IF2_ANADF
ID IF2_ANADF Reviewed; 970 AA.
AC A7H9F3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-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};
GN OrderedLocusNames=Anae109_1141;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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; CP000769; ABS25349.1; -; Genomic_DNA.
DR RefSeq; WP_011985455.1; NC_009675.1.
DR AlphaFoldDB; A7H9F3; -.
DR SMR; A7H9F3; -.
DR STRING; 404589.Anae109_1141; -.
DR EnsemblBacteria; ABS25349; ABS25349; Anae109_1141.
DR KEGG; afw:Anae109_1141; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 61243at2; -.
DR Proteomes; UP000006382; 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..970
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008196"
FT DOMAIN 469..638
FT /note="tr-type G"
FT REGION 54..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..485
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 503..507
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 524..527
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 578..581
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 614..616
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 524..528
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 578..581
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 970 AA; 102676 MW; 0F0A412ECB1B9331 CRC64;
MSKKRVHELG KQLKEQGIEL SNQELVEKLL HLGYDVKSHS SSLEDDQAHA AYEKILAERK
PKAAPARPSG PGFVVRKRAH VEPPPVQEAQ PVEAQPSYEE QPSYEEQPSY EEQPSLEEPA
EVAAEAAPEP VEEPASSPEG GAPAGGAEPQ PAPEAPPPSA APAMPAAPSA PPSPAVRPPA
PSVPAGAQPP GAPVRPAAPG VRPAAPGVRP AAPGVRPTGP GVRPSVPGGP RAPGQPTAPM
AAAPHGPGAQ PGQPAAPGPD PRTLRPTATQ AVVISRPLVP VRRVTPPTGA RTQFPAAPGP
RALGEVRELK VVPGSLGRER EFIDVSRDKR RGRTPGRPMS EEQAKSLSGK ELLQAAITDR
AYIPIRGKKK KPTKKGAKTQ ITEKAEHKKV IRVEESISVS ELSQAMGVKA SDLIRKLMQA
GTMATINQQI DADTAAFLAT EFGYTLEKKG FEVEEYIPEV EVDESKLVIR PPVVTVMGHV
DHGKTSLLDA IRQADVAAGE AGGITQHIGA YAVQTPQGPI TFLDTPGHEA FTAMRQRGAQ
VTDLVVLVVA ADDGVMPQTV ESIKAAKAAG VTILVAINKI DKPGATPERV MQQLTEYELV
AEQWGGSTIM LPVSARTKQG IPELLEYIAL QSEVLELKAN PEMLASGRVI EAKLEKGRGP
VATVLVEEGT LRVGDALVTG IHYGRVRAMM NERGEQVKEV PPGYPVEVLG LSGVPVAGDE
FDVVQDEKAA KEVAEHRAEK QRKKELGASR KATLEDLFAK AKSGGGKVLN VVVKADVQGS
SEAVTQALQK AATKKVGVKI LDSGVGAITK SDVLTAAAGN GIIVGFNTKP ESEIESIASQ
QGVKILLFDI IYEAVDKIRE EMAGLLEPII REKPLGKAEV RALFSIPKLG NIAGSAVTEG
VIKRAANVRV LRDRKVVYSG KIGSLKRLKD DVREVQTGFE CGIGIEGFSD VKPGDVIEAY
ELEEIRQSLD
