EF1A_AJECG
ID EF1A_AJECG Reviewed; 460 AA.
AC P40911; C0NUV4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=TEF; ORFNames=HCBG_06718;
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7642125; DOI=10.1016/0378-1119(95)00269-c;
RA Shearer G. Jr.;
RT "Cloning and analysis of cDNA encoding an elongation factor 1 alpha from
RT the dimorphic fungus Histoplasma capsulatum.";
RL Gene 161:119-123(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) 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 -!- 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; U14100; AAB17119.1; -; mRNA.
DR EMBL; GG663372; EEH04767.1; -; Genomic_DNA.
DR PIR; JC4214; JC4214.
DR AlphaFoldDB; P40911; -.
DR SMR; P40911; -.
DR STRING; 447093.P40911; -.
DR PRIDE; P40911; -.
DR EnsemblFungi; EEH04767; EEH04767; HCBG_06718.
DR VEuPathDB; FungiDB:HCBG_06718; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P40911; -.
DR OrthoDB; 1150082at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
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 2: Evidence at transcript level;
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_0000090950"
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; 50212 MW; D5B3FA36082F61CF CRC64;
MGKEDKTHIN LVVIGHVDSG KSTTTGHLIY KCGGIDSRTI EKFEKEAEEL GKKSFKYAWV
LDKLKSERER GITIDIALWK FETPKYSVTV IDAPGHRDFI KNMITGTSQA DCAILIIAAG
TGEFEAGISK DGQTREHALL AFTLGVRQLI VAINKMDTTK WSESRFNEII KEVSNFIKKV
GYNPKAVPFV PISGFEGDNM IEPSPNCTWY KGWNKETASG KSSGKTLLDA IDAIEPPTRP
TDKPLRLPLQ DVYKISGIGT VPVGRVETGV IKPGMVVTFA PSNVTTEVKS VEMHHQQLQA
GYPGDNVGFN VKNVSVKEVR RGNVAGDSKN DPPKGCESFN AQVIVLNHPG QVGAGYAPVL
DCHTAHIACK FSELIEKIDR RTGKSVENNP KFIKSGDAAI VKMVPSKPMC VEPFTDYPPL
GRFAVRDMRQ TVAVGVIKSV IKSDKTAGKV TKAAQKATKK
