ID D9IQ85_9ACAR Unreviewed; 352 AA.
AC D9IQ85;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=Ef1alpha100E {ECO:0000313|EMBL:ADJ53274.1};
OS Proctophyllodes ciae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Proctophyllodidae; Proctophyllodinae; Proctophyllodes.
OX NCBI_TaxID=799884 {ECO:0000313|EMBL:ADJ53274.1};
RN [1] {ECO:0000313|EMBL:ADJ53274.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AD815 {ECO:0000313|EMBL:ADJ53274.1};
RX PubMed=21554840; DOI=10.1017/S003118201100031X;
RA Knowles L.L., Klimov P.B.;
RT "Estimating phylogenetic relationships despite discordant gene trees across
RT loci: the species tree of a diverse species group of feather mites (Acari:
RT Proctophyllodidae).";
RL Parasitology 138:1750-1759(2011).
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; HM165120; ADJ53274.1; -; Genomic_DNA.
DR AlphaFoldDB; D9IQ85; -.
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; 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; 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:ADJ53274.1};
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:ADJ53274.1}.
FT DOMAIN 1..186
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADJ53274.1"
FT NON_TER 352
FT /evidence="ECO:0000313|EMBL:ADJ53274.1"
SQ SEQUENCE 352 AA; 38631 MW; 5EA69D521BFA8F3A CRC64;
AWVLDKLKAE RERGITIDIT LWKFETPKYY VTVIDAPGHR DFIKNMITGT SQADVAVLIV
AAGTGEFEAG ISKNGQTREH ALLAYTLGVK QLIVGVNKMD TTEPPFSQSR FEEIQKEVSA
YVKKIGYNPA TVAFVPISGW NGDNMLEPST NMTWFKGWTI ERKGQKFEGK TLLQALDAQE
PPTRPTDKPL RLPLQDVYKI GGIGTVPVGR VETGVLKPGM VVTFAPAGIT TEVKSVEMHH
EALQEAVPGD NVGFNVKNVS VKELRRGYVA GDSKDNPPKG CEEFTAQVIV LNHPGQISNG
YTPVLDCHTA HIACKFKEIK EKCDRRSGKK LEDMPKSIKS GDAAIIDLAP TK
//
