EF1A_BLAHO
ID EF1A_BLAHO Reviewed; 434 AA.
AC P54959;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=HE87-1;
RX PubMed=8813670; DOI=10.1016/0166-6851(96)02600-x;
RA Nakamura Y., Hashimoto T., Yoshikawa H., Kamaishi T., Nakamura F.,
RA Okamoto K.I., Hasegawa M.;
RT "Phylogenetic position of Blastocystis hominis that contains cytochrome-
RT free mitochondria, inferred from the protein phylogeny of elongation factor
RT 1 alpha.";
RL Mol. Biochem. Parasitol. 77:241-245(1996).
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; D64080; BAA10962.1; -; mRNA.
DR AlphaFoldDB; P54959; -.
DR SMR; P54959; -.
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; 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; 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..434
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090955"
FT DOMAIN 5..232
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 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 196..198
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 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 47823 MW; 25DF7D44DC77F373 CRC64;
MGKEKPHINL VVIGHVVAGK STTTGHLIYA CGGIDKRTIE RFEEGGQRIG KGSFKYAWVL
AKMKAERERG ITIDISLWKF ETRKDFFTII DAPGHRDFIK NMITGTSQAD VAILVIASGA
GEFEAGYSKN GQTREHALLA NTLGVKQMIV CCNKMDDKSV NYSEARYKEI KNEMTSFLTK
VGYAKVEERI PFIPISGFNG DNMIEHSANM PWYKGPTLLE ALDNVHPPKR PVDKPLRLPL
QDVYKIGGIG TVPVGRVETG VLKPGMTVTF APVNVSTEVK SVEMHHESIP QALPGDNVGF
NVNNVSVEDI HRGNVCGDAK NDPPCKTESD AQVIVMNHPS GIRPGYCPVV DCHTAHIACK
FEKIMSEMDK RTGKVLRENP DIVKNGKSMM AQLVPSKPMC VETFSDYPPL GRFAVRDMRQ
TVAVGIIKST VRAK
