ID A0A1S3J7H6_LINUN Unreviewed; 461 AA.
AC A0A1S3J7H6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN Name=LOC106170554 {ECO:0000313|RefSeq:XP_013405897.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013405897.1};
RN [1] {ECO:0000313|RefSeq:XP_013405897.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013405897.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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 RefSeq; XP_013405799.1; XM_013550345.1.
DR RefSeq; XP_013405897.1; XM_013550443.2.
DR AlphaFoldDB; A0A1S3J7H6; -.
DR STRING; 7574.A0A1S3J7H6; -.
DR EnsemblMetazoa; g13742.t1; g13742.t1; g13742.
DR EnsemblMetazoa; g33524.t1; g33524.t1; g33524.
DR EnsemblMetazoa; XM_013550443.2; XP_013405897.1; LOC106170554.
DR GeneID; 106170554; -.
DR KEGG; lak:106170554; -.
DR InParanoid; A0A1S3J7H6; -.
DR OMA; VACTFES; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000085678; Unplaced.
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:SF308; ELONGATION FACTOR 1-ALPHA; 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|RefSeq:XP_013405897.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|RefSeq:XP_013405897.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 5..242
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 461 AA; 50825 MW; 250F68A46BB6810C CRC64;
MPKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRQIE KFEKEAQEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETSKYEVTII DAPGHRDFIK NMITGTSQAD CAVLIVASGT
GEFEAGISKN GQTREHALLA FTLGVKQMIV GVNKIDSTEP PYSEARFKEI CTEVSNYLKK
VGYNPKAVAM VPISGWHGDN MMEPSPNMSW YKGWAIERKE GNAKGMTLLE ALDSILPPQR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILKPGMVVTF APAMLTTEVK SVEMHHESLT
EALPGDNVGF NVKNVSVKEI RRGFVCGDSK SDPPQETAEF KAQVIVLNHP GQINAGYAPV
IDCHTAHIAC KWSELQEKID RRSGKKLEDN PKFLKSGDAG IVNMIPSKPL CVEAFSNYQP
LGRFAVRDMR QTVAVGVIKE TKKKENTGKM TKAAEKATKK K
//
