ID A0A1I0Q7E7_9EURY Unreviewed; 599 AA.
AC A0A1I0Q7E7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=SAMN05216285_3179 {ECO:0000313|EMBL:SEW22819.1};
OS Natrinema salifodinae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEW22819.1, ECO:0000313|Proteomes:UP000183275};
RN [1] {ECO:0000313|Proteomes:UP000183275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOIS01000004; SEW22819.1; -; Genomic_DNA.
DR RefSeq; WP_049991758.1; NZ_JROF01000036.1.
DR AlphaFoldDB; A0A1I0Q7E7; -.
DR STRING; 1202768.SAMN05216285_3179; -.
DR eggNOG; arCOG01560; Archaea.
DR OrthoDB; 30957at2157; -.
DR Proteomes; UP000183275; 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:UP000183275}.
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; 65347 MW; E04AB5AF3F9969CF CRC64;
MSDTDTRDPT SLRTPIVAVL GHVDHGKTSL LDKIRGSAVI EGEAGAITQH IGATAVPLDI
ISSIAGDLVD PEDFDLPGLL FIDTPGHHSF TTLRSRGGAL ADIAILVVDV NDGFQPQTLE
ALDILKRSQT PFIVAANKID TVPGWNANED EPINDTYESQ SERVRQRLDE ELYEIIGNLS
DEGFSADLYW RVQNFQRNIG VVPVSAMTGE GVPDLLTVMM GLSQRYMKEE MEIDVAGPGV
GTVLEVKEEK GFGTTVDTVL YDGTIRADDK IVVGGQNEPI VTDVRALLQP RPLAEIRTES
RFEKVDEVGA AAGIKIAAPD LADAMAGAPV RVVRDRDLDE VIEEVQAELA DIAVDTAEEG
VVVKADTLGS LEAMADALGE AEVPIVRAEV GDVAPRDVSV ASTADDPKQK AILGFNVDTL
DDAEQRAEIE DVTIFTDEVI YQLIEGYEEY VEEIEQAQQD TILENISRPA RFRILPDHTF
RQNDPAVVGV EVNSGTLRNN TNVVKFEGNE PERVGQVKGI QEQGEDIDEA RSGNRVSVAI
DGPTVGRQIE EDDELWAEIP EKHAKILEQE LASEIPGDEL EALNMYLDKQ RSRDPFWGK
//
