IF2_FINM2
ID IF2_FINM2 Reviewed; 763 AA.
AC B0S1E5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=FMG_0767;
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(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; AP008971; BAG08185.1; -; Genomic_DNA.
DR RefSeq; WP_012290616.1; NC_010376.1.
DR AlphaFoldDB; B0S1E5; -.
DR SMR; B0S1E5; -.
DR STRING; 334413.FMG_0767; -.
DR EnsemblBacteria; BAG08185; BAG08185; FMG_0767.
DR KEGG; fma:FMG_0767; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001319; 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..763
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093785"
FT DOMAIN 265..434
FT /note="tr-type G"
FT REGION 52..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..281
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 299..303
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 320..323
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 374..377
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 410..412
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274..281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 320..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 374..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 763 AA; 85139 MW; F6C9FBAACCB734E4 CRC64;
MEKIRVYELA KQLNVSTKDL MSKLKDNKIE VKSHMSTLDK DQIAKVKSFY EKQKKVQTSQ
NNSKSNDENK KITNKNTEKT TEKISTVDSN KQNNSNKRFK PKHPRNNDEE SVSHFDKIKH
KNKSEMNEKR DLNDKKKNKN FKNTKNKNSN NNKNSKNNKN NKNNDHNRKD EAIKHETKEP
KKFIIQPTIT VKDLSEKISV SISELIMKLM ELGIMANQNQ EIDFDTASLV AGEFDVIVEQ
DEVEDFDDDD VFNLDFEDKK EDLKERPPVI TVMGHVDHGK TSILDRIRNS RVAGREAGGI
TQHIGAYTIR VNDKKIVFLD TPGHEAFTAM RSRGAQVTDV SILVVAADDG VMPQTIEAIN
HSKAAGVPII VAINKIDKEN ANIERVKTEL AENGLVPEDW GGDTVLVPVS ARTGEGIDDL
LEMILMVAEM EELKANPNRL AVGTVIEAQL DKGRGPTATI LVQKGTLKHS DMVFSGQASG
RIRAMFNDQG KQVKKAGPST PVLILGLNEV PEAGDMIYAV KDEKEARNYA QKIKDHNREE
QIKSSSTMNL DELFGKISDG ETKDLNIIIK TDVKGTIDAI KQSLIKLSNE EVKVNIIHGA
VGGITESDVN LASASSAIII GFNVRPTQVA MDMAKNESIE IRTYRVIYDA IEDVKNAITG
MLKPQYQEEV LGRATVRDTF KVPGVGTVAG VYVNTGKVTR NATVRLLRDE ILIFEGPVSS
LKRYKDDVKE LTQGYEGGMG LENYNDIKPG DVLEAYVLNE VQR
