IF2_SALAI
ID IF2_SALAI Reviewed; 995 AA.
AC A8M746;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sare_1327;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) 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; CP000850; ABV97228.1; -; Genomic_DNA.
DR RefSeq; WP_012181536.1; NC_009953.1.
DR AlphaFoldDB; A8M746; -.
DR SMR; A8M746; -.
DR STRING; 391037.Sare_1327; -.
DR EnsemblBacteria; ABV97228; ABV97228; Sare_1327.
DR GeneID; 5708132; -.
DR KEGG; saq:Sare_1327; -.
DR PATRIC; fig|391037.6.peg.1349; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
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; 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; 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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..995
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335510"
FT DOMAIN 486..658
FT /note="tr-type G"
FT REGION 53..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..502
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 520..524
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 545..548
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 599..602
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 635..637
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 545..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 599..602
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 995 AA; 102114 MW; 6D0E5DF865B24850 CRC64;
MAGKARVHEL AKELGVESKT VLAKLKEMGE FVKSASSTVE APVARRLRNA FVNNAGSPAP
AAPPAVAPPT PTPTPPRTPT PAPPPGGPRV SAKPMPPRRQ GVPTPGPKPK GPVPGPPQSA
TPVTKPASAH DIEVAAAEAR AAALKAEQEA AVKAAQAARQ QQRENVRREP PTEGGPRPGP
RPGPGTMPPR PGSPAAGRSG APAPGPGPRP GGRPPARGAG NNPFGIQGGQ QRPPAAGAGG
PRPSPASMPP RPSPASMPPR PSPASMPSQR PGRPGGPGSG RPGSGAGRPG GGGGGGYRGG
GGGGGGGGYR GGPGGGGGGG GGFRGGPGGG GGGFRSGPGG GGRPGGGGRG RGGGAAGAFG
RPGGRPTRGR KSKKQRRQEF DNLSAPTMSS GAPRGQGQVV RLSRGASLSD FADKINANPG
SLVQEMFNLG EMVTATQSCS DDTLLLLGEH LGFAVQIVSP EDEDRELLAQ FNIDLDAEVA
EDRLVSRPPV VTVMGHVDHG KTKLLDAIRK ANVVAGEAGG ITQHIGAYQV HVPHDGEDRA
ITFIDTPGHE AFTAMRARGA QVTDIVILVV AADDGVMPQT IEALNHAKAA EVPIVVAVNK
IDKPEANPDK VRQQLTEYGL VAEEYGGDTM FVNVAAKPGT GIESLLEAVL LTADASLELT
APTDGPAQGV AIEAHLDKGR GAVATVLVQK GTLRAGDSIV AGGAHGRVRA MLDENGNQVA
EAGPSRPVLV LGLTAVPGAG DTFLAAEDDR TVRQIAEQRQ ARRRAAAFAN SRGRATLETL
MEQLKAGEKT SLNLVLKGDV SGSVEALEDA LFNLDIPEEV QLRIIHRGVG SITESDVMLA
SASSEAVTII GFNVRAANKV REMADREGVE IRYYTVIYQA IEEIEAALKG LLKPEYEEVE
LGTAEVREVF RSSKVGNISG CIVRSGLIRR NAKARLLRDG AVVADNLTIG SLKRFKDDAT
EVREGFECGL TLGGYNNVQV GDVIETFEMR EKARA
