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Database: UniProt
Entry: Q876P6_METAN
LinkDB: Q876P6_METAN
Original site: Q876P6_METAN 
ID   Q876P6_METAN            Unreviewed;       333 AA.
AC   Q876P6;
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:AAO27889.1};
OS   Metarhizium anisopliae (Entomophthora anisopliae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=5530 {ECO:0000313|EMBL:AAO27889.1};
RN   [1] {ECO:0000313|EMBL:AAO27889.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ARSEF 3145 {ECO:0000313|EMBL:AAO27889.1};
RA   Sung G.-H., Spatafora J.W.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAO27889.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ARSEF 3145 {ECO:0000313|EMBL:AAO27889.1};
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; AF543774; AAO27889.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q876P6; -.
DR   VEuPathDB; FungiDB:MAN_02472; -.
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   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:AAO27889.1};
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:AAO27889.1}.
FT   DOMAIN          1..142
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAO27889.1"
FT   NON_TER         333
FT                   /evidence="ECO:0000313|EMBL:AAO27889.1"
SQ   SEQUENCE   333 AA;  36034 MW;  FF362931367D34C8 CRC64;
     IKNMITGTSQ AECAILIIAA GTGEFEAGIS KDGQTREHAL LAYTLGVKQL IVAINKMDTT
     KWSEARYQEI IKETSNFIKK VGYNPKTVAF VPISGFHGDN MLQASTNCPW YKGWEKETKA
     GKSTGKTLLE AIDAIEPPKR PTDKPLRLPL QDVYKIGGIG TVPVGRIETG ILKPGMVVTF
     APSNVTTEVK SVEMHHEQLT EGVPGDNVGF NVKNVSVKEI RRGNVAGDSK NDPPSGAASF
     DAQVIVLNHP GQVGAGYAPV LDCHTAHIAC KFSEIKEKID RRTGKAVESA PKFIKSGDSA
     IVKMVPSKPM CVEAFTDYPP LGRFAVRDMR QTV
//
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