ID A0A6A7BAN5_9PLEO Unreviewed; 1095 AA.
AC A0A6A7BAN5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Elongation factor-like 1 {ECO:0000256|ARBA:ARBA00081809};
GN ORFNames=T440DRAFT_394527 {ECO:0000313|EMBL:KAF2851475.1};
OS Plenodomus tracheiphilus IPT5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus.
OX NCBI_TaxID=1408161 {ECO:0000313|EMBL:KAF2851475.1, ECO:0000313|Proteomes:UP000799423};
RN [1] {ECO:0000313|EMBL:KAF2851475.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IPT5 {ECO:0000313|EMBL:KAF2851475.1};
RG DOE Joint Genome Institute;
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S.E., Barry K., Bills G., Bluhm B.H., Cannon C.,
RA Castanera R., Culley D.E., Daum C., Ezra D., Gonzalez J.B., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B.G., Goodwin S.B., Spatafora J.W.,
RA Crous P.W., Grigoriev I.V.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; MU006302; KAF2851475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A7BAN5; -.
DR OrthoDB; 364892at2759; -.
DR Proteomes; UP000799423; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:TreeGrafter.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0042256; P:cytosolic ribosome assembly; IEA:TreeGrafter.
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 FunFam; 3.30.70.240:FF:000006; Elongation factor like GTPase 1; 1.
DR FunFam; 3.90.1430.10:FF:000002; Elongation factor like GTPase 1; 1.
DR FunFam; 3.30.70.870:FF:000002; Translation elongation factor 2; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
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; IPR053905; EF-G-like_DII.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR056752; EFL1.
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.
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; PF22042; EF-G_D2; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF25118; EFL1; 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; 2.
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KAF2851475.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000799423};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT DOMAIN 17..221
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 851..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 120567 MW; D898DD569684370C CRC64;
MVVVAPDKLV TLQRSPETIR NICVLAHVDH GKTSLTDALI ATNGIISPKL AGKIRYLDSR
PDEQLRGITM ESSAISLYFS LLRRPAPEAQ PEHKEFLINL IDSPGHIDFS YEVSTASRLC
DGAIVLVDAV EGVCSQTVTV LRQTWIEKLK PLLVINKMDR LITELKMSPG EAYTHLSKLL
EQVNAVMGSF YQGERMEDDA RWREKMEERL NAVAEEKTDS RDTRVSNLID NADGIDTTST
PAEYEEKDDE DIYFAPEKNN VIFGSAIDGW AFTVKQFAGL YERKLGIKRS VLEKVLWGDF
YLDTKTKRVL SSKHLKGRHL KPMFVQLVLE NIWAIYEATT GGNNGKGDPT MVEKITKSLN
ITLPAHIMRS RDPRALLMAL FAAWLPLSTA LLVSVTEYLP PPTKAQAERI PEILDSSPGA
DYVAPEIRNA MTGFKTDGDA PVVAYVSKMI SVPDSELPQN KRRGGALTAE EAREMGRKKR
AEIARQQAAN AEDGDMHSVT DALSSAAIGE TETPEEEIPE DKGEVEHLIG FARIFSGTLS
VGDEVYVLGP KFTPANPHAA PEPQKVKVTA LYLMMGRGLE PLTSVPAGVV FGIGGLEGHM
LKSGTLCSQL PGSPNLAGVQ MGTQPIVRVA LEPENPYDLD KMIKGLKLLV QSDPCAEYEQ
LPSGEHVILT AGELHLERCL KDLRERFAKC EIQAGEPIVP YRESIVAAAE MNPPKDPSLP
RGTVVGETAS KHVSVRLRVR PLPPSVTEFL GKNAGAIRRL YSERRGEEEH NSPNVIAGAE
HDGMQEAEQR EVGHALDFPE FKKQLKAAFA EAKGQKEIWA DVIEKITAFG PRRVGPNILV
DATKAGICGK ALRDTESPSH DPDNNTEATS DRTITPSTFA STITYAFQLA TAQGPCCAEP
IQGIAVILED VHLTIPDDEP SHDRGRLTGE VIKAVRSAIH QGFLDWSPRM LLAMYSCEIQ
ASTDVLGRVY AVLTRRRGTI LSETLSSTSS ASTTGNQTFT ISALLPVAES FGFSDEIRKR
SSGSASPQLR FAGFEMLDED PFWVPFTEDE LEDLGELADR ENVARRYVDK VRRRKGLLVR
EVLVRDAEKQ KTLKR
//
