EF1A_AERPE
ID EF1A_AERPE Reviewed; 437 AA.
AC Q9YAV0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-1-alpha {ECO:0000255|HAMAP-Rule:MF_00118};
DE AltName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=APE_1844;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- INTERACTION:
CC Q9YAV0; Q9YAZ5: pelA; NbExp=3; IntAct=EBI-15880729, EBI-15880754;
CC Q9YAV0; Q9YAF1: prf1; NbExp=3; IntAct=EBI-15880729, EBI-15887661;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
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|HAMAP-Rule:MF_00118}.
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DR EMBL; BA000002; BAA80848.1; -; Genomic_DNA.
DR PIR; C72570; C72570.
DR PDB; 3VMF; X-ray; 2.30 A; A=1-437.
DR PDB; 3WXM; X-ray; 2.30 A; A/C/E/G=1-437.
DR PDB; 4CXG; EM; 8.70 A; A=1-437.
DR PDB; 4CXH; EM; 8.90 A; A=1-437.
DR PDB; 6JI2; X-ray; 3.00 A; A/E=1-437.
DR PDBsum; 3VMF; -.
DR PDBsum; 3WXM; -.
DR PDBsum; 4CXG; -.
DR PDBsum; 4CXH; -.
DR PDBsum; 6JI2; -.
DR AlphaFoldDB; Q9YAV0; -.
DR SMR; Q9YAV0; -.
DR DIP; DIP-59399N; -.
DR IntAct; Q9YAV0; 2.
DR STRING; 272557.APE_1844; -.
DR EnsemblBacteria; BAA80848; BAA80848; APE_1844.
DR KEGG; ape:APE_1844; -.
DR PATRIC; fig|272557.25.peg.1237; -.
DR eggNOG; arCOG01561; Archaea.
DR OMA; AIRDMGM; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; IPR005225; Small_GTP-bd_dom.
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 TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..437
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090974"
FT DOMAIN 4..229
FT /note="tr-type G"
FT REGION 13..20
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 69..73
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 90..93
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 152..155
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 193..195
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 90..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 152..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:3VMF"
FT TURN 157..161
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3VMF"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3VMF"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:3VMF"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:3VMF"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 322..332
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 352..365
FT /evidence="ECO:0007829|PDB:3VMF"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 385..394
FT /evidence="ECO:0007829|PDB:3VMF"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3VMF"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 417..429
FT /evidence="ECO:0007829|PDB:3VMF"
SQ SEQUENCE 437 AA; 48663 MW; D6AE87FEB8AD003C CRC64;
MAEKPHMNLV VIGHVDHGKS TLVGHLLYRL GYIEEKKLKE LEEQAKSRGK ESFKFAWILD
KMKEERERGI TIDLTFMKFE TKKYVFTIID APGHRDFVKN MITGASQADA AILVVSARKG
EFEAGMSTEG QTREHLLLAR TMGIEQIIVA VNKMDAPDVN YDQKRYEFVV SVLKKFMKGL
GYQVDKIPFI PVSAWKGDNL IERSPNMPWY NGPTLVEALD QLQPPAKPVD KPLRIPVQNV
YSIPGAGTVP VGRVETGVLR VGDKVVFMPP GVVGEVRSIE MHYQQLQQAE PGDNIGFAVR
GVSKSDIKRG DVAGHLDKPP TVAEEFEARI FVIWHPSAIT VGYTPVIHVH TASVSSRIIE
IKAKLDPKTG QVVEQNPQFL KAGDAAIVRF KPVKPLVVEK FSEIPQLGRF AMRDMNRTVG
IGIVTDVKPA KVDIKAK
