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Database: UniProt
Entry: Q4TWJ7_9BASI
LinkDB: Q4TWJ7_9BASI
Original site: Q4TWJ7_9BASI 
ID   Q4TWJ7_9BASI            Unreviewed;       322 AA.
AC   Q4TWJ7;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Translation elongation factor 1-alpha {ECO:0000313|EMBL:AAY46254.1};
DE   Flags: Fragment;
GN   Name=tef1 {ECO:0000313|EMBL:AAY46254.1};
OS   Guepiniopsis buccina.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Guepiniopsis.
OX   NCBI_TaxID=160906 {ECO:0000313|EMBL:AAY46254.1};
RN   [1] {ECO:0000313|EMBL:AAY46254.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AFTOL-ID 888 {ECO:0000313|EMBL:AAY46254.1};
RX   PubMed=17081773; DOI=10.1016/j.ympev.2006.08.024;
RA   Matheny P.B., Wang Z., Binder M., Curtis J.M., Lim Y.W., Henrik Nilsson R.,
RA   Hughes K.W., Hofstetter V., Ammirati J.F., Schoch C.L., Langer E.,
RA   Langer G., McLaughlin D.J., Wilson A.W., Froslev T., Ge Z.W.,
RA   Kerrigan R.W., Slot J.C., Yang Z.L., Baroni T.J., Fischer M., Hosaka K.,
RA   Matsuura K., Seidl M.T., Vauras J., Hibbett D.S.;
RT   "Contributions of rpb2 and tef1 to the phylogeny of mushrooms and allies
RT   (Basidiomycota, Fungi).";
RL   Mol. Phylogenet. Evol. 43:430-451(2007).
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; DQ028588; AAY46254.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4TWJ7; -.
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; 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; 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:AAY46254.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:AAY46254.1}.
FT   DOMAIN          1..145
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY46254.1"
FT   NON_TER         322
FT                   /evidence="ECO:0000313|EMBL:AAY46254.1"
SQ   SEQUENCE   322 AA;  35033 MW;  244C3DEA68C198D5 CRC64;
     RDFIKNMITG TSQADCAILI IAAGTGEFEA GISKDGQTRE HALLAFTLGV RQLIVAVNKM
     DTTKWSEQRF EEIIKETSTF IKKVGYNPKS VAFVPISGWH GDNMLEESSN MPWYKGWTKE
     TKAGVVKGKT LLDAIDAIEP PQRPSDKPLR LPLQDVYKIG GIGTVPVGRV ETGVIKAGMI
     VNFAPSNVTT EVKSVEMHHE QLVEGLPGDN VGFNVKNVSV KDIRRGNVAS DSKNDPAKEA
     ASFNAQVIVL NHPGQIGAGY APVLDCHTAH IACKFAELIE KIDRRSGKTM EASPKFVKSG
     DAAIVKLIPS KPMCVESYNE YP
//
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