ID Q5EG88_9APHY Unreviewed; 401 AA.
AC Q5EG88;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=tef1 {ECO:0000313|EMBL:AAW81761.2};
OS Fomitopsis pinicola.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fomitopsis.
OX NCBI_TaxID=40483 {ECO:0000313|EMBL:AAW81761.2};
RN [1] {ECO:0000313|EMBL:AAW81761.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MB 03-036 {ECO:0000313|EMBL:AAW81761.2};
RA Wang Z., Matheny P.B., Binder M., Hibbett D.S.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAW81761.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MB 03-036 {ECO:0000313|EMBL:AAW81761.2};
RA Matheny P.B., Hibbett D.S.;
RT "Assembling the Fungal Tree of Life.";
RL Submitted (FEB-2005) 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; AY885152; AAW81761.2; -; Genomic_DNA.
DR AlphaFoldDB; Q5EG88; -.
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 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:AAW81761.2};
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:AAW81761.2}.
FT DOMAIN 1..225
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAW81761.2"
FT NON_TER 401
FT /evidence="ECO:0000313|EMBL:AAW81761.2"
SQ SEQUENCE 401 AA; 43703 MW; F14DC7571242C688 CRC64;
VDSGKSTTTG HLIYKCGGID KRTIEKFEKE AAELGKGSFK YAWVLDKLKA ERERGITIDI
ALWKFETPKF VVTVIDAPGH RDFIKNMITG TSQADCAVLI IAAGTGEFEA GISKDGQTRE
HALLAFTLGV RQLIVAINKM DTTKWSEDRF NEIVKETSTF IKKVGYNPKA VSFVPISGWH
GDNMLEESAN MPWYKGWTKE TKAGVVKGKT LLDAIDAIEP PSRPSDKPSR LPLQDVYKIG
GIGTVPVGRV ETGIIKAGMV VTFAPSNVTT EVKSVEMHHE QLEQGVPGDN VGFNVKNVSV
KDIRRGNVAS DSKNDPAKEA ASFNAQVIIL NHPGQIGAGY APVLDCHTAH IACKFAELIE
KIDRRTGKSL EASPKFVKSG DACIAKLVPS KPLCVESYNE Y
//