ID A0A0K1RAH4_9CORY Unreviewed; 952 AA.
AC A0A0K1RAH4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=AK829_02220 {ECO:0000313|EMBL:AKV58176.1};
OS Corynebacterium riegelii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156976 {ECO:0000313|EMBL:AKV58176.1, ECO:0000313|Proteomes:UP000060016};
RN [1] {ECO:0000313|EMBL:AKV58176.1, ECO:0000313|Proteomes:UP000060016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PUDD_83A45 {ECO:0000313|EMBL:AKV58176.1,
RC ECO:0000313|Proteomes:UP000060016};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-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}.
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DR EMBL; CP012342; AKV58176.1; -; Genomic_DNA.
DR RefSeq; WP_052203869.1; NZ_CP012342.1.
DR AlphaFoldDB; A0A0K1RAH4; -.
DR STRING; 156976.AK829_02220; -.
DR PATRIC; fig|156976.3.peg.438; -.
DR Proteomes; UP000060016; Chromosome.
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 SMART; SM00173; RAS; 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:UP000060016}.
FT DOMAIN 448..622
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 54..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 507..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 561..564
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 952 AA; 98809 MW; 0D9B79E9BEEA5037 CRC64;
MPGKLRVHEL AKQLGVTSKE LLATLKEQGE FVKTASSTIE PPVVKKMKAY YEAQSGGGEE
EAAEGKPAAA KPAAKPAAAK PAAAKPAAAK PAAPKPGAAK PAAAKPAQPA KPAAAKPAAP
KPGAAKPAAA KPAAAKPAQP AKPAAAKPAA PKPAQPAKPA AAKPAAPKPG APKPGAAKPA
AGGPTPGAMP RPMPKPGGRP RVANNPFSSN TGGPRPAPRP GGGRGGNQQG GGRGRGPGQG
GERAGQGQGQ GRRPSPADMA AHPSPTQMPS KSANVGRGGR GGQGGPGRGR GGQGGPGAPR
DGYRGGRGGR RGGTAGAFGR PGGAPGRGRK SKRQKRTEYE EMHAPNVIGG VRLPDGGGKT
VRLRQGATLS DFADKIGTEA SNLVQALFNL GEMVTATQSV PEETLQLLGA EINYEVQIVS
PEDEDRELLE SFDLQFGEDE GGEEALEQRP PVVSVMGHVD HGKTRLLDSI RKANVGKGEA
GGITQGIGAY QTEVTLDGET RKITFLDTPG HEAFTAMRAR GAKSTDLAIL VVAADDGVMP
QTVEAINHAK AADLPIVVAV NKVDKEEAQP DKIRGQLTEY GLVPEEYGGD TMFINISAKQ
GTGIDELLEA VLLTADAALE LTANPDMDAQ GVAIESHLDR GRGPVSTVIV QRGTLRVGDS
IVVGGNFGRV RRMVDEWGND VEEAGPSRPV QVQGLNGVPG PGDNLLVVED DRVARQIAAQ
RDARQRAAMQ ARSKKRVSLE NLDQALKETS TLNLILKGDN AGSVEALEEA LLKIEVDDEV
EVNIIDRGVG AVTQTNVLLA AASDAVIVAF NVRADGKATE EANADGVEIR YYSVIYQVIE
EVEKALKGML KPIYEERELG AAEIRQIFKA SAVGLIAGCM VTEGKVKRGA KLRLVRDGNV
ITPDATIESL RREKDDATEV AKGYECGMVL SYPDIQVGDI IQTYEMVEVP RN
//
