ID A0A094RUJ7_9ACTN Unreviewed; 983 AA.
AC A0A094RUJ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=GM46_7210 {ECO:0000313|EMBL:KGA08773.1};
OS actinobacterium acAcidi.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA08773.1, ECO:0000313|Proteomes:UP000029305};
RN [1] {ECO:0000313|EMBL:KGA08773.1, ECO:0000313|Proteomes:UP000029305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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|HAMAP-Rule:MF_00100,
CC 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}.
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:KGA08773.1}.
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DR EMBL; JNSG01000061; KGA08773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094RUJ7; -.
DR PATRIC; fig|1504320.4.peg.1450; -.
DR Proteomes; UP000029305; 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; 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; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 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.
DR PROSITE; PS01176; IF2; 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}.
FT DOMAIN 480..649
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 36..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..631
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 43..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 535..539
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 589..592
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 983 AA; 102591 MW; 1947211DB6663463 CRC64;
MPVKKIRIAE LAKELGLTNK EALDLSKTMG IDVKGVSSSM EEAQADRVRR KAVKDGLKRD
VQPEEEKPAK KAAAKKAAVK KVDAEDGSTP APAKKAAAKK APAKKAAAAK VDAAPAVEVS
APVVEAPAPA PVAEAPAPVI ETPAPVVEAP AAAVVDAPAP VAETPTGESR VISSGRPTPT
SSIPRPPINP MPSARPAPST RSTPPGMPPT GMPPRGPGAP GARPIPPPPG PMSATGRPIP
PPPGGRVAPG ESRPGFRPGP GGARPGPGGA GFRPGPGSRP GPGGPGGPRT GGPGGPRTGG
PGGPGGPRTG FAPRTGGPGG PGGARPGGPG AGAPGAGGPG GGPRPGGGPG GPRNNGQRRA
PRKKSRARRR AEFDELQPQF TSYSNSNAPV PEGTIIIERG ASAQEFAPKL NRTPADVVRY
LLEHGEMVTA TMSLGDDQME LFALEVGAEI LLVDPGQQQE TELQALFDDS DDDDESLQQP
RPPVITVMGH VDHGKTTLLD RIRSANVVAG EAGGITQHIG AYQVEKDGKK VTFIDTPGHA
AFSKMRMRGA QVTDIVVLVV AADDGVMPQT IEAINHAKAA DVPIIVAVNK IDKDNADPQR
VLTQLAEYEL VPEAWGGDTI VVEMSAQQNL GIDDLLEQLT VVAELEELTA NPVGRAKGVV
LEANLDIGRG PVATVLVDKG TLKVGDPIVA GAAWGKVRAL INERGEQIKE AGPSTPVQVL
GLSSVPQAGD EFRSAPDEKT ARVVGDARGH SRRVLSQRGD SRVQGGVKLE DIFSQIQAGE
VATLNLVIKA DVQGSLEAVS ESLRKLERPE VKVAFVHRGV GGITENDITL AATTNATLIG
FNVRPDRKSR DLAEAEKVEI RTYEIIYKLL EDMERAMLGL LAPEFEEVVT GEAEVREIFR
VPKLGAIAGC FIRTGVITRG TKVRFLRDGT IIWKGSIQSL RRFKDDVREV REGFECGIGL
SDFQDLKPGD LIETFEEREI ARV
//
