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Elongation factor 1-alpha (Fragment)

 Q4PS64_GANTS            Unreviewed;       379 AA.
Q4PS64;
19-JUL-2005, integrated into UniProtKB/TrEMBL.
19-JUL-2005, sequence version 1.
22-NOV-2017, entry version 55.
RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
Flags: Fragment;
Name=tef1 {ECO:0000313|EMBL:AAY62530.1};
Ganoderma tsugae (Hemlock varnish shelf mushroom) (Polyporus tsugae).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Polyporales; Polyporaceae; Ganoderma.
NCBI_TaxID=34467 {ECO:0000313|EMBL:AAY62530.1};
[1] {ECO:0000313|EMBL:AAY62530.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AFTOL-ID 771 {ECO:0000313|EMBL:AAY62530.1};
Matheny P.B., Binder M., Hibbett D.S.;
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AAY62530.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AFTOL-ID 771 {ECO:0000313|EMBL:AAY62530.1};
PubMed=17081773; DOI=10.1016/j.ympev.2006.08.024;
Matheny P.B., Wang Z., Binder M., Curtis J.M., Lim Y.W.,
Henrik Nilsson R., Hughes K.W., Hofstetter V., Ammirati J.F.,
Schoch C.L., Langer E., Langer G., McLaughlin D.J., Wilson A.W.,
Froslev T., Ge Z.W., Kerrigan R.W., Slot J.C., Yang Z.L., Baroni T.J.,
Fischer M., Hosaka K., Matsuura K., Seidl M.T., Vauras J.,
Hibbett D.S.;
"Contributions of rpb2 and tef1 to the phylogeny of mushrooms and
allies (Basidiomycota, Fungi).";
Mol. Phylogenet. Evol. 43:430-451(2007).
-!- FUNCTION: This protein promotes the GTP-dependent binding of
aminoacyl-tRNA to the A-site of ribosomes during protein
biosynthesis. {ECO:0000256|RuleBase:RU000325}.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
subfamily. {ECO:0000256|RuleBase:RU000325}.
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EMBL; DQ059048; AAY62530.1; -; Genomic_DNA.
ProteinModelPortal; Q4PS64; -.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
InterPro; IPR004161; EFTu-like_2.
InterPro; IPR031157; G_TR_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR009000; Transl_B-barrel_sf.
InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
Pfam; PF00009; GTP_EFTU; 1.
Pfam; PF03144; GTP_EFTU_D2; 1.
Pfam; PF03143; GTP_EFTU_D3; 1.
PRINTS; PR00315; ELONGATNFCT.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00483; EF-1_alpha; 1.
PROSITE; PS00301; G_TR_1; 1.
PROSITE; PS51722; G_TR_2; 1.
3: Inferred from homology;
Elongation factor {ECO:0000256|RuleBase:RU000325,
ECO:0000313|EMBL:AAY62530.1};
GTP-binding {ECO:0000256|RuleBase:RU000325};
Nucleotide-binding {ECO:0000256|RuleBase:RU000325};
Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
ECO:0000313|EMBL:AAY62530.1}.
DOMAIN 1 212 Tr-type G. {ECO:0000259|PROSITE:PS51722}.
NON_TER 1 1 {ECO:0000313|EMBL:AAY62530.1}.
NON_TER 379 379 {ECO:0000313|EMBL:AAY62530.1}.
SEQUENCE 379 AA; 41479 MW; 8D1D6C864BB12590 CRC64;
YKCGGIDKRT IEKFEKEAAE LGKGSFKYAW VLDKLKAERE RGITIDIALW KFETPKFMVT
VIDAPGHRDF IKNMITGTSQ ADCAILIIAA GTGEFEAGIS KDGQTREHAL LAFTLGVRQL
IVAVNKMDTT KWSEDRFNEI IKETSTFIKK VGYNPKAVAF VPISGWHGDN MLEESSNMTW
YKGWTKETKA GVVKGKTLLD AIDAIEPPVR PSDKPLRLPL QDVYKIGGIG TVPVGRVETG
VIKAGMVVTF APTNVTTEVK SVEMHHEQLE QGLPGDNVGF NVKNVSVKDI RRGNVASDSK
NDPAKEAASF TAQVIILNHP GQIGAGYAPV LDCHTAHIAC KFAELIEKID RRTGKSIEDK
PKFVKSGDAC IAKLVPSKP


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