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 27-MAR-2024, entry version 103.
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 VEuPathDB; CryptoDB:cgd6_3990; -.
DR VEuPathDB; CryptoDB:CPATCC_0015600; -.
DR OMA; RDMGQTV; -.
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 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 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 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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
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 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
//
