IF2_IDILO
ID IF2_IDILO Reviewed; 896 AA.
AC Q5QTY8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=IL0968;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV81808.1; -; Genomic_DNA.
DR RefSeq; WP_011234219.1; NC_006512.1.
DR AlphaFoldDB; Q5QTY8; -.
DR SMR; Q5QTY8; -.
DR STRING; 283942.IL0968; -.
DR PRIDE; Q5QTY8; -.
DR EnsemblBacteria; AAV81808; AAV81808; IL0968.
DR KEGG; ilo:IL0968; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001171; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228204"
FT DOMAIN 396..565
FT /note="tr-type G"
FT REGION 46..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..412
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 430..434
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 451..454
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 505..508
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 541..543
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 84..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405..412
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 451..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 505..508
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 896 AA; 99178 MW; CB35F344197F31FE CRC64;
MEEVTLDKLA TDVGTTVDRL VQQFAEAGMT KKAGDSVNEE EKQKLLAHLN RQHGGGGSSE
PSKMTLKRKT KSTLSVGGGR DSKSVQVEVR KKRTYVKRSA SEEQEREEQE RLAQEKEAEE
AKLREEEKQR EEEQQRKEAE AKAKAEREKA EKEKAEKEKL RKEKEKERQK AEAEKRAAMT
PEEREAADKA KADAEKLKRQ QEEEARKKAE KEAEAQAEEA RKLAEENAKR WEEEEQKRKQ
QEKEDVHFTT SSTAQEAEDA QDFDEERKSR KRGKKRRRKD EESDDTPRRE KRRKGARRGS
SLQQGFNKPA QPVERDVKIG ETITVGELAN RMAVKASDLI KTMMKMGEMV TINQILDQDT
AALVVEELGH KPALVKDNAL EEEVLSDRQE GGEEAPRAPV VTVMGHVDHG KTSLLDYIRK
AKVASGEAGG ITQHIGAYHV ETGHGMVTFL DTPGHAAFTS MRARGAGATD VVILVVAADD
GVMPQTKEAV QHAKAAGVPL VVAINKMDKE GADPDRVKNE LSQLEVIPED WGGDVQFIPL
SAHTGEGIDE LLEAILLQSE VLDLRAEKTG MASGIVVESR LDRGRGPVAT VLVQRGLLKQ
GDVVLCGLEY GRIRAMRDET GKEIKEAGPS IPVEILGLSG VPQAGDEATV VRDERKAREV
ANYRQGKYRD VKLAKQQKAK LENMFADMAE GDVAELNIVL KSDVQGSLEA ISDALTKLST
DEVKVNIIGS GVGGITETDI SLASASNAIV VGFNVRAEAA ARKLVEQESV DLRYYSVIYD
LIDEVKAAMS GMLQPEFKQQ IIGLAEVRDV FKSPKIGAIA GCMVTEGVVK RSAPIRVLRD
NVVIYEGELE SLRRFKDDVQ EVRNGMECGI GVKNYNDVKE GDQIEVFETI QIERTL
