EF1A_PYRHO
ID EF1A_PYRHO Reviewed; 428 AA.
AC O59153;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=PH1484;
GN ORFNames=PHCC033;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000001; BAA30591.1; -; Genomic_DNA.
DR PIR; G71023; G71023.
DR RefSeq; WP_010885563.1; NC_000961.1.
DR PDB; 3WY9; X-ray; 2.30 A; A/B=1-428.
DR PDB; 3WYA; X-ray; 2.35 A; A=1-428.
DR PDB; 7CSL; X-ray; 2.00 A; A/B=1-428.
DR PDBsum; 3WY9; -.
DR PDBsum; 3WYA; -.
DR PDBsum; 7CSL; -.
DR AlphaFoldDB; O59153; -.
DR SMR; O59153; -.
DR STRING; 70601.3257908; -.
DR EnsemblBacteria; BAA30591; BAA30591; BAA30591.
DR GeneID; 1443801; -.
DR KEGG; pho:PH1484; -.
DR eggNOG; arCOG01561; Archaea.
DR OMA; AIRDMGM; -.
DR OrthoDB; 13117at2157; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..428
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090990"
FT DOMAIN 5..217
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 68..72
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 89..92
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 144..147
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 181..183
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 89..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 144..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 50..67
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:3WY9"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3WY9"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3WY9"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:7CSL"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 153..169
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7CSL"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:7CSL"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3WY9"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:7CSL"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 349..362
FT /evidence="ECO:0007829|PDB:7CSL"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 382..391
FT /evidence="ECO:0007829|PDB:7CSL"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 414..425
FT /evidence="ECO:0007829|PDB:7CSL"
SQ SEQUENCE 428 AA; 47525 MW; 830379915E67E6EA CRC64;
MPKEKPHVNI VFIGHVDHGK STTIGRLLYD TGNIPETIIK KFEEMGEKGK SFKFAWVMDR
LKEERERGIT IDVAHTKFET PHRYITIIDA PGHRDFVKNM ITGASQADAA VLVVAATDGV
MPQTKEHAFL ARTLGIKHII VTINKMDMVN YDQKVFEKVK AQVEKLLKTL GYKDFPVIPT
SAWNGDNVVK KSDKMPWYNG PTLIEALDQI PEPEKPIDKP LRIPIQDVYS IKGVGTVPVG
RVETGKLKVG DVVIFEPAST IFHKPIQGEV KSIEMHHEPL QEALPGDNIG FNVRGVSKND
IKRGDVAGHT DKPPTVVRTK DTFKAQIIVL NHPTAITVGY SPVLHAHTAQ IPVRFEQILA
KVDPRTGNIV EENPQFIKTG DSAIVVLRPM KPVVLEPVKE IPQLGRFAIR DMGMTIAAGM
VISIQKGE