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Database: UniProt
Entry: A0A0A1V2A8_9HYPO
LinkDB: A0A0A1V2A8_9HYPO
Original site: A0A0A1V2A8_9HYPO 
ID   A0A0A1V2A8_9HYPO        Unreviewed;       460 AA.
AC   A0A0A1V2A8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Elongation factor 1-alpha {ECO:0000256|ARBA:ARBA00013870, ECO:0000256|RuleBase:RU000325};
GN   ORFNames=X797_003570 {ECO:0000313|EMBL:EXV03771.1};
OS   Metarhizium robertsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV03771.1, ECO:0000313|Proteomes:UP000030151};
RN   [1] {ECO:0000313|EMBL:EXV03771.1, ECO:0000313|Proteomes:UP000030151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV03771.1,
RC   ECO:0000313|Proteomes:UP000030151};
RA   Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA   Gibson D.M.;
RT   "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT   ARSEF 2575.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|RuleBase:RU000325}.
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,
CC       ECO:0000256|RuleBase:RU000325}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXV03771.1}.
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DR   EMBL; JELW01000003; EXV03771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1V2A8; -.
DR   eggNOG; KOG0052; Eukaryota.
DR   HOGENOM; CLU_007265_3_5_1; -.
DR   OrthoDB; 5477300at2759; -.
DR   Proteomes; UP000030151; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01883; EF1_alpha; 1.
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   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|RuleBase:RU000325,
KW   ECO:0000313|EMBL:EXV03771.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW   ECO:0000313|EMBL:EXV03771.1}.
FT   DOMAIN          6..241
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   460 AA;  49840 MW;  2145A33D777A2C1C CRC64;
     MGKDDKTHIN VVVIGHVDSG KSTTTGHLIY QCGGIDKRTI EKFEKEAAEL GKGSFKYAWV
     LDKLKAERER GITIDIALWK FETPKYYVTV IDAPGHRDFI KNMITGTSQA DCAILIIAAG
     TGEFEAGISK DGQTREHALL AYTLGVKQLI VAINKMDTTK WSEARYQEII KETSNFIKKV
     GYNPKTVAFV PISGFHGDNM LQASTNCPWY KGWEKETKAG KSTGKTLLEA IDAIEPPKRP
     TDKPLRLPLQ DVYKIGGIGT VPVGRIETGV LKPGMVVTFA PSNVTTEVKS VEMHHEQLTE
     GVPGDNVGFN VKNVSVKEIR RGNVAGDSKN DPPMGAASFD AQVIVLNHPG QVGAGYAPVL
     DCHTAHIACK FSEIKEKIDR RTGKAVESAP KFIKSGDSAI VKMVPSKPMC VEAFTDYPPL
     GRFAVRDMRQ TVAVGVIKSV EKAAAGSGKV TKSAAKAGKK
//
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