IF2_PERMH
ID IF2_PERMH Reviewed; 875 AA.
AC C0QTL9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PERMA_0238;
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX NCBI_TaxID=123214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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; CP001230; ACO04790.1; -; Genomic_DNA.
DR AlphaFoldDB; C0QTL9; -.
DR SMR; C0QTL9; -.
DR STRING; 123214.PERMA_0238; -.
DR PRIDE; C0QTL9; -.
DR EnsemblBacteria; ACO04790; ACO04790; PERMA_0238.
DR KEGG; pmx:PERMA_0238; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_0; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001366; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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..875
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118770"
FT DOMAIN 379..547
FT /note="tr-type G"
FT REGION 123..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..395
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 413..417
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 525..527
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 240..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388..395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 435..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 875 AA; 98875 MW; 2F1553734CD66E16 CRC64;
MSKIKISDLA KEFGMTWKEL AGEIEELTGK TVKSPSTKID EEIVSLLRDV LQPAEEVEEA
VEKKVEKEKG YRIFELSHDW NIPFEELAED LKAIGYTKSI DNFTILDEET VNRLKDYIKE
KKEKEKEKKK EEKEEKKVKV EKKVEEKPVE VKKEEKKEEK VEKVEKKEEK VQKKPEKKEV
KRKEKIVAKE EKPERKKAVE EKPKKKEVKE VKKVEKPKVE VVEEKEETKI KIPEAEIRKE
TKEEKAELEA LRKLMGPQPK KKKKKKKKKE EEKAPVETKE KEEELKIAII PEVVTVRELS
DILDMPVNEI MAELLKRGIL ATVNQTIDPE IALQIAEEHG YLAEIQKEGE EVKIVEELPQ
EEKKKLLGEE EEEEENLVER PPVVTVMGHV DHGKTTLLDT IRKTDVAAKE KGGITQHIGA
YKIKLSNGKE ITFLDTPGHE AFTTLRARGS KVADIAVLVV AADDGVKPQT VEAINHAKSA
GVPIIVAINK IDKPGADPER VKRELAQYEL IPEEWGGDTI MVPVSAKTGQ NVEELLENIL
LVSEILELKA NPNRPAIGTI IESKLDPKRG PVATVLIENG TLHQGDYFVA GFTWGKVRAM
FDERGRQVKE ATPGTPVEVL GFNEVPQAGD KFVVKPSERE ARLLAEQRKQ KYEEELQAKR
TRIHLENLKD VKEINIILKA DVQGSLEAIT KSIEELSEKF EDVTINIIHS GIGAITESDV
MLAAASNALI IGFNVRPDAS ARKAAEEEDV DIKIYGIIYD LIDDLEKALK GMLTPKEREV
LLGICEVKQI FRIKGVGTVA GCMVTEGVIR RNAKARLVRD GVVIYDGEIT SLKRFKEDVK
EVAKGYECGL MLKDFNDIKP GDQIEAYEIV QEKAE
