ID A0A1I3YUC4_9CELL Unreviewed; 980 AA.
AC A0A1I3YUC4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05216467_3041 {ECO:0000313|EMBL:SFK35462.1};
OS Cellulomonas sp. KH9.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1855324 {ECO:0000313|EMBL:SFK35462.1, ECO:0000313|Proteomes:UP000199404};
RN [1] {ECO:0000313|Proteomes:UP000199404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH9 {ECO:0000313|Proteomes:UP000199404};
RA Varghese N., Submissions S.;
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|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}.
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DR EMBL; FOSE01000004; SFK35462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3YUC4; -.
DR STRING; 1855324.SAMN05216467_3041; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000199404; 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; 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|ARBA:ARBA00022490, 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:UP000199404}.
FT DOMAIN 473..644
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 45..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482..489
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 532..536
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 586..589
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 980 AA; 101280 MW; 66773BBED7B4142D CRC64;
MAKVRVYELA KELGVDSKTI MTKLNELGEF VRSASSTIEP PVVRKLRDTY PVGGSGKPAA
PARPAAPQAA APSGGTPAPA PARPAAPAAP APAAPAPAAA APQAPAPLAP APQAPAPQAP
AAQAPAPQAP APQAPAAQSP APRAAAPANP GARPSQSAPQ GARPGAPRPP QSGGQGGARP
GAPRPAARPG NNPFAPAQGM PRQGERPGGP RPGGPRPGNN PFAPSQGMPR PGDRRPAPAE
GAPAAAAGER PGGPRPGGPR PGGPRPNPGM MPGRTQSGVG RPGERPAPAG RGGGGRPGGG
GGGYGARPGG GAPGGGGGFA GRPGGGGRPG GAGRGSTQGA FGRAGGRPVR GRKSKRAKRQ
EFEQMQAPSL GGVSVPRGNG KTVVRLRHGS SLNDFADKID ANPASLVTVL FHLGEMATAT
QSLDEDTFGA LASELGYVIE MVSAEEEDRE LLGAFDIDLE AELEAEGDEV LEARPPVVTV
MGHVDHGKTK LLDAIRSTDV VAGEAGGITQ HIGAYQVRAE HEGVERAITF IDTPGHEAFT
AMRARGAQVT DIAILVVAAD DGVMPQTIEA LNHAQSANVP IVVAVNKVDK EGANPDKIRQ
QLTEYNLVAE EYGGDTMFVD VSAKQRQGID QLLEAVLLTA DAALDLRANP DKDARGVAIE
ANLDKGRGAV ATVLVQSGSL HVGDAIVAGT AHGRVRAMLD EHGENLTEAG PARPVQVLGL
SSVPRAGDTF LVAPDERTAR QIAEKRESAE RAALLAKRRK RISLEDFTQA LQQGKVETLN
LVLKGDVSGA VEALEDALLK IDVGDEVDLR VIHRGVGAIT QNDVNLATVD NAIIIGFNVK
LAPRVEELAD REGVDVRFYS VIYQAIDDVE AALKGMLKPE YEEAQLGSAE VREIFRSSKF
GNIAGCIVRS GEIRRNTKAR VLRKGKVIGD NLTIESLKRF KDDATEVREG YECGIGLGSF
NDLQLEDVIE TFEMREKPRS
//
