IF2_NOSS1
ID IF2_NOSS1 Reviewed; 1039 AA.
AC Q8YQJ1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=alr3832;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB75531.1; -; Genomic_DNA.
DR PIR; AI2284; AI2284.
DR RefSeq; WP_010997973.1; NZ_RSCN01000011.1.
DR AlphaFoldDB; Q8YQJ1; -.
DR SMR; Q8YQJ1; -.
DR STRING; 103690.17132966; -.
DR EnsemblBacteria; BAB75531; BAB75531; BAB75531.
DR KEGG; ana:alr3832; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR OMA; NIAVKSH; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002483; 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..1039
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137165"
FT DOMAIN 533..706
FT /note="tr-type G"
FT REGION 39..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..549
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 567..571
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 592..595
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 646..649
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 682..684
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 592..596
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 646..649
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1039 AA; 111596 MW; 91E0B2B1038071C0 CRC64;
MNNGKVRIYE LSKELNLDNK ELLAICDQLN IAVKSHSSTI SESEAESIRA AAEKLAATNG
TSKKELNATS HKPNSAPAGS RNRPAPPQKQ QQILEIRKPK ILRNTTSNAP EASVANNQIA
SSEANSPAPP RPFATPVSPM KPTAPSRPVP RNLSETPQKP AAPEAEPEAQ SQAPAKIAVE
KPEKSAQPRP GKPERQPKPQ LVAPPSRPTA EKLDLSEITG APGEKPILKR DRPRREDERD
QAKPRVAKPA QGETSSAPVQ KQARPAQGLV KPEQRVNRPG APSGDGIRPQ RPVRPSADAA
PVATPPRGVP GGGRGEAGDT AAIAPDLLDL KRPTPPRLAK GGKKWQEEEI IDEIKEKAGK
AGVKGKRVKP LVEDDFEDED LLDEEGLEIP ATVQVSLSIA RPPKPKAARS ASAATAAPIS
SPTTRGKRSS HNNRDQNRRQ ETEVKRERPE KVAVTGAMTV QELADLMAVA DTEIVKILFM
KGMAVSITQN LDIPTITLVG KELEIEVETA EPEAEARKVT EMIEVGDLEH LLRRPPVVTI
MGHVDHGKTT LLDSIRKTKV AAGEAGGITQ HIGAYHVDIV HDGKEQQIVF LDTPGHEAFT
AMRARGARVT DIAVLVVAAD DGVRPQTVEA ISHAQAAGVP IVVAINKIDK EGAQPDRVKQ
ELTQYGLTSE EWGGETIMVP VSAIRGENLD TLLEMILLVA EVGELSANPD RNARGTVIEA
HLDKAKGAVA TLLIQNGTLH VGDILLAGSA FGKVRAMVDD RGRRVDIAGP SFAVEVLGLS
DVPAAGDEFE VFDNEKEARA LASDRADKQR LSRLLQGRVT LTTLSAQAQE GELKELNLIL
KGDVQGSVEA IVGSLKQIPQ NEVQIRMLLT AAGEITETDI DLAAASGAVI IGFNTTFASG
ARQAADEAGV DVREYNIIYK LIEDIQGALE GLLEPELVEE PLGQTEVRAV FPVGRGAVAG
CYVQSGKLVR NCKVRVRRAG KVIYEGVLDS LKRMKDDARE VNAGYECGIG VDKFHDWAEG
DIIESYQMVT KRRTLALTR
