ID A0A0F0HQJ0_9PSEU Unreviewed; 1048 AA.
AC A0A0F0HQJ0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=UK12_14510 {ECO:0000313|EMBL:KJK57760.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK57760.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK57760.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK57760.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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:KJK57760.1}.
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DR EMBL; JYJF01000037; KJK57760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0HQJ0; -.
DR PATRIC; fig|1427391.3.peg.4302; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000033409; 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; 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 Pfam; PF04760; IF2_N; 2.
DR PRINTS; PR01217; PRICHEXTENSN.
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:UP000033409}.
FT DOMAIN 541..713
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 550..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 600..604
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 654..657
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1048 AA; 107152 MW; 6312336F64721979 CRC64;
MAKVRVYELA KELGLESKAV MAKLTELGEF VRSASSTIEA PVVRKLTDAL GATPPAGGSA
AKPGPRKPAA PQPAGATGAA APKPGAPTPG PRPTATPGPR PTPAAAAPAA PATPAAPKPA
AATPGPRPAA RPAAPAPAAP AAEFSSPAPA GEAPARPAAP APRPAAAAPS SGARPGPRPA
GPRPGNNPFT SGGATGMARP GDRRSGGGQG DRPRPAGAPG QGERPRPGGD RPRPAGAPGQ
GERPRPGGDR PRPAGAPGGD RPRPGGDRPR PAAGPGGAPR PGGPGAGAPR PDGMPRPAGP
RPGAPSPSGM PRPNPGMMPQ RPAGPGPRPG PGGRGPGGPG GRPGGPGGGG ARPGFAGRPA
GPGSRPAGGG FGGPRPGGGA PGGGGGFGPR PGGFGGRPGG PGARGGTQGA FGRGPGGRPA
RGRKSKRAKR QEYEAMQAPS VGGVMLPRGN GQTVRLSRGA SLMDFAEKIN ANPAALVSVM
FNLGEMVTAT QSVSDATLEL LAGEMGFVLE IVSRDDEDRE LLESFDIDFG ANEGDEDMLA
PRPPVVTVMG HVDHGKTRLL DAIRKSNVVA GEAGGITQHI GAYQVATMVN GEERPITFLD
TPGHEAFSAM RARGAKSTDI AILVVAANDG VMPQTVEALN HAKAAGVPIV VAVNKIDVEG
ADPTKVRGQL TEFGLVAEEY GGDTMFVDIS ARQGLHIDQL LEAVVLTADA SLDLRANPEQ
DAQGIAIEAH LDKGRGAMAT VLVQRGTLRV GDSIVVGDAY GRVRAMLDEN GNHLEEAGPS
RPVLLLGLTS VPRAGDSFIV VEEDRTARQI AEKRSARDRN AAFAQRRVRI SLEDLDKAIA
AGSIEQLNLI IKGDVSGSVE ALEDALVKLD VGEEVELRVL HRGVGAITES DVDLAMGSDA
IIIGFNVRAE GRARTAAEKE GVDVRYYSVI YQAIEEIESA LKGLLKPEYE EVRLGSAEIR
EVFRSSKFGN IAGVLVREGL LRRNAKARLI RDGKVVSENL TIEGLRRFKD DATEVREGFE
AGVTLGSFND IKVEDIIETY EMREKPRA
//
