ID A0A0M8QP12_9ACTN Unreviewed; 1000 AA.
AC A0A0M8QP12;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ADK41_26290 {ECO:0000313|EMBL:KOT34553.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT34553.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT34553.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT34553.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-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:KOT34553.1}.
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DR EMBL; LGCN01000217; KOT34553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8QP12; -.
DR PATRIC; fig|36816.3.peg.5684; -.
DR Proteomes; UP000037773; 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; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000037773}.
FT DOMAIN 493..665
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 29..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..281
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 502..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 552..556
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 606..609
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1000 AA; 102202 MW; 8CE6F90F1B6358C3 CRC64;
MAKLQELGEF VRSASSTIEA PVVRKLTDAF QQGGGNGRSA AKPGAPRKAA PRPAAPSPAQ
AARPGPAAPK PPAAPKPAAA QPPAAPSAPS APAPAASGSR PTPGPRPAPR PAPAAPEFQA
PPAAAPAPAG PKPGGARPGA PKPGGRPAGQ GQGQGGQGGQ GRPAGQGQRP GGGAPRPGGR
PAGPRPGNNP FTSGGSTGMA RPQAPRPQGG ARPGPGGPGG AGPRPQAPGG QGGGPRPQAP
GGQRPTPGSM PRPQGGPRPG GGPGGPRPNP GMMPQRPAAG PRPGGGPGGR GPGGAGRPGG
AGRPGGGGFA GRPGGGGGAG RPGGGGGFAG RPGGGGGFGG GGGRPGFGGR PGGPGGRGGT
QGAFGRPGGP ARRGRKSKRQ RRQEYEAMQA PSVGGVMLPR GNGETIRLSR GASLTDFAEK
INANPASLVA VMMNLGEMVT ATQSVSDETL QLLAGEMNYT VQIVSPEEED RELLESFDLE
FGEDEGDEED LVVRPPVVTV MGHVDHGKTR LLDAIRKTNV IAGEAGGITQ HIGAYQVATE
VNEEERKITF IDTPGHEAFT AMRARGARST DIAILVVAAN DGVMPQTVEA LNHAKAADVP
IVVAVNKIDV EGADPTKVRG QLTEYGLVAE EYGGDTMFVD ISAKQGLHID SLLEAVILTA
DASLDLRANP TQDAQGISIE SRLDRGRGAV ATVLVQRGTL RVGDTMVVGD AYGRVRAMLD
DNGNNVAEAG PSTPVQVLGL TNVPGAGDNF IVVDEDRTAR QIAEKRAARE RNAAFAKRTR
RVSLEDLDKV LKAGEVQQLN LIIKGDASGS VEALESSLLQ LDVGEEVDIR VLHRGVGAVT
ESDIDLAMGS DAIVIGFNVR AAGRAAQMAE REGVDVRYYS VIYQAIEEIE AALKGMLKPE
YEEVELGTAE IREVFRSSKL GNIAGVLIRS GEVRRNTKAR LLRDGKVIAE NLNIEGLRRF
KDDVTEIREG YEGGINLGNF NDIKVDDVIA TYEMREKPRV
//
