IF2_PSYWF
ID IF2_PSYWF Reviewed; 905 AA.
AC A5WBS5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=PsycPRwf_0157;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) 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; CP000713; ABQ93116.1; -; Genomic_DNA.
DR RefSeq; WP_011959452.1; NC_009524.1.
DR AlphaFoldDB; A5WBS5; -.
DR SMR; A5WBS5; -.
DR STRING; 349106.PsycPRwf_0157; -.
DR EnsemblBacteria; ABQ93116; ABQ93116; PsycPRwf_0157.
DR KEGG; prw:PsycPRwf_0157; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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; 1.
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.
FT CHAIN 1..905
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000071291"
FT DOMAIN 406..575
FT /note="tr-type G"
FT REGION 52..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..422
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 440..444
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 461..464
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 515..518
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 551..553
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 67..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..422
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 461..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 515..518
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 905 AA; 99298 MW; A59D99309D3B2BE1 CRC64;
MADKTVKELA DMVSKTVSAV QKQLTDAGLP ARGEDDLVTE LEQEQLVAFL KQSHGQKEKR
RISLKSKTTS TARVTGSSGK SKSVNVEVRK KKVFEKPDPN KLAEEIAARE QAALEAKKRA
EEEAKKREQV KKEAEERQAA TLAAMRANLG GGSSSSDKKE ELSTVVVKKG SKAAAAAKEA
PKKKVAQTKP KVETAAERKA RETREAEEER LRQIEAETRR KQAEEAQKKT LEQMRKMAGK
YSDKDPVAEV RKDEPLAEGL VGEALEESFE KERREIKRGS ASTATRGRRR KGQEEREIRN
RKHGLKSSQA SQHKFEKPVE KIVHDVEIGE QIVVSDLAQR MAVKAREVTK LLMKMGEIVS
ADQEIDQATA SLIVEEMGHN PIPVSDTKVE DDLQEAVEER RSNVQTRPPV VTIMGHVDHG
KTSLLDKIRE TKVATGEAGG ITQHIGAYHV ETDRGVITFL DTPGHAAFTA MRSRGAQATD
IVILVVAADD GMMPQTEEAI DHARASGTPL IVAINKMDKS TADPDRVLNE LTTKEVVTEA
WGGDVPMAKI SAKTGEGIDE LLELINLQAE LMELEAPTDG AAQGVVIESR LEKGRGAVAS
ILVKKGTLNQ GDLVLAGEFY GKVRAMTDET GKRVKSAGPS IPVEILGLPD TPAAGSEFLV
VSDEKKAREV AEFRATRERE RQLERQNKMR LESMFEQMGQ DDLSFLNIIL KTDVRGTLEA
LLAALEDLST DEVKVKVISS GVGPIAESDV TLAESSEAVL LGFNVRADNA AKRKADEAGI
DIRYYSVIYG LIDDVKAAMS GMLSPEHREK ILGIAEVRDV FRSSKFGAAA GCMVVEGTIY
RNKSIRVLRD DKVAFTGQLQ SLRRYKDDVN EVRSGMECGL AVRGYDVEVG DKIEVFEIQE
IQRTI
