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Database: UniProt
Entry: Q94839_9MICR
LinkDB: Q94839_9MICR
Original site: Q94839_9MICR 
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
//
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