IF2_NOVAD
ID IF2_NOVAD Reviewed; 875 AA.
AC Q2G5E7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Saro_2490;
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) 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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP000248; ABD26926.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2G5E7; -.
DR SMR; Q2G5E7; -.
DR STRING; 279238.Saro_2490; -.
DR PRIDE; Q2G5E7; -.
DR EnsemblBacteria; ABD26926; ABD26926; Saro_2490.
DR KEGG; nar:Saro_2490; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000009134; 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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..875
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335493"
FT DOMAIN 374..544
FT /note="tr-type G"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..390
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 408..412
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 430..433
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 484..487
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 520..522
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 66..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383..390
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 430..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 484..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 875 AA; 93570 MW; BD12426E1B1E5A33 CRC64;
MSDSDKKPTL GRRPLGLKTA VEAGEVKQTF SHGRTNKVVV EVKRRKLMGR PGEAAPTAAP
AAAATPAPTP VAPPPPPPPP PPPPSASRET RQEMQVRLLR EAEEARLAAL EAANRREQEE
RLRAIEEERR RAEEKARAEA EAAAAPAAPA APAAPSAAPA AAQSAPEAAP APVAEPEVAR
QPEAAPVAAT APAAPKAEEA KPAAPAVPAP RRFTPVAPAA PIKRPELAAK KPAHPQRDRK
TEDRRGGKLT VTRALNEDEG ARARSLAALK RAREKERRAH FAGQSQPREK QVRDVVVPDA
ITVQDLANRM AEKAADLVKA LFKMGMMVTI NQTIDQDTAE LLVTEFGHNI QRVSESDADI
DTSADVDPEE SLKARPPVVT IMGHVDHGKT SLLDALRGTD VVRGEAGGIT QHIGAYQIKT
KGGDFITFLD TPGHEAFTEM RIRGANVTDI VILVVAGDDG LMPQTIEAIN HTKAAGVPMI
VAITKADKPE FQPQKIRERL LEHEIIVEAM SGDVQDVEVS AKTGAGLDEL IEKILLQAEL
LELKANPDRS AEATVIEAKL DKGKGPLATV LVNRGTLKVG DILVVGTQSG RVRAMLDDKG
RQVKAAGPSL PVEVLGIGGV PMAGDTLTVV ESEARAREVA AYRQERATAK RTAQAPASLE
NMFSALAAKN AVIEYPLVIR ADVQGSAEAI VNALNKISTD EIKVRILASG VGAITESDVN
LAQASGAPIV GFNVRPNAKA RELIERNKVR MKYFDVIYQL TDDIRSEMAG ELGPEAIETV
VGRAEVKEVF PAGKRDKAAG LLVVEGVIRK GLHARLTRND VIVSRTTIAS LRRFKDDVPE
VRAGLECGVL LQDTNDIKAG DQLEVFEVEM RERTL
