ID A0A3Q7ULK5_VULVU Unreviewed; 461 AA.
AC A0A3Q7ULK5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN Name=LOC112930131 {ECO:0000313|RefSeq:XP_025868195.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025868195.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025868195.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025868195.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025868195.1};
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_025868195.1; XM_026012410.1.
DR AlphaFoldDB; A0A3Q7ULK5; -.
DR STRING; 9627.ENSVVUP00000037614; -.
DR Ensembl; ENSVVUT00000049391; ENSVVUP00000037614; ENSVVUG00000026886.
DR KEGG; vvp:112930131; -.
DR OMA; PSTKMSW; -.
DR OrthoDB; 5477300at2759; -.
DR Proteomes; UP000286640; Unplaced.
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:SF290; 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_025868195.1};
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_025868195.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT DOMAIN 5..242
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 461 AA; 50585 MW; F52E95813B32B32A CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTID RFEKEASEVG KGSFKYAWAL
DKLKAERERG ITIDISLWKF ETKKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVASGV
GEFESGISKN GQTREHVLLA YTLGVKQLIV AVNKMDITEP PYSSARFEEI SKEVKAYIKK
IGYNSEAVAF VPISGWHGDN MIEPSTKMSW FKGWKITRKE GNIVGMTLLE ALDSIMPPAR
PMDKPLRLPL QDVYKIGGIG TVPVGRVETG YLKPGMVVNF APCNITTEVK SVEMHHEALA
EALPGDNVGF NVKNVSVKDI RRGYVAGDSK NDPPLEVASF ISQVIILNHP GSIAVGYSPV
LDCHTAHIAC KFAELREKID RRSGKKLEDH PKALKSGDSA IVQMIPRKPM CVESFSEYPP
LGRFAVRDMR QTVAVGVIKA VEKKAATGGK ITKSATKAAK K
//