ID   EF1A_CRYPV              Reviewed;         435 AA.
AC   P90519;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Elongation factor 1-alpha;
DE            Short=EF-1-alpha;
OS   Cryptosporidium parvum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=5807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9130588; DOI=10.1016/s0167-4781(97)00013-4;
RA   Bonafonte M.T., Priest J.W., Garmon D., Arrowood M.J., Mead J.R.;
RT   "Isolation of the gene coding for elongation factor-1alpha in
RT   Cryptosporidium parvum.";
RL   Biochim. Biophys. Acta 1351:256-260(1997).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U71180; AAC47526.1; -; mRNA.
DR   AlphaFoldDB; P90519; -.
DR   SMR; P90519; -.
DR   PRIDE; P90519; -.
DR   VEuPathDB; CryptoDB:cgd6_3990; -.
DR   OMA; AIRDMGM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..435
FT                   /note="Elongation factor 1-alpha"
FT                   /id="PRO_0000090920"
FT   DOMAIN          5..226
FT                   /note="tr-type G"
FT   REGION          14..21
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          70..74
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          91..94
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          151..154
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          190..192
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..154
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   435 AA;  48162 MW;  911FBE41044F703F CRC64;
     MGKEKTHINL VVIGHVDSGK STTTGHLIYK LGGIDKRTIE KFEKESSEMG KGSFKYAWVL
     DKLKAERERG ITIDIALWQF ETPKYHYTVI DAPGHRDFIK NMITGTSQAD VALLVVPADR
     FEGAFSKEGQ TREHALLAFT LGVRQMIVGI NKMDTCEYKQ SRFDEIFNEV DGYLKKVGYN
     TEKIPFVAIS GFVGDNMVER SDKMPWYKGK TLVEALDTME PPKRPTDKPL RLPLQDVYKI
     GGVGTVPVGR VETGIIRPGM NVTFAPAGVT TEVKSVEMHH EQMPEAVPGD NVGFNVKNVS
     IKDIKRGFVA SDAKNDPAKG CEDFTAQVIV LNHPGEIKNG YSPVVDCHTA HISCKFQTIT
     AKMDKRSGKV LEENPKLIKS GDAALVVMQP LKPLCVEAFT DYPPLGRFAV RDMKQTVAVG
     VIKSVTKKEA TSKKK