ID L9XBI9_9EURY Unreviewed; 599 AA.
AC L9XBI9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Probable translation initiation factor IF-2 {ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN ORFNames=C493_05525 {ECO:0000313|EMBL:ELY59085.1};
OS Natronolimnohabitans innermongolicus JCM 12255.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronolimnohabitans.
OX NCBI_TaxID=1227499 {ECO:0000313|EMBL:ELY59085.1, ECO:0000313|Proteomes:UP000011602};
RN [1] {ECO:0000313|EMBL:ELY59085.1, ECO:0000313|Proteomes:UP000011602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12255 {ECO:0000313|EMBL:ELY59085.1,
RC ECO:0000313|Proteomes:UP000011602};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Function in general translation initiation by promoting the
CC binding of the formylmethionine-tRNA to ribosomes. Seems to function
CC along with eIF-2. {ECO:0000256|ARBA:ARBA00024852, ECO:0000256|HAMAP-
CC Rule:MF_00100, ECO:0000256|RuleBase:RU000644}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
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:ELY59085.1}.
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DR EMBL; AOHZ01000030; ELY59085.1; -; Genomic_DNA.
DR RefSeq; WP_007258408.1; NZ_AOHZ01000030.1.
DR AlphaFoldDB; L9XBI9; -.
DR STRING; 1227499.C493_05525; -.
DR PATRIC; fig|1227499.3.peg.1126; -.
DR eggNOG; arCOG01560; Archaea.
DR OrthoDB; 30957at2157; -.
DR Proteomes; UP000011602; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_A; IF_2_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR004544; TF_aIF-2_arc.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00491; aIF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 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 GTP-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000011602}.
FT DOMAIN 12..227
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 599 AA; 65087 MW; E9E9FD06A93A8E83 CRC64;
MSNTDTRDHT SLRTPIVAVL GHVDHGKTSL LDKIRGSAVI EGEAGAITQH IGATAVPLDI
ISSIAGELVD PDDFDLPGLL FIDTPGHHSF TTLRSRGGAL ADIAILVVDV NDGFQPQTLE
ALDILKRSQT PFIVAANKID TVPGWSVNED SPINDTYEAQ TDRVSSRLDE SLYEIIGNLS
DEGFSADLYW RVQNFQRNVG VVPVSAMTGE GVPDLLTVMM GLSQRYMKEE MEIDVAGPGV
GTVLEVKEEK GFGKTVDIVL YDGTIREDDT LVVGGQNDPI VTEVRALLQP RPLAEIRTES
RFENVDEVGA AAGIKVAAPE LEDAMAGAPV RVVRDRSLDE VVGEVEAELA DIAVDTAEEG
VVVKADTLGS LEAMADALDE AEVPIVRAEV GDVAPRDISV ASTAEDPKQQ AILGFNVDVL
SDAKQRAEIE DVTVFTDQVI YQLIEEYEDH VEGIEKAQQD TILENISRPA RFRILPDHTF
RQNDPAVVGV EVNAGTIQNN ANVVKFDGNE PNRVGQVKGI QEQGEDVDEA RAGNRVSVAI
DGPTVGRQIE EDDELWIEIP EKHAKILEQE LADEIPGDEL EALNMYLDNQ RSRDPFWGK
//
