ID Q9HGC9_9FUNG Unreviewed; 366 AA.
AC Q9HGC9;
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:AAG28982.1};
OS Backusella circina.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Backusellaceae; Backusella.
OX NCBI_TaxID=64653 {ECO:0000313|EMBL:AAG28982.1};
RN [1] {ECO:0000313|EMBL:AAG28982.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL2446 {ECO:0000313|EMBL:AAG28982.1};
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:AAG28982.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL2446 {ECO:0000313|EMBL:AAG28982.1};
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; AF157232; AAG28982.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HGC9; -.
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:AAG28982.1};
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:AAG28982.1}.
FT DOMAIN 1..222
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAG28982.1"
FT NON_TER 366
FT /evidence="ECO:0000313|EMBL:AAG28982.1"
SQ SEQUENCE 366 AA; 40005 MW; C09D7DE5B1495430 CRC64;
GKSTTTVHLI YKCGGIDKRT IEKFEKEAAE LGKGSFKYAW VLDKLKAERE RGITIDIALW
KFETPKYNVT VIDAPGHRDF IKNMITGTSQ ADCAILIIAG GTGEFEAGIS KDGQTREHAL
LAFTLGVRQL IVAINKMDTT KWSEARYNEI VKEVSSFIKK IGFNPKSVPF VPISGWHGDN
MLEESTNMPW FKGWNKETKA GAKTGKTLLE AIDNIEPPSR PVDKPLRLPL QDVYKIGGIG
TVPVGRVETG VIKAGMVVTF APANVTTEVK SVEMHHELLP EGGLPGDNVG FNVKNVSVKD
IRRGNVTSDS KNDPAKEAGS FTAQVIILNH PGQIGAGYAP VLDCHTAHIA CKFSELIEKI
DRRPGK
//