ID M0AMX7_NATA1 Unreviewed; 609 AA.
AC M0AMX7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=C481_15565 {ECO:0000313|EMBL:ELY99282.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELY99282.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELY99282.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELY99282.1,
RC ECO:0000313|Proteomes:UP000011554};
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:ELY99282.1}.
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DR EMBL; AOIO01000034; ELY99282.1; -; Genomic_DNA.
DR RefSeq; WP_006110185.1; NZ_AOIO01000034.1.
DR AlphaFoldDB; M0AMX7; -.
DR STRING; 29540.C481_15565; -.
DR PATRIC; fig|29540.5.peg.3174; -.
DR eggNOG; arCOG01560; Archaea.
DR OrthoDB; 30957at2157; -.
DR Proteomes; UP000011554; 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; 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; 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:UP000011554}.
FT DOMAIN 22..237
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 31..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 93..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 609 AA; 66116 MW; 08D528FED7B11F7A CRC64;
MSDTDTDTDT DADAGARNST SLRTPIVAVL GHVDHGKTSL LDKIRGSAVI EGEAGAITQH
IGATAVPLDV ISSIAGDLVD PDDFDLPGLL FIDTPGHHSF TTLRSRGGAL ADIAILVVDV
NDGFQPQTLE ALDILKRSET PFIVAANKID TVPGWNATED SPINATYEAQ TDRVSSRLDE
SLYEIIGNLS DEGFSADLYW RVQNFQRNVG VVPVSAMTGE GVPDLLTVMM GLSQRYMKEE
MEIDVTGPGV GTVLEVKEEK GFGTTIDTVL YDGTIRADDQ LVVGGMNEPI VTDVRALLQP
RPLAEIRTES RFEKVDEISA ASGIKIAAPE LEDAMAGAPV RVVRDRELDE VIQEVEAELA
DIAVDTAEEG VVVKADTLGS LEAMADALDE AEVPIVRAEV GDVAPRDVSV ASTADDPKQQ
AILGFNVETL SDADQRAETE DVTIFTDEVI YQLIDEYEEH VDELERAQQD TILDNIVRPA
RFRILPDHTF RQNDPAVVGV EVNSGTVQNN TNIVKFDGSE PERVGQVKGI QEQGEDVDEA
RAGNRVSVAI DGPTVGRQIE EDDELWAEIP EKHAKILEQE LASEIPGDEL EALNMYLDKQ
RSRDPFWGK
//
