IF2_ACISJ
ID IF2_ACISJ Reviewed; 943 AA.
AC A1W8Z4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ajs_2561;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000539; ABM42719.1; -; Genomic_DNA.
DR RefSeq; WP_011805756.1; NC_008782.1.
DR AlphaFoldDB; A1W8Z4; -.
DR SMR; A1W8Z4; -.
DR STRING; 232721.Ajs_2561; -.
DR PRIDE; A1W8Z4; -.
DR EnsemblBacteria; ABM42719; ABM42719; Ajs_2561.
DR KEGG; ajs:Ajs_2561; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000645; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..943
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335454"
FT DOMAIN 443..612
FT /note="tr-type G"
FT REGION 96..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..459
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 477..481
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 498..501
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 552..555
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 588..590
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 117..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 943 AA; 101832 MW; 3875EDAD6F8EC7A1 CRC64;
MSSNTVAEFA AELKKSPETL LDQLKSAGVV KVSPSDVLNE ADKQKLLAHL QASHGTAGGD
RKKITLVKKS TSEIKQADAS GKARTIQVEV RKKRTFIKRD DNVDAPSDAA ESAPSAEDLE
LVRREEEARR QAELIRRQEE ELALTRRERE ERERREREAE ERAAAYAAQQ AEKKAQESAE
RAEAQREAAV EAEERAKAQA DARAKADEES KARAAEETAR AADLDERRRK ALAEAEAIRA
MMAAPKKVLV AKKPEEPKPA AKAGASGDAK KGTLHKPATG SGTGARAAAP SAPGGAGKEV
KSAKLSSSWA NDTTKKKEIK TRGDSSGGVG RNNWRGGPRG RRGNDRDDQR QQQAATEFRV
LEVYVPETIT VAELAHKMAI KASEVIKSLM KMGQMVTINQ PLDQDTAMIV VEEMGHTAKV
AALDDPEAFT AEEVSSQDAE QLSRAPVVTV MGHVDHGKTS LLDYIRRSKV ASGEAGGITQ
HIGAYHVETP RGIVTFLDTP GHEAFTAMRA RGAQATDIVI LVCAADDGVM PQTKEAIKHA
KAAGVPIVVA LTKADKPEAN IERVKQELVG EQVVPEEYGG DSPFVAVSSK TGMGIDALLE
QVLLQAEVLE LKAPVDAAAK GIVIETQLDK GRGSVATVLV QSGTLKVGDV VLAGQTFGRV
RAMLDEDGKQ TKEAGPSIPV EIQGLNEVPQ AGDDFMVLQD ERRAREIATY RAGKFRNTKL
AKQQAAKLEN MFAEMGAGEV QTLPLIIKAD VQGSQEALAA SLLKLSTEEI RVQIVYSGVG
GISESDVNLA IASKAIVIGF NVRADAQARK TAEGNDVDIR YYNIIYDAVD EVKAAMSGML
APEQREEAIG TAEIRTVFVA SKIGTVAGSY ITSGQVTRNC KFRLLRDNIV IYTGDVESVR
RMKDDVKEVK EGFECGIKLK NYNDIKEGDQ LEFFEIKEIA RTL
