IF2_EHRCJ
ID IF2_EHRCJ Reviewed; 848 AA.
AC Q3YS01;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ecaj_0467;
OS Ehrlichia canis (strain Jake).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake;
RX PubMed=16707693; DOI=10.1128/jb.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68504.1; -; Genomic_DNA.
DR RefSeq; WP_011304582.1; NC_007354.1.
DR AlphaFoldDB; Q3YS01; -.
DR SMR; Q3YS01; -.
DR STRING; 269484.Ecaj_0467; -.
DR EnsemblBacteria; AAZ68504; AAZ68504; Ecaj_0467.
DR KEGG; ecn:Ecaj_0467; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000435; 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; 1.
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..848
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228194"
FT DOMAIN 346..516
FT /note="tr-type G"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..362
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 380..384
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 402..405
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 456..459
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 492..494
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 355..362
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 402..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 456..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 848 AA; 93816 MW; 59FD73ECC9C4A8E9 CRC64;
MNESKGAVDS GLMSGKTERT TLKLSDKLKL SSSIQQNTKF ALNKSITTVE VRKSKKRRDI
DNIEQASVVL QNDNVYQSDG DNNTLTIQEQ ISRMNALQNA NIHEKKEEVS DDQTDKKEEV
TNAETVGLLP VEENVNTDLV IEEGHSEKVE EVIEESVIED QPNLEHLDVI EEKNGPNQSG
DQNVDNSIVD LLQSKAVEEK KLKKYEKEHE EKKGNPKKGV SNHMYSKHVK LVIEEELEDN
NKQIIQTHKT RKNRSVSSIK NKITRKVLIP KKITVQELAS NMSERVKDVQ NMLFQMGRRD
IKPNDFLDSD QAAIIVEAFN HTFKLVNDGK LEDDLYSDGN DKELLPRAPV VTVMGHVDHG
KTSLLDAIRE SNVADGEFKG ITQHIGAYQI ILDGDKRITF IDTPGHEAFT AMRACGTNVT
DIVVLVVAAD DGIMPQTIES INHVKAANVA MIVAVNKIDK HDANLDKITN SLLNHGVVAE
SLGGDVIVVP VSAKEKINLD QLKSSILLMA ELLELKAIYN TRASGVVIES KIDKNCGVVA
TLIVQKGTLK SGDIIVVGHN SYGKVRNMFN SDGRSQKVAI PSMPVKVLGL NNVPNSGSSF
IVVDSEKQAR ELINYRQELF NASLEENAKS KMDASNILAC DVVDELNVIL KCDVMGSVEA
ICYSISKITH EDIKLNVLYK GVGNVTKSDV LLAETSNSII LAFNVKADAQ VKELAKQRCV
EINHYSVIYD IIDDVKRILS SMLKPLQQEV QVGALAIRKV FSSGNAGSVL GCYVTSGVVK
KGSLVKLIRN NTIIHEGKIK VLRRFKDDVK EVSSGFECGI LLDYSKEIYP ESDIINVLEV
IEEVRVIK
