EF1A1_EUPCR
ID EF1A1_EUPCR Reviewed; 442 AA.
AC Q27139;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Elongation factor 1-alpha 1;
DE Short=EF-1-alpha-1;
GN Name=EFA1;
OS Euplotes crassus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Hypotrichia; Euplotida; Euplotidae; Moneuplotes.
OX NCBI_TaxID=5936;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=POR3;
RX PubMed=8626055; DOI=10.1016/0378-1119(95)00728-8;
RA Bergemann J., Florian V., Kremser T., Klein A.;
RT "Two different macronuclear EF-1 alpha-encoding genes of the ciliate
RT Euplotes crassus are very dissimilar in their sequences, copy numbers and
RT transcriptional activities.";
RL Gene 168:109-112(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; U26260; AAB04943.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27139; -.
DR SMR; Q27139; -.
DR PRIDE; Q27139; -.
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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..442
FT /note="Elongation factor 1-alpha 1"
FT /id="PRO_0000090923"
FT DOMAIN 5..227
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 194..196
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 442 AA; 48537 MW; 423E15FB3292D265 CRC64;
MGKEKEHLNL VVIGHVDSGK STTTGHLIYK LGGIDARTIE KFEKESAEMG KASFKYAWVL
DKLKAERERG ITIDIALWKF ETENRHYTII DAPGHRDFIK NMITGTSQAD AAILIIASGT
GEFEAGISKE GQTREHALLA YTMGVKQMVV AMNKMDSTEP PYSEDRYEEI KKEVSTFLAK
VGYKPAKMNF VPISGFQGDN IQENSTNMPW YKGPTLCAAL DSFKIPKRPI AKPLRLPLQD
VYKIGGIGTV PVGRVETGVL KAGMVITFAP KGCSAECKSV EMHHEEVPEA APGNNVGFNV
KGLSVKDIKR GFVASDSKND PATDTESFVS HTIVMNHPGE IKAGYTPVID CHTAHIACKF
EELLTKADKR SGKMTEENPK FLKAGDAGLI RLSPSKPLCV ETFATYAPLG RFAVRDMRQT
VAVGVIQEIK KKATEDKKGK KK