ID I1ZC50_9ACAR Unreviewed; 372 AA.
AC I1ZC50;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=Ef1alpha {ECO:0000313|EMBL:AFJ21831.1};
OS Apionacaridae gen. sp. AD1423.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Apionacaridae.
OX NCBI_TaxID=1111438 {ECO:0000313|EMBL:AFJ21831.1};
RN [1] {ECO:0000313|EMBL:AFJ21831.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23417682; DOI=10.1093/sysbio/syt008;
RA Klimov P.B., OConnor B.;
RT "Is permanent parasitism reversible?--critical evidence from early
RT evolution of house dust mites.";
RL Syst. Biol. 62:411-423(2013).
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; JQ000780; AFJ21831.1; -; Genomic_DNA.
DR AlphaFoldDB; I1ZC50; -.
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:AFJ21831.1};
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:AFJ21831.1}.
FT DOMAIN 1..194
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFJ21831.1"
FT NON_TER 372
FT /evidence="ECO:0000313|EMBL:AFJ21831.1"
SQ SEQUENCE 372 AA; 40938 MW; 79F91B985B019C36 CRC64;
MGKGSFKYAW VLDKLKAERE RGITIDITLW KFETSKYYVT VIDAPGHRDF IKNMITGTSQ
ADVAVLIVAA GTGEFEAGIS KNGQTREHAL LAYTLGVKQL IVGVNKMDTT EPPFSQSRFE
EIQKEVSAYV KKIGYNPATV AFVPISGWNG DNMLEPSPNM SWFKGWTIER KGQKLDGKTL
LDALNAQEPP TRPTDKPLRL PLQDVYKISG IGTVPVGRVE TGILKLGAVV TFAPAGITTE
VKSIEMHHET LQEALPGDNV GFNVKNVSVK ELRRGYVTGD SKDNPPKGCE EFTAQVIVLN
HPGQISNGYT PVLDCHTAHI ACKFKEIKEK CDRRSGKKLE DMPKSIKSGD AAIIDLAPTK
PMCVETFMEF PP
//
