ID Q6L8Q1_9PEZI Unreviewed; 457 AA.
AC Q6L8Q1;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
GN Name=tef1 {ECO:0000313|EMBL:BAD21144.1};
OS Rosellinia sp. PF1022.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=241238 {ECO:0000313|EMBL:BAD21144.1};
RN [1] {ECO:0000313|EMBL:BAD21144.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PF1022 {ECO:0000313|EMBL:BAD21144.1};
RX PubMed=15184904; DOI=10.1038/nbt978;
RA Yanai K., Sumida N., Okakura K., Moriya T., Watanabe M., Murakami T.;
RT "Para-position derivatives of fungal anthelmintic cyclodepsipeptides
RT engineered with Streptomyces venezuelae antibiotic biosynthetic genes.";
RL Nat. Biotechnol. 22:848-855(2004).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|RuleBase:RU000325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC ECO:0000256|RuleBase:RU000325}.
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DR EMBL; AB116235; BAD21144.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6L8Q1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:BAD21144.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:BAD21144.1}.
FT DOMAIN 4..237
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 457 AA; 49882 MW; 9F28481048C25E82 CRC64;
MSTKAHLNVV VIGHVDSGKS TTTGHLIYQC GGIDKRTIEK FEKEAAELGK GSFKYAWVLD
KLKAERERGI TIDIALWKFE TPKYYVTVID APGHRDFIKN MITGTSQADC AILIIAAGTG
EFEAGISKDG QTREHALLAF TLGVKQLIVA INKMDTAQWA EARYNEIVKE TSSFIKKVGF
NPKHVAFVPI SGFNGDNMLE VTKNASWYKG WEKESPKGAK ISGKTLLDAI DAIEEPKRAN
DKPLRLPLQD VYKIGGIGTV PVGRIETGEL KPGMVVTFAP AMVTTEVKSV EMHHQQLEKG
NPGDNVGFNV KNVSVKDIRR GNVAGDSKND PPYGAESFNA QVIVLNHPGQ VGAGYAPVLD
CHTAHIACKF SELLEKIDRR TGKSVEANPK FVKSGDAAIV KMVPSKPMCV EAFTDYPPLG
RFAVRDMRQT VAVGVIKSVE KDTKVKGKET KSATKKK
//
