IF2_THEVB
ID IF2_THEVB Reviewed; 957 AA.
AC Q8DK04;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=tlr1066;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08619.1; -; Genomic_DNA.
DR RefSeq; NP_681857.1; NC_004113.1.
DR RefSeq; WP_011056909.1; NC_004113.1.
DR AlphaFoldDB; Q8DK04; -.
DR SMR; Q8DK04; -.
DR STRING; 197221.22294790; -.
DR PRIDE; Q8DK04; -.
DR EnsemblBacteria; BAC08619; BAC08619; BAC08619.
DR KEGG; tel:tlr1066; -.
DR PATRIC; fig|197221.4.peg.1120; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; NIAVKSH; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000440; 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..957
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137270"
FT DOMAIN 444..617
FT /note="tr-type G"
FT REGION 34..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..460
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 478..482
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 557..560
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 593..595
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 100..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 453..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 503..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 557..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 957 AA; 104247 MW; 13E9E041ADBC1280 CRC64;
MSIGKVRIYD LSKELNLDNR DLLAICEQLG IAYKSHSSTI SDADADRIRE AAKTYQPHSA
SPRKVSKTSP PVKKAPAPQK TQQIVAVHTQ PRSETPEAPK PQLQKPPARP QPPQAPTRPT
PPAPVAPKPV EPVAAKPPAP PAKPEPTPPR PVPTLVPPPT RPTKKEEKVA ATPPPRKELK
EPPKKEKGAI AAAKPSSQDR IEIVQRAVPP APAKPPEMAP KPALPELQPP PKPVRAPNPP
KPVTETVEVL DDKSVSKVIK DRHRHKDFDE EESKRKSSRV VKLREEIIDE EEELELTSRL
VGVHQVTVDV SQSLQRPPKP KVPRPARPVT PAAKTEKSSE KKQSRHRDRR PEEPAEAPPP
DHITIAGPMS VQELATLVRR PEAEIIKTLF FKGIAATINQ TLEVETIELV AKELGITVET
AEHKVEATKV TEMLESSDLD HLQRRPPVVT IMGHVDHGKT TLLDAIRNAK VAQGEAGGIT
QHIGAYHVDV EHNGEKHQVV FLDTPGHEAF TAMRARGARV TDIAVLVVAA DDGVQPQTIE
AISHAKAAKV PIIVAINKID KESAQPERIK QELTEYGLVP EEWGGDTIMV PVSALQQQNL
DTLLEMILLV AEVEDLYANP NRPAKGTVIE AHLDRARGPV ATLLVQNGTL RVGDILVAGA
CFGRVRAMID DRGQRVEAAT PSFAVEVLGL AEVPAAGDEF EVLSDEKAAR ALAEERAAAQ
RQSRLAQAAA ARRVSLTSLS SQAREGELKE LNLILKADVQ GSVEAILTAL NQLPQDQVQL
RVLLAAPGEI TETDVDLAAA SSAVIIGFNT TLASGARQAA EQHNVDIREY NIIYKLLDDI
QGAMEGMLEP ELVEEELGQA EVRAIFPLSK GVVAGCYVLN GKLVRNCKVR VLRQQQVIHT
GILSSLKRLK DDVREVAAGY ECGVRLDDFQ QWQEGDIIYA FQTVTKRRSL GSGSDRN
