IF2_DESRM
ID IF2_DESRM Reviewed; 985 AA.
AC A4J5X2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Dred_1957;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-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; CP000612; ABO50475.1; -; Genomic_DNA.
DR RefSeq; WP_011878285.1; NC_009253.1.
DR AlphaFoldDB; A4J5X2; -.
DR SMR; A4J5X2; -.
DR STRING; 349161.Dred_1957; -.
DR EnsemblBacteria; ABO50475; ABO50475; Dred_1957.
DR KEGG; drm:Dred_1957; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; PRPGYQG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001556; 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; 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; 2.
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; Reference proteome.
FT CHAIN 1..985
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000071288"
FT DOMAIN 485..654
FT /note="tr-type G"
FT REGION 49..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..501
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 519..523
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 540..543
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 594..597
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 630..632
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 49..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 494..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 540..544
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 594..597
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 985 AA; 107321 MW; 431EAB0A3547D7C0 CRC64;
MTKKRVHELA KELNIENKEL INKLMQIGIS VKSHMSALEN DAVEKVYHQY GKKQEKSSDS
ANKQIQREHG RGQGMEDKKE KDQLFRPDNA KGPGLVDRVP NRPPDRRYED KAKVAQKPAQ
ELRGSKTTTN SENEQTAPRQ GSAQQSGQGR PQANRPQGSQ GRPYGGRPQG GQSRPYGDRP
QGGQGRPYGD RPQGGQGRPY GDRPQGGQGR PYGDRPQGGQ GRPYGDRPQG GQGRPYGDRP
QGGQGRPYGD RPQGGQSRPY GDRPQGGQGR PYGDRPQGGQ SRPYGDRPQG GQGRPYGDRP
QGGQGRHYGD RPQGGQGRPQ GAGRPGANRG AGPSIPKPPE QVAQPKPTKA PDKTKGDRRK
NYEKDGKWAD GQIEKNKLFK GRNNKNKKRQ HQQSAPPPIL DKKPVQIAEV ITVQELAEKL
KKTAAEVIKK LMGLGVLATI NQEVDFETAT LIAGEYGIET ELKVAVDKEA LVMAEPEEDE
DKLVLRPPVV TIMGHVDHGK TSLLDAIRET NVTAGEAGGI TQHIGAYQVE RNGKKITFVD
TPGHAAFTSM RARGAQITDI AILVVAADDG VMPQTIEAIN HAKAANVPII VAINKMDKPD
ANPDKVKQEL TQHELVVEDW GGDVIAVPVS AKNRTGLDNL LEMILLVAEV HELKANPDRM
ARGTVVEAEL DKGRGPVATV LVQNGTLNVG DTIVVGQVSG RVRAMIDDKG RRVKKAPPST
PVEILGLSDV PEAGDILVAV EDEKLARDVA EKRKIRKREE GLKSSTKISL DDLFKHIQEG
QIKELPIIVK ADVQGSIEAL AQALEKLTTE EVKVNLIHTG VGAVNETDIM LATASNAIVI
GFNVRPDNNA RKLADAEKVD INLYRVIYEV IDDVKKAMSG LLDPEFKEVV LGHVEVRKTF
KASKIGTIAG GYVTEGKIVR DASVRVIRDG IVVFEGKLDS LKRFKDDAKE VAQGYECGLT
IDRFNDVQEG DIIEAFTMEA IKREI
