ID   EF1A_ENCCU              Reviewed;         471 AA.
AC   Q8SS29;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
DE   AltName: Full=Eukaryotic elongation factor 1A;
DE            Short=eEF1A;
DE   AltName: Full=Translation elongation factor 1A;
GN   Name=TEF1; OrderedLocusNames=ECU04_1100;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: GTP-binding component of the eukaryotic elongation factor 1
CC       complex (eEF1). In its active GTP-bound form, binds to and delivers
CC       aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
CC       In the presence of a correct codon-anticodon match between the
CC       aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the
CC       ribosome acts as a GTPase activator and the GTP is hydrolyzed. The
CC       inactive GDP-bound form leaves the ribosome and must be recycled by its
CC       guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before
CC       binding another molecule of aminoacyl-tRNA. Required for nuclear export
CC       of aminoacyl-tRNAs. May also be involved in translational quality
CC       control by targeting cotranslationally damaged proteins to the
CC       proteasome (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC   -!- SUBUNIT: Component of the eukaryotic elongation factor 1 complex
CC       (eEF1). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AL590444; CAD25298.2; -; Genomic_DNA.
DR   RefSeq; NP_584794.1; NM_001041144.1.
DR   AlphaFoldDB; Q8SS29; -.
DR   SMR; Q8SS29; -.
DR   STRING; 284813.Q8SS29; -.
DR   GeneID; 858942; -.
DR   KEGG; ecu:ECU04_1100; -.
DR   VEuPathDB; MicrosporidiaDB:ECU04_1100; -.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   InParanoid; Q8SS29; -.
DR   OrthoDB; 1150082at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000819; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.300; -; 1.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..471
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000383139"
FT   DOMAIN          10..239
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          75..79
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          96..99
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          156..159
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          196..198
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         96..100
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..159
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   471 AA;  51587 MW;  7668B5B4D0061DEC CRC64;
     MATKVEDDSK PRLNACFIGH VDSGKSTTVG MLSYQLGAVD KREMEKYEKE AALNNKETFY
     LAYLTDKTDA ERKRGITITT TLVNLPTEKF NINILDCPGH KDFVKNMVTG ASQADVAVVI
     VPASGFESCV GVGGMLKTHI MISGILGCEK LIVCVNKMDE IPENKRMEKF NEVSAEMLRI
     VKRSHKDKNP IIIPISAFKG INLTKKGEKF EWFKGWKEKE GSSVIYTLEE ALNYQDVPER
     HNDKPLRMPI TKVCSIAGVG KIFTGRVEYG TITPNLKITI QPAGVVGETR SVEIHNKPRS
     MIPCGENCGV ALKGGVIGEI DKVDAGHVIS ANDENKAVAY PGAKIRTIVV GRPKGLSPGY
     TPQINFGNCH SPGRIAKILS KVVGKEVHEN PENVANGENF TGIVVFQKPL VIDKMERFQN
     LAKFALMDSN GVVGIGNVME PLTRDQLLKD YGIDLNEDPK AAKKAASKKK A