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Database: UniProt
Entry: A5X903_NYCOV
LinkDB: A5X903_NYCOV
Original site: A5X903_NYCOV 
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
//
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