IF2_ANASK
ID IF2_ANASK Reviewed; 946 AA.
AC B4UHG0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=AnaeK_1162;
OS Anaeromyxobacter sp. (strain K).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=447217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA Beliaev A.;
RT "Complete sequence of Anaeromyxobacter sp. K.";
RL Submitted (AUG-2008) 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; CP001131; ACG72395.1; -; Genomic_DNA.
DR RefSeq; WP_012525221.1; NC_011145.1.
DR AlphaFoldDB; B4UHG0; -.
DR SMR; B4UHG0; -.
DR EnsemblBacteria; ACG72395; ACG72395; AnaeK_1162.
DR KEGG; ank:AnaeK_1162; -.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 61243at2; -.
DR Proteomes; UP000001871; 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; 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..946
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093757"
FT DOMAIN 445..614
FT /note="tr-type G"
FT REGION 58..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..461
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 479..483
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 500..503
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 554..557
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 590..592
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 87..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..461
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 500..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 554..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 946 AA; 100698 MW; 36C276576A665BD5 CRC64;
MSKKRVHELG KQLKEQGIEL SNQELVEKLH ALGYLEVKSH SSSLEDDQAH AAYEKILAER
KPKPAPVRPS GPGFVVRKRA HVEPPTVTAP AAPPPAEPEY AEPPQAEQAY EPEPQEAQPE
AAPEPVAAPE QPAEAAPLAA QAAPSPGAEA AAPAAPQAQP AQPAAPVAPP APSAQPSAPQ
PAAAQPRPPQ PPMPSRPPPA GYRPAPPPGA RPPMSAAPGA PAQPGAAAQP PRPPVDPRTL
RPTSTQAVVI SRPLVPVRRV TPPTSARQQF PVAPGPRALG EVRELKVVPG SLGREREFID
VSRDKRRGRQ PGRPISEEQA KSLSGKELLQ AAISDRAYIP IRGKKKKPTK KGAKTQITEK
AEHKKVIRIE ESISVSELSQ VMGVKASDLI RKLMQMGKMV TINAQIDADT AAILALEHGY
TVEKKGFEVE EFIPEVEVDE SKLVIRPPVV TVMGHVDHGK TSLLDAIRQA DVAAGEAGGI
TQHIGAYSVN TPQGPITFLD TPGHEAFTAM RQRGAQVTDL VVLVVAADDG VMPQTVESIK
AAKAAGVTIL VAINKVDKPQ AAPERVMQQL TEYELVAEQW GGTTIMLPVS ARTKQGIPEL
LEYIALQSEV LELKANPDKL AAGRVIEAKL EKGRGPVATV LVEEGTLRVG DALVTGVHFG
RVRAMMNERG EQVDNVGPGY PVEVLGLSGV PVAGDEFDVV EDEKAAKEVA QHRATKQRQK
ELGGVKKATL EDLFAKAKTS GQKVLNLVVK ADVQGSSEAV SQALEKAATK KVGVKILESA
VGAITKSDVL TAAAGNAVIV GFNTKPESEI ENIASQQGVK ILMFGIIYEA VDRIREEMAG
LLEPIIKEKP LGKAEVRQVF NIPRVGQIAG SAVTEGVVKR AGHVRVVRDR KVIFTGKIGS
LKRVKDDVRE VAQGFECGIG VDGFSDVKQG DILEVYELEE IRPSLD
