ID Q9HG95_9FUNG Unreviewed; 417 AA.
AC Q9HG95;
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:AAG29016.1};
OS Mucor indicus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=64623 {ECO:0000313|EMBL:AAG29016.1};
RN [1] {ECO:0000313|EMBL:AAG29016.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL28634 {ECO:0000313|EMBL:AAG29016.1};
RX PubMed=11404008; DOI=10.1016/S0378-1119(01)00464-4;
RA Voigt K., Wostemeyer J.;
RT "Phylogeny and origin of 82 zygomycetes from all 54 genera of the Mucorales
RT and Mortierellales based on combined analysis of actin and translation
RT elongation factor EF-1alpha genes.";
RL Gene 270:113-120(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; AF157266; AAG29016.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HG95; -.
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:AAG29016.1};
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:AAG29016.1}.
FT DOMAIN 1..222
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAG29016.1"
FT NON_TER 417
FT /evidence="ECO:0000313|EMBL:AAG29016.1"
SQ SEQUENCE 417 AA; 45556 MW; D44D0ED5C08DA3A7 CRC64;
GKSTTTGHLI YKCGGIDKRT IEKFEKEAAE LGKGSFKYAW VLDKLKAERE RGITIDIALW
KFETPKYNVT VIDAPGHRDF IKNMITGTSQ ADCAILIIAG GTGEFEAGIS KDGQTREHAL
LAFTLGVRQL IVAINKMDTT KWSEARYNEI VKEVSSFIKK IGFNPKSVPF VPISGWHGDN
MLDESTNMPW FKGWNKETKA GSKTGKTLLE AIDAIDPPTR PVDKPLRLPL QDVYKIGGIG
TVPVGRVETG VIKAGMVVTF APAAVTTEVK SVEMHHETLT EGLPGDNVGF NVKNVSVKDI
RRGNVCSDSK NDPAKESASF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELIEKID
RRSGKKLEDA PKFVKPGDSA IVKMIPSKPM CVEAYTDYPP LGRFAVRDMR QTVAVGV
//
