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Database: UniProt
Entry: Q876P3_EPITY
LinkDB: Q876P3_EPITY
Original site: Q876P3_EPITY 
ID   Q876P3_EPITY            Unreviewed;       333 AA.
AC   Q876P3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870};
DE   Flags: Fragment;
GN   Name=tef1 {ECO:0000313|EMBL:AAO27892.1};
OS   Epichloe typhina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX   NCBI_TaxID=5113 {ECO:0000313|EMBL:AAO27892.1};
RN   [1] {ECO:0000313|EMBL:AAO27892.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 56429 {ECO:0000313|EMBL:AAO27892.1};
RA   Sung G.-H., Spatafora J.W.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAO27892.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 56429 {ECO:0000313|EMBL:AAO27892.1};
RX   PubMed=12532015; DOI=10.1126/science.1078155;
RA   Currie C.R., Wong B., Stuart A.E., Schultz T.R., Rehner S.A., Mueller U.G.,
RA   Sung G.H., Spatafora J.W., Straus N.A.;
RT   "Ancient tripartite coevolution in the attine ant-microbe symbiosis.";
RL   Science 299:386-388(2003).
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; AF543777; AAO27892.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q876P3; -.
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; 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; 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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:AAO27892.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:AAO27892.1}.
FT   DOMAIN          1..142
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAO27892.1"
FT   NON_TER         333
FT                   /evidence="ECO:0000313|EMBL:AAO27892.1"
SQ   SEQUENCE   333 AA;  36043 MW;  B46276979D4C99E7 CRC64;
     IKNMITGTSQ ADCAILIIAA GTGEFEAGIS KDGQTREHAL LAYTLGVKQL IVAINKMDTT
     KWSEARYQEI IKETSNFIKK VGYNPKTVAF VPISGFNGDN MLAASTNCPW YKGWEKETKA
     GKSTGKTLLE AIDSIEPPKR PTDKPLRLPL QDVYKIGGIG TVPVGRIETG VLKPGMVVTF
     APANVTTEVK SVEMHHEQLT EGNPGDNVGF NVKNVSVKDI RRGNVCGDSK NDPPMGAASF
     DAQVIVLNHP GQVGAGYAPV LDCHTAHIAC KFAEIREKID RRTGKAVEDA PKFIKSGDSA
     IVKMVPSKPM CVEAFTDYPP LGRFAVRDMR QTV
//
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