ID   EF1A_SORMA              Reviewed;         460 AA.
AC   Q09069;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
GN   Name=TEF;
OS   Sordaria macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=5147;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OOO;
RX   PubMed=9454646; DOI=10.1006/fgbi.1997.1012;
RA   Gagny B., Rossignol M., Silar P.;
RT   "Cloning, sequencing, and transgenic expression of Podospora curvicolla and
RT   Sordaria macrospora eEF1A genes: relationship between cytosolic translation
RT   and longevity in filamentous fungi.";
RL   Fungal Genet. Biol. 22:191-198(1997).
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; X96615; CAA65435.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q09069; -.
DR   SMR; Q09069; -.
DR   PRIDE; Q09069; -.
DR   VEuPathDB; FungiDB:SMAC_05446; -.
DR   OMA; AIRDMGM; -.
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_0000090970"
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;  49805 MW;  E187C23581CAB47D CRC64;
     MGKEDKAHIN VVVIGHVDSG KSTTTGHLIY KCGGIDKRTI EKFEKEAAEL GKGSFKYAWV
     LDKLKAERER GITIDIALWK FETPKYYVTV IDAPGHRDFI KNMITGTSQA DCAILIIAAG
     TGEFEAGISK DGQTREHALL AYTLGVKQLI VAINKMDTTQ WSQARFEEII KETKNFIKKV
     GYNPATVAFV PISGFNGDNM LEASTNCPWY KGWEKETKAG KSTGKTLLEA IDAIEQPKRP
     TDKPLRLPLQ DVYKIGGIGT VPVGRIETGV LKPGMVVTFA PSNVTTEVKS VEMHHEQLAQ
     GVPGDNVGFN VKNVSVKDIR RGNVAGDSKN DPPVGAASFT AQVIVLNHPG QVGAGYAPVL
     DCHTAHIACK FAELLEKIDR RTGKAVETSP KFIKSGDAAI VKMIPSKPMC VEAFTDYPPL
     GRFAVRDMRQ TVAVGVIKAV DKTQAVAGKV TKSAAKAAKK