IF2_KINRD
ID IF2_KINRD Reviewed; 1044 AA.
AC A6W7Z2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Krad_1443;
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX NCBI_TaxID=266940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT "Survival in nuclear waste, extreme resistance, and potential applications
RT gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL PLoS ONE 3:e3878-e3878(2008).
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; CP000750; ABS02931.1; -; Genomic_DNA.
DR RefSeq; WP_011981930.1; NC_009664.2.
DR AlphaFoldDB; A6W7Z2; -.
DR SMR; A6W7Z2; -.
DR STRING; 266940.Krad_1443; -.
DR EnsemblBacteria; ABS02931; ABS02931; Krad_1443.
DR KEGG; kra:Krad_1443; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001116; 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 PRINTS; PR00315; ELONGATNFCT.
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..1044
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335480"
FT DOMAIN 537..709
FT /note="tr-type G"
FT REGION 31..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..553
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 571..575
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 596..599
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 650..653
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 686..688
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 546..553
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 596..600
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 650..653
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1044 AA; 107925 MW; 542FF970B9259760 CRC64;
MAKVRVYELA KEFGVESKVV LATLKEMGEF VRSASSTVEP PVIRRLKDKF PTEGGAASRP
APAVKPGPRL PQGARPGPAP AARPQAPAPA QPAPPQPAPA AASTPAPAPA PAPRPAEPAA
NPAPAAPPAF QAPAPAPAER PAAAQRPAAP APQRPAPAGR PSTPPVSGGP GQGPRPGARP
GGPGAPGARP GAPGAGGPGA RRPGPGDRPE RSERPDRGDR PQGDRPRSDR PQGERQQGDR
PQGDRPGRPG APGGAPRPGA GAPRPGNNPF APSQGMPRSQ GDRPGGAPRP GNNPFASNQG
MPRPQGGPRP TPAGPGGPRP GGPRPNPGMM PARPTVGRPG AGPGAGRPGA PGRGGPGGAR
GGAGGGFAGR PGGPSAGGGG GGFAGRPGGG GGGPRGNRGG TQGAFGRAGG RPVRGRKSKR
AKRQEYEAMQ APAVGGVSVR HGDGTTVLRI RRGASLSDFA ERIDADPAAL VTILFHLGEM
ATATQSLDED TFQLLGGELG YVIEVVSPED EERELLAGFS IDLDAELEAE GDDDLSARPP
VVTVMGHVDH GKTKLLDAIR SSDVVAKEAG GITQHIGAYQ VVKEHEGIER PITFIDTPGH
EAFTAMRARG AKVTDIAILV VAADDGVMPQ TIEALNHAQA ADVPIVVAVN KVDKEGANPD
KVRQQLTEYN LVAEEYGGDT MFVDVSARQG TGLDSLLEAV LLTADASLDL RANSDKDARG
IAIEGNLDKG RGPVATVLVQ SGTLHVGDAI VAGTGYGRVR AMLDENGDAV QEATPSRPVQ
VLGLTSVPGA GDTFLVAPDD RTARQIAEKR EAQERNAALA KARKRITLED FTKALQQGKV
ETLNLILKGD GAGSVEALED ALFKIDVGDE VELRVIDRGV GAVTKNNVNL AVASNAIIIG
FNVRPEQQTK EYADREGVDI RFYSVIYAAI EDVEASLKGL LKPEFEEVQL GTAEVREIFR
SSKFGNIAGT LVRSGLIRRN SKARVLRRGV VHGDNLTIES LRRFKDDATE VREGYECGIG
LGSYNDLQVD DVIETYEMQE KPRG
