EF1A_ASPOR
ID EF1A_ASPOR Reviewed; 460 AA.
AC Q9Y713; Q2U6V5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=tef1; Synonyms=tef; ORFNames=AO090120000080;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KBN616;
RX PubMed=9720204; DOI=10.1007/s002530051260;
RA Kitamoto N., Matsui J., Kawai Y., Kato A., Yoshino S., Ohmiya K.,
RA Tsukagoshi N.;
RT "Utilization of the TEF1-alpha gene (TEF1) promoter for expression of
RT polygalacturonase genes, pgaA and pgaB, in Aspergillus oryzae.";
RL Appl. Microbiol. Biotechnol. 50:85-92(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE62710.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007770; BAA76296.1; -; Genomic_DNA.
DR EMBL; AP007166; BAE62710.1; ALT_SEQ; Genomic_DNA.
DR PIR; T43894; T43894.
DR RefSeq; XP_001823843.2; XM_001823791.2.
DR AlphaFoldDB; Q9Y713; -.
DR SMR; Q9Y713; -.
DR STRING; 510516.Q9Y713; -.
DR PRIDE; Q9Y713; -.
DR EnsemblFungi; BAE62710; BAE62710; AO090120000080.
DR GeneID; 5996102; -.
DR KEGG; aor:AO090120000080; -.
DR VEuPathDB; FungiDB:AO090120000080; -.
DR OMA; AIRDMGM; -.
DR Proteomes; UP000006564; Chromosome 5.
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; Reference proteome.
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_0000090953"
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; 50067 MW; A0CC3805BDC0CAC7 CRC64;
MGKEDKQHIN IVVIGHVDSG KSTTTGHLIY KCGGIDQRTI EKFEKEAAEL GKGSFKYAWV
LDKLKSERER GITIDIALWK FQTSKYEVTV IDAPGHRDFI KNMITGTSQA DCAILIIASG
TGEFEAGISK DGQTREHALL AFTLGVRQLI VALNKMDTCK WSQDRYNEIV KETSNFIKKV
GYNPKSVPFV PISGFNGDNM IEASTNCPWY KGWEKETKAG KSTGKTLLEA IDAIEPPVRP
TDKPLRLPLQ DVYKISGIGT VPVGRVETGV IKPGMVVTFA PANVTTEVKS VEMHHQQLQA
GNPGDNVGFN VKNVSVKEVR RGNVAGDSKN DPPAGCDSFN AQVIVLNHPG QVGNGYAPVL
DCHTAHIACK FAELLEKIDR RTGKSVEDKP KFIKSGDAAI VKMIPSKPMC VESFTDFPPL
GRFAVRDMRQ TVAVGVIKSV EKNTGGSGKV TKAAQKAGKK
