ID Q9HG84_9FUNG Unreviewed; 370 AA.
AC Q9HG84;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF-1alpha {ECO:0000313|EMBL:AAG29027.1};
OS Pilobolus umbonatus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Pilobolaceae; Pilobolus.
OX NCBI_TaxID=101123 {ECO:0000313|EMBL:AAG29027.1};
RN [1] {ECO:0000313|EMBL:AAG29027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL6349 {ECO:0000313|EMBL:AAG29027.1};
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:AAG29027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL6349 {ECO:0000313|EMBL:AAG29027.1};
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; AF157277; AAG29027.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HG84; -.
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 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; 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; 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:AAG29027.1};
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:AAG29027.1}.
FT DOMAIN 1..227
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAG29027.1"
FT NON_TER 370
FT /evidence="ECO:0000313|EMBL:AAG29027.1"
SQ SEQUENCE 370 AA; 40282 MW; A940FCA6283196BF CRC64;
GHVDSGKSTT TGHLIYKCGG IDKRTIEKFE KEASELGKGS IKYAWVLDKL KAERERGITI
DIALWKFETP KYNVTVIDAP GHRDFIKNMI TGTSQADCAI LIIAGGTGEF EAGISKDGQT
REHCLLAFTL GVRQLIVAIN KMDTTKWSEA RYNEIVKEVS SFIKKIGFNP KAVPFVPISG
WHGDNMLEES KNMPWFKGWT KESKAGNKAG KTLLEAIDAI EPPSRPSDKP LRLPLQDVYK
IGGIGTVPVG RVETGVIKAG MVVTFAPAAV TTEVKSVEMH HETLTEGLPG DNVGFNVKNV
SVKDIRRGNV CSDSKNDPAK EAGSFTAQVI ILNHPGQIGA GYAPVLDCHT AHIACKFAEL
LEKIDRRSGK
//