ID U5KP29_9PEZI Unreviewed; 360 AA.
AC U5KP29;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF1a {ECO:0000313|EMBL:AGT21749.1};
OS Eleutherascus lectardii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Ascodesmidaceae; Eleutherascus.
OX NCBI_TaxID=336791 {ECO:0000313|EMBL:AGT21749.1};
RN [1] {ECO:0000313|EMBL:AGT21749.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 626.71 {ECO:0000313|EMBL:AGT21749.1};
RA Hansen K., Perry B.A., Dranginis A.W., Pfister D.H.;
RT "A multi-gene phylogeny of the cup-fungus family Pyronemataceae
RT (Pezizomycetes, Ascomycota).";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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; KC109230; AGT21749.1; -; Genomic_DNA.
DR AlphaFoldDB; U5KP29; -.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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; 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; 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:AGT21749.1};
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:AGT21749.1}.
FT DOMAIN 1..210
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGT21749.1"
FT NON_TER 360
FT /evidence="ECO:0000313|EMBL:AGT21749.1"
SQ SEQUENCE 360 AA; 39559 MW; D429A7A37C3BDD04 CRC64;
CGGIDKRTIE KFEKEAAELG KGSFKYAWVL DKLKAERERG ITIDIALWKF ETPRYQVTVI
DAPGHRDFIK NMITGTSQAD CAILIIASGT GEFEAGISKD GQTREHALLA YTLGVKQLIV
AINKMDTNQW SEDRYKEIVK EVSNFIKKVG YNPKSVAFVP ISGFHGDNMI EPSTNCPWYK
GWERETKLGK YTGKTLLEAI DSIEPPSRPS DKPLRLPLQD VYKIGGIGTV PVGRVETGVI
KPGMVVTFAP AGVTTEVKSV EMHHEQLPEG LPGDNVGFNV KNVSVKEIRR GNVAGDSKND
PPKGAESFNA QVILMNHPGQ VGNGYAPVLD CHTAHIACKF AELIEKIDRR TGKSVEQAPK
//
