IF2_TRIV2
ID IF2_TRIV2 Reviewed; 1038 AA.
AC Q3MBZ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ava_1867;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA21489.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3MBZ7; -.
DR SMR; Q3MBZ7; -.
DR STRING; 240292.Ava_1867; -.
DR EnsemblBacteria; ABA21489; ABA21489; Ava_1867.
DR KEGG; ava:Ava_1867; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; NIAVKSH; -.
DR Proteomes; UP000002533; 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.
FT CHAIN 1..1038
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008197"
FT DOMAIN 532..705
FT /note="tr-type G"
FT REGION 39..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..548
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 566..570
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 591..594
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 645..648
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 681..683
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 427..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 541..548
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 591..595
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 645..648
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1038 AA; 111597 MW; 8314C56B675FBABD CRC64;
MNNGKVRIYE LSKELNLDNK ELLAICDQLN IAVKSHSSTI SESEAESIRA AAEKLAATNG
TSKKELNTTS HKPNSAPAGS RNRPAPPQKQ QQILEIRKPK ILRNTTSNAP EASVANNQIA
SSEANSPAPP RPFATPVSPM KPTAPSRPVP RNLSETPQKP AAPEAEPEAQ SQAPAKIAVE
KPEKSAQPRP GKPERQPKPQ LVAPPSRPTA EKLDLSEITG APGEKPILKR DRPRREDERD
QAKPRVAKPA QGETSSAPVQ KQARPAQGPV KPEQRVNRPG APSGDGIRPQ RPVRPSVDAA
PVATPPRGVP GGRGEVGDTA AIAPDLLDLK RPTPPRLAKG GKKWQEEEII DEIKEKAGKA
GVKGKRVKPL VEDDFEDEDL LDEEGLEIPA TVQVSLSIAR PPKPKAARAA TAATAAPISS
PTTRGKRSSH NNRDQNRRQE TEVKRERPEK VAVTGPMTVQ ELADLLAVAD TEIVKILFMK
GMAVSITQNL DIPTITLVGK ELEIEVETAE PEAEARKVTE MIEVGDLEHL LRRPPVVTIM
GHVDHGKTTL LDSIRKTKVA AGEAGGITQH IGAYHVDIVH DGKEQQIVFL DTPGHEAFTA
MRARGARVTD IAVLVVAADD GVRPQTVEAI SHAQAAGVPI VVAINKIDKE GAQPDRVKQE
LTQYGLTPEE WGGETIMVPV SAIKGENLDT LLEMILLVAE VGELSANPDR NARGTVIEAH
LDKAKGAVAT LLIQNGTLHV GDILLAGSAF GKVRAMVDDR GRRVDIAGPS FAVEVLGLSD
VPAAGDEFEV FDNEKEARAL ASDRADKQRL SRLLQGRVTL TTLSAQAQEG ELKELNLILK
GDVQGSVEAI VGSLKQIPQN EVQIRMLLTA AGEITETDID LAAASGAVII GFNTTFASGA
RQAADEAGVD VREYNIIYKL IEDIQGALEG LLEPELVEEP LGQTEVRAVF PVGRGAVAGC
YVQSGKLVRN CKVRVRRAGK VIYEGVLDSL KRMKDDAREV NAGYECGIGV DKFHDWAEGD
IIESYQMVTK RRTLALTR
