ID A5X903_NYCOV Unreviewed; 392 AA.
AC A5X903;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
GN Name=EF-1alpha {ECO:0000313|EMBL:ABG81373.1};
OS Nyctotherus ovalis.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Armophorea;
OC Clevelandellida; Nyctotheridae; Nyctotherus.
OX NCBI_TaxID=70075 {ECO:0000313|EMBL:ABG81373.1};
RN [1] {ECO:0000313|EMBL:ABG81373.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16760419; DOI=10.1093/molbev/msl032;
RA Zufall R.A., McGrath C.L., Muse S.V., Katz L.A.;
RT "Genome architecture drives protein evolution in ciliates.";
RL Mol. Biol. Evol. 23:1681-1687(2006).
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 -!- 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; DQ665314; ABG81373.1; -; Genomic_DNA.
DR AlphaFoldDB; A5X903; -.
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:ABG81373.1};
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|EMBL:ABG81373.1}.
FT DOMAIN 1..211
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABG81373.1"
FT NON_TER 392
FT /evidence="ECO:0000313|EMBL:ABG81373.1"
SQ SEQUENCE 392 AA; 43321 MW; 616173D55D110815 CRC64;
SGKSTSTGHL IYKCGGIDKR TIEKFEKESG EKGKGSFKYA WVLDKLKAER ERGITIDISL
WKFSTEKYYF TIIDAPGHRD FIKNMITGTS QADVALLVIA AGAGEFEAGI SKEGQTREHG
LLAFTLGVRQ MIVLVNKMDA AKWSEERYND ISKEVKAYLK NVGYNPDKIP FVPISGWHGD
NMLDVSTNMP WYKGPTLIQA LDNVNPPKRP VDKPLRLPIQ DVYKIQGIGT VPAGRVETGV
LKPGMIVTFA PSNISTEVRS VEMHHESLEQ AIPGDNVGFN IKSVSTKEIK RGYVCGDSKN
DPPKEAGSFE AQVIVLNHPG QINAGYTPVI DCHTAHIACK FGEIKTKIDK RTNKSLEDNP
KFIKAGDSAI VKMEPQKPIC VEAFNQYPPL GR
//