ID A0A316TJR4_9ACTN Unreviewed; 931 AA.
AC A0A316TJR4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DJ010_05060 {ECO:0000313|EMBL:PWN03489.1};
OS Nocardioides silvaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2201891 {ECO:0000313|EMBL:PWN03489.1, ECO:0000313|Proteomes:UP000245507};
RN [1] {ECO:0000313|EMBL:PWN03489.1, ECO:0000313|Proteomes:UP000245507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2018079 {ECO:0000313|EMBL:PWN03489.1,
RC ECO:0000313|Proteomes:UP000245507};
RA Li C., Wang G.;
RT "Nocardioides silvaticus genome.";
RL Submitted (MAY-2018) 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:PWN03489.1}.
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DR EMBL; QGDD01000002; PWN03489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TJR4; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000245507; 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|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:UP000245507}.
FT DOMAIN 424..596
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 60..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 483..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 537..540
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 931 AA; 96419 MW; 7A945AA1EAA4FFF5 CRC64;
MAKTRVSELA KKYGIPSKEA LEKLGAIGEF AKTASSSIEP PAVKKFEDAY GAELLARMKP
AAEPAEAPAK KAAAPKPGPK KPKAPEPEPA PAPVEEPAAA APAPEAPAAE PEAPAEPAAE
APAAAAPSAP SAPDAPAAPK PGAPTPKAPA PRPVGKPSGT PRPGNNPFAS SQGMGRRPAP
PPREGEAGPG GPRPPAGPGR PGMPRPNPAM MPKNPAAFGA GPGGRGPGRG GPGGGPGGAR
GGAPGRGGVG APGRGGPGGA PGRGGPGGGP GGFPGGGGRP GGGRPGQRGQ TQGAFGRPGG
PARRGRKSKR ARRQEFEAME APTIGGMRVR KGNGETVRLS RGSSLTDFAE KIGVDAASLV
QMLFHLGEMV TATQSVGDET LELLGDELNY KVEVVSPEDE DRELLESFDL EFGADEGDEG
DLVVRPPVVT VMGHVDHGKT KLLDALRGAN VVEGEAGGIT QHIGAYQVHT EVDGADRRIS
FIDTPGHEAF TAMRARGSQS SDIAILVVAA DDGVMPQTVE ALNHAKAAGV PIVVAVNKID
KPEADPTKVR GQLTEYGLVP EEYGGDSMFV DVSAKAGLNL DKLLEAVVLT ADASLDLRAN
PDQDAQGLVV EAHLDRGRGP VATILVQRGT LRVGDSIVAG PAYGRVRAML DEHGEEMSEA
DPGRPAMVLG LSAVPGAGQN FIVVEDDRMA RQIAEKREAR ERAALQAKRR VRRTLEDFMA
SMEKGESQEL NLILKGDVSG SVEALEDALA QLEVGDEVSL RVIDRGVGAI TEANVNLAAA
SDAIIIGFNV RAQGKAAELA DREGVEIKYY SVIYQAIEEI EAALKGMLKP EFEESTLGQA
EIRAIFRSSK IGNIAGCMVT SGVIRRNAKV RVLRDGAVVA DNLDLASLKR EKDDASEVRE
GFECGLVLRN FQDIKEGDIV EAFEMKEIPR S
//
