD
     VVEGVCTQTI AVLRQAWMDR LAPILVLNKM DRLVTELRLS PSEAYHHLTQ LIENVNAVMG
     SFFASERMED DLRWHEAREA RLKARKEAAS ESVVGQSSSD TNGHDALGEQ EDEERYQELD
     DEDIYFDPAR GNVIFASAID NWAFRLDRFS QLYSKKLGIQ ESKFRKVLWG DFFFDPKGKR
     VIGHKQKERE GKNLKPVFVQ FVLDNVWAVY ESALNRDQEK IEKIVKTLEL KILPRDLRAK
     ESSTLLPLIF SQWLPLAACT FSALVQCVPP PAVAQRTRVA KMLHPELSYF SKKEALTPLE
     VDLFEARAGD GARTCAYVSK LFAVRRGELP EGRRKELTAD EMRQKGKEAR ERAAAAKEAL
     LRATGASEAQ GSEHASSPQP EAHKTEEGTV IENGQAGPSA RELAQRDEDE NQARKDEEVV
     LGFARLYSGV LQVGRKVFAL LPKYNPALKA GHAANAKHIR EVNIEALYMM MGRDLIAVSE
     VPAGNVFAIR GLEGTVLRNA TLCAPPVQKG SPVTQELDVA SSGDCFVNLA GVGLGSAPIV
     RVALEPSRPT DMPKLVEGLR LLNQADPCVE TLVQETGEHV ILCAGELHLE RCLKDLRERF
     AKCAIQASKP LVPFRETAVK GQEMPPPKIE GAARGTMQGS LSGGVVSYSI RAVPLPEKVT
     DFLIANARTI RQLVSTDRRH GATNAGQETV ETIAGSNASE VEAASREVRP QNFWSELTKL
     LDSCGPQWRG VVDQIWSLGP RRIGPNLLVD SASLLAQRLR QRTELRKGPL KESQPASGVS
     TPAGQGAQLT GDSEVDDLAS ALEHATLPEA AEDSRTQESW TAEDLLDSIE SGFQIATLQG
     PLCAEQVQGL AYFVESVVVN HAVEEREGNR IKFSQITGSL ISSVREACRN GLLDWSPRIM
     LAMYSCDIQA STDVLGKVHA VLSRRRGRIT SEEMKEGTSF FTVGALLPVV ESFGFADGEW
     TAAQNRTELR MVSLGFFLTL QNVSLRAEIR KRTSGAASPQ LIFKGFELFD MDPYWVPRTE
     EELEDLGVLG ERENVAKKYV DNVRKRKGLF VDRRIVDAAE KQRTLKSN
//
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