ID   Q9HG59_9FUNG            Unreviewed;       426 AA.
AC   Q9HG59;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE   Flags: Fragment;
GN   Name=EF-1alpha {ECO:0000313|EMBL:AAG29053.1};
OS   Zychaea mexicana.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Zychaea.
OX   NCBI_TaxID=64656 {ECO:0000313|EMBL:AAG29053.1};
RN   [1] {ECO:0000313|EMBL:AAG29053.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL6237 {ECO:0000313|EMBL:AAG29053.1};
RA   O'Donnell K.L., Cigelnik E.;
RT   "Molecular Phylogeny of the Mucorales.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAG29053.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL6237 {ECO:0000313|EMBL:AAG29053.1};
RA   O'Donnell K., Lutzoni F.M., Ward T.J., Benny G.L.;
RT   "Evolutionary relationships among mucoralean fungi (Zygomycota): evidence
RT   for family polyphyly on a large scale. [Erratum: July/Aug 2001, v. 93 (4),
RT   p. 814.";
RL   Mycologia 93:286-297(2001).
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; AF157303; AAG29053.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HG59; -.
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; IPR009001; Transl_elong_EF1A/Init_IF2_C.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
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:AAG29053.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW   ECO:0000313|EMBL:AAG29053.1}.
FT   DOMAIN          1..231
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAG29053.1"
FT   NON_TER         426
FT                   /evidence="ECO:0000313|EMBL:AAG29053.1"
SQ   SEQUENCE   426 AA;  46394 MW;  97A0C42CD5EE67B8 CRC64;
     VVVIGHVDSG KSTTTGHLIY KCGGIDKRTI EKFEKEAAEL GKGSFKYAWV LDKLKAERER
     GITIDIALWK FETPKYHVTV IDAPGHRDFI KNMITGTSQA DCGILIIAAG TGEFEAGISK
     DGQTREHALL AFTLGVRQLI VAINKMDSTK YSEARYNEIV KEVSTFIKKI GFNPKSVPFV
     PISGWNGDNM LDESPNMPWF KGWNKETKAG AKSGKTLLEA IDSIDPPVRP SDKPLRLPLQ
     DVYKIGGIGT VPVGRVETGV IKAGMVVTFA PANVTTEVKS VEMHHEQLVE GVPGDNVGFN
     VKNVSVKDIR RGNVCSDSKN DPAKEAASFT AQVIVLNHPG QIGSGYSPVL DCHTAHIACK
     FSELLEKVDR RSGKKLEDAP KFVKSGDSAI VKMVPSKPMC VEAYTEYPPL GRFAVRDTRQ
     TVAVGV
//