ID A0A0D7AML7_9AGAR Unreviewed; 412 AA.
AC A0A0D7AML7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Elongation factor 1-alpha {ECO:0000313|EMBL:KIY52556.1};
GN ORFNames=FISHEDRAFT_63767 {ECO:0000313|EMBL:KIY52556.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY52556.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY52556.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY52556.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KN881640; KIY52556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AML7; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
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; cd01883; EF1_alpha; 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; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
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; 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 PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:KIY52556.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:KIY52556.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT DOMAIN 5..240
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 412 AA; 44882 MW; 9CF6B454D8AB36EF CRC64;
MGKEKTHVNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPKFMVTVI DAPGHRDFIK NMITGTSQAD CAILIIAAGT
GEFEAGISKD GQTREHALLA FTLGVRQLIV AVNKMDTTKW SEDRFNEIVK ETSTFIKKVG
YNPKGVAFVP ISGWHGDNML EESSNMTWYK GWTKETKAGV VKGKTLLEAI DAIEPPARPS
DKPLRLPLQD VYKIGGIGTV PVARISVSAV TVPPIGTASA RITTKEAASF NAQVIILNHP
GQIGAGYAPV LDCHTAHIAC KFAELLEKID RRTGKSLEQN PKFVKSGDAC IAKLVPSKPM
CVESYNEYPP LGRFAVRDMR QTVAVGIIKS VDKTDKSAGK VTKSAEKAAK KK
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