ID   EF1A_PODAS              Reviewed;         460 AA.
AC   Q01520;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
GN   Name=TEF; Synonyms=AS4;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=8289244; DOI=10.1016/s0022-2836(05)80029-4;
RA   Silar P., Picard M.;
RT   "Increased longevity of EF-1 alpha high-fidelity mutants in Podospora
RT   anserina.";
RL   J. Mol. Biol. 235:231-236(1994).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X74799; CAA52806.1; -; Genomic_DNA.
DR   PIR; S43861; S43861.
DR   AlphaFoldDB; Q01520; -.
DR   SMR; Q01520; -.
DR   PRIDE; Q01520; -.
DR   VEuPathDB; FungiDB:PODANS_1_19720; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Gene3D; 3.40.50.300; -; 1.
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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW   Protein biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   CHAIN           2..460
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090960"
FT   DOMAIN          6..241
FT                   /note="tr-type G"
FT   REGION          15..22
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          71..75
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          92..95
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          154..157
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          193..195
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..96
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N,N,N-trimethylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         3
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         3
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         31
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         80
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         317
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         317
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
FT   MOD_RES         391
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02994"
SQ   SEQUENCE   460 AA;  49852 MW;  B17A0991589AAC3B CRC64;
     MGKEDKTHIN VVVIGHVDSG KSTTTGHLIY KCGGIDKRTI EKFEKEAAEL GKGSFKYAWV
     LDKLKAERER GITIDIALWK FETPKYYVTV IDAPGHRDFI KNMITGTSQA DCAILIIAAG
     TGEFEAGISK DGQTREHALL AYTLGVKQLI VAINKMDTTK WSEARFNEII KETSNFIKKV
     GYNPKTVAFV PISGFNGDNM LEASTNCPWY KGWEKEVKGG KATGKTLLEA IDSIEPPKRP
     TDKPLRLPLQ DVYKIGGIGT VPVGRIETGI LKPGMVVTFA PSNVTTEVKS VEMHHEQLAE
     GVPGDNVGFN VKNVSVKEIR RGNVAGDSKN DPPMGAASFD AQVIVLNHPG QVGAGYAPVL
     DCHTAHIACK FSELLQKIDR RTGKAVEESP KFIKSGDAAI VKMVPSKPMC VEAFTEYPPL
     GRFAVRDMRQ TVAVGVIKKV EKAAAGSGKV TKSAAKAGKK