ID A0A1G6DAZ0_9FIRM Unreviewed; 842 AA.
AC A0A1G6DAZ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN ORFNames=SAMN02910317_02094 {ECO:0000313|EMBL:SDB42259.1};
OS Ruminococcaceae bacterium FB2012.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1520817 {ECO:0000313|EMBL:SDB42259.1, ECO:0000313|Proteomes:UP000199364};
RN [1] {ECO:0000313|EMBL:SDB42259.1, ECO:0000313|Proteomes:UP000199364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB2012 {ECO:0000313|EMBL:SDB42259.1,
RC ECO:0000313|Proteomes:UP000199364};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000256|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100}.
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; FMXS01000011; SDB42259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6DAZ0; -.
DR STRING; 1520817.SAMN02910317_02094; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000199364; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.10.2480; -; 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_B; IF_2_B; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
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; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000199364}.
FT DOMAIN 344..513
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 72..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..495
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 78..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 353..360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 399..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 453..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 842 AA; 92377 MW; 6451ABA98045B9FA CRC64;
MAVKKYKLNE LAKDLKLSNA EVIECLGALG GDAKKTVSAL APEEVSYVFE FFTQKNQVEN
FNAYFAANVA PEGVTAKKKP APKTEEKKEE PKAEEKKPAA KASEVKAPEV KAEAEKETPK
AEEKKPAEAA PSEQAKKTER RKEQKKQAKK QDHGVKTFIG GSKSGSTDEG YTVSEAGDSG
KGKNVDTRGS YVELDKYNEK YDNLANTKQN RSKDTFQKKQ KLTQKSQQYK KQLKQSAKRR
EGESEKERLR RLELEKARKQ QLKVLIPDEI VVSELASRLK VTVTEVIKKL MGLGVMASIN
ETVDFDTAAL VAEELGAKVE KEVIVTIEER LITDEADSEE DLEERSPVVV VMGHVDHGKT
SILDRIRHAN VAEGEAGGIT QHIGAYQVYY NNKKITFLDT PGHEAFTAMR ARGANVTDIA
ILVVAADDGI MPQTVESINH AKAAGVSIIV AINKMDKEGA DAERVKQELT EHSLVVEEWG
GDVIAVPVSA KTGQGIDELL ENILLVAEVK ELKANPHKAA KGTVIEAKLD KGKGPTATLL
VEGGTLHTGD VIIAGTAVGR VRTMTNDKGH KIDKAGPSTP VEITGLAEVP MSGDTFNAVA
DEKLARELVE QRKHQAKEEE FKKVSKVTLD NLFSQISEGE MKELPIIVKA DVQGSVEAVK
QSLEKISNDE VRVRVIHGAV GAVNESDVML ANASNAIIVG FNVRPDPVAK EQAERDGVDI
RLYRIIYDAI EEITTAMKGM LAPKFREIDT ARVEVRQVYK ISSVGNVAGC YVLSGKIGRN
DLIRVVRDGI IIADDKMSSL KRFKDDVKEV AEGYECGITL EKFTDIKEGD IFEGYIMEEY
RE
//