ID Q2HJN7_OSCTI Unreviewed; 459 AA.
AC Q2HJN7;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN Name=eft-2 {ECO:0000313|EMBL:AAY17223.1};
OS Oscheius tipulae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Rhabditinae;
OC Oscheius.
OX NCBI_TaxID=141969 {ECO:0000313|EMBL:AAY17223.1};
RN [1] {ECO:0000313|EMBL:AAY17223.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CEW1 {ECO:0000313|EMBL:AAY17223.1};
RX PubMed=18696027; DOI=10.1007/s00239-008-9147-8;
RA Akamine R.N., Winter C.E.;
RT "Oscheius tipulae as an example of eEF1A gene diversity in nematodes.";
RL J. Mol. Evol. 67:278-290(2008).
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|ARBA:ARBA00003982, 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}.
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DR EMBL; AY928339; AAY17223.1; -; mRNA.
DR AlphaFoldDB; Q2HJN7; -.
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 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 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:AAY17223.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:AAY17223.1}.
FT DOMAIN 5..242
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 459 AA; 50057 MW; EE4B919CE28D216D CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETAKFYVTII DAPGHRDFIK NMITGTSQAD CAVLVVACGT
GEFEAGISKN GQTREHALLA QTLGVKQMIV ACNKMDSTEP PFSEQRFEEI ITEVKSFIKK
IGYNPATIPF VPISGFNGDN MLEPSANMSW YKGWSVERKE GNASGKTLLE ALDCIIPPQR
PTDRPLRLPL QDVYKIGGIG TVPVGRAETG VIKPGMVVTF ASQNVTTEVK SVEMHHESLP
EAQPGDNVGF NVKNVSVKDI RRGSVCSDSK NDPAKESKSF TAQVIVMNHP GQIGAGYTPV
LDCHTAHIAC KFAELKEKVD RRTGKKVEDL PKFLKSGDAG IVELIPTKPL CVEAFTDYAP
LGRFAVRDMR QTVAVGVIKG VTKDDGSGGK VTKSAAKKK
//
