ID A0A150IW90_9EURY Unreviewed; 529 AA.
AC A0A150IW90;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Elongation factor 1-alpha {ECO:0000313|EMBL:KYC49192.1};
GN Name=tuf_3 {ECO:0000313|EMBL:KYC49192.1};
GN ORFNames=AMQ22_01700 {ECO:0000313|EMBL:KYC49192.1};
OS Candidatus Methanofastidiosum methylthiophilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC Methanofastidiosum.
OX NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC49192.1, ECO:0000313|Proteomes:UP000075398};
RN [1] {ECO:0000313|EMBL:KYC49192.1, ECO:0000313|Proteomes:UP000075398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U1lsi0528_Bin055 {ECO:0000313|EMBL:KYC49192.1};
RX PubMed=26943620;
RA Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT fastidious methyl-reducing methanogen.";
RL ISME J. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC49192.1}.
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DR EMBL; LNGC01000104; KYC49192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150IW90; -.
DR STRING; 1705564.APG08_01064; -.
DR Proteomes; UP000075398; Unassembled WGS sequence.
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 CDD; cd03708; GTPBP_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:KYC49192.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 116..343
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 529 AA; 59500 MW; 3B8BF820C8A56F5F CRC64;
MKESIHQVLK KGERKNIEFK SALGDEHLLK DRRERLSAQM KYRLKTGGGK AYYIIGVSDD
GDVVCQSQEE FEKTLDVIKR LTEGINAKIT DIEKYNENGF FARITIEETN SEKGIKEHIT
IGTIGHVDHG KSTLIGTLLT GMEDDGVGKT RIFLDFLPHE IERGLTAEIT HAVFGFKGDE
RIYLKNPLNK KEVAELIDRS TKIISFVDCP GHAPWLRTTV RGILGQRVDY VLLIVASDDG
VTPITKEHLG IALAMDIPLI IVITKIDKVS YEEAKQVISD VSALLRRVGK VPLNVKDKET
AHDISKKVSE RFLIPIIKAS SITLEGLDIL NELFLNLPEK TNDELYKKPF LMYIDKVYKV
RGAGTVVSGR VKQGIVKKGQ ELLLGPINDK YETVSCQSIK QHHLVQAKGE VGDILGIAIK
GVDADLIKRG MVIKDENGES KPVREFLAEV FILNHPTRIK EGYEPIIHLE TICETVTFEK
IYNQEYLSTG DRALIKMKFK YNSYYFSEGD KFIFREAKSK GIGGIKKIL
//