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Database: UniProt
Entry: A0A1G6DAZ0_9FIRM
LinkDB: A0A1G6DAZ0_9FIRM
Original site: A0A1G6DAZ0_9FIRM 
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
//
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