ID Q94839_9MICR Unreviewed; 445 AA.
AC Q94839;
DT 01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Elongation factor 1 alpha {ECO:0000313|EMBL:BAA06865.1};
DE Flags: Fragment;
GN Name=EF-1 alpha {ECO:0000313|EMBL:BAA06865.1};
OS Glugea plecoglossi.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Glugeidae; Glugea.
OX NCBI_TaxID=40978 {ECO:0000313|EMBL:BAA06865.1};
RN [1] {ECO:0000313|EMBL:BAA06865.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8919877; DOI=10.1007/BF02198852;
RA Kamaishi T., Hashimoto T., Nakamura Y., Nakamura F., Murata S., Okada N.,
RA Okamoto K., Shimizu M., Hasegawa M.;
RT "Protein phylogeny of translation elongation factor EF-1 alpha suggests
RT microsporidians are extremely ancient eukaryotes.";
RL J. Mol. Evol. 42:257-263(1996).
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}.
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DR EMBL; D32139; BAA06865.1; -; mRNA.
DR AlphaFoldDB; Q94839; -.
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 CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd01513; Translation_factor_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; 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; IPR004160; Transl_elong_EFTu/EF1A_C.
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; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Elongation factor {ECO:0000313|EMBL:BAA06865.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:BAA06865.1}.
FT DOMAIN 1..217
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA06865.1"
SQ SEQUENCE 445 AA; 47912 MW; 88C627E729CE046A CRC64;
STTVGNLAFQ LGAIDARKMD KLKKEAEERG RGTFSYAYVM DMSAAERERG ITITTSLMKL
ETSKHMLNVI DCPGHQDFIK NMVTGAAQAD VGVVLVPCAT GEFESCISGG TLKDHIMISG
VLGCRKLIVC VNKVDTIDEK NRISRFDEVA KEMKGIIAKS HPDKDPIIIP ISGYLGINIV
EKGDKFEWFK GWKPVSGAGD SIFTLEGALN SQIPPPRPID KPLRMPIDSI HKIPGIGMVY
TGRVSTGAIK PGMVVSSQPT GVVAEVKTLE IHKQSRAAVV SGENCGVALK AASQGNPALI
NPGHVFSNTK DSPVEIFEAA RAKIVVVAHP KGIKPGYCPT MDLGTHHVPC QITKFISKRM
PGIKEEIPSP DVVQKGENVT CIIHPQKQVV METLKEVPSL ARFALRDAGR IVGIGAIEAR
YTKAEYETEV PSTTGKGRKA TRGPG
//