EF1A2_EUPCR
ID EF1A2_EUPCR Reviewed; 439 AA.
AC Q27140;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha-2;
GN Name=EFA2;
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:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; U26267; AAB04941.1; -; Genomic_DNA.
DR AlphaFoldDB; Q27140; -.
DR SMR; Q27140; -.
DR PRIDE; Q27140; -.
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 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..439
FT /note="Elongation factor 1-alpha 2"
FT /id="PRO_0000090924"
FT DOMAIN 6..229
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 71..75
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 92..95
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 154..157
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 193..195
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 92..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 154..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 439 AA; 48697 MW; 88B00D5056C1C7E7 CRC64;
MERKEKDHLN LVVIGHVDSG KSTTTGHLIY KLGGIDERTL AKLEEKALEL NKASFKYAFV
LDNLKAEQER GITINCALRQ FDTPSRSYTI IDAPGHKDFI KNMITGTSQA DAAVLIIAAK
KGEFEDGFSR EGSTKDHALL AYTMGIKQAI VAINKMDTID YDEERFNEIV ENVSDHLGKI
GYKKENVKYI PISGFDGDNM LEQSENLPWY KGPTLTEALD EFKVPKRPIK KPLRVPIQDV
YKIAGIGTVP VGRVETGVLK RGMEVQFTTG ATSEVKSLEA HHNKLEEAEP GLNVGFNVRL
EAKEIKAGHV CGDAKNDPPK NAESFIAQVI VMNHPGHIKA GYQPVLDIHT AHVATKFKTL
LSKNEARTGK LIEEAPKFLK NGESGIVELV PTKPLCVEEF SKYAALGRFV IRDMKRTVAV
GVIQEVIHKK ETKKKASKR
