IF2_GEOSM
ID IF2_GEOSM Reviewed; 980 AA.
AC C6E2Q0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=GM21_2981;
OS Geobacter sp. (strain M21).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter; unclassified Geobacter.
OX NCBI_TaxID=443144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001661; ACT19010.1; -; Genomic_DNA.
DR RefSeq; WP_015838229.1; NC_012918.1.
DR AlphaFoldDB; C6E2Q0; -.
DR SMR; C6E2Q0; -.
DR STRING; 443144.GM21_2981; -.
DR EnsemblBacteria; ACT19010; ACT19010; GM21_2981.
DR KEGG; gem:GM21_2981; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_3_7; -.
DR OMA; QVRPEMI; -.
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; 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.
FT CHAIN 1..980
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000202773"
FT DOMAIN 480..647
FT /note="tr-type G"
FT REGION 47..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..496
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 514..518
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 535..538
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 589..592
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 625..627
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 535..539
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 589..592
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 980 AA; 104584 MW; 68C0498438C6D0D2 CRC64;
MSKTRVYELA QQMGIDNKEL MARLADAGVS VKNHMAVLED SDIKALSAPA QTPHKEVSQE
EVRVKPTLIR RRAKAVEPEA AAAEAAPAPA AQEEAPLKAE PEKVEPEKAE APKPRQAAEP
VRARIIEAAP VPKPAAAPAE AAKPEKEKPA EPAPAPKAAE APAAPAAEAA PAPAPAPTEA
PAAKPEAPAP TAPAAPVAAA PAEAQAPAKV EEPEPEKATP TRARILGRVE IPIPAQRPAE
RREYQRTAPG ERPAPRPGMP RGVERPGTER PAPRPGGPRP AGAPGRPGER PTTGRPGGPA
GGRPDRPAPL APIDAPPLLG DDRRKGRKPA PAGGTDYAKN GKKGAPAAAG KGKKETFKDI
LDKRERVFEP GPRSKGKKGK YEKVQIGKKT EITVPKAIKR IIKISESITV GELAKRMGIK
ATDLIRALMK LGVMATINHP LDFDTATLLA TDFGYEIENV ALDVDEILEA EPDAPESLLK
RPPVVTIMGH VDHGKTSLLD AIREANVIAG EAGGITQHIG AYDVELNGKK ITFLDTPGHE
AFTAMRARGA KVTDIVILVV AADDGVMPQT REAVNHSKAA GVPIIVAINK IDKPDASPGK
VKQELMEFGL VSEEWGGETI FVEVSAKKRI NLESLLEMVL LQADVLELRA NPEKAARGTV
VEAKLDKGRG PVATILVQEG TLKSGDYFVA GVHYGRVRAM QNDRGEKVLA AGPAMPVEVI
GFNGVPDAGD IFVAMGDEKQ AKEIANHRQM KLRESELAKH SKLSLEQLYE KIQKGEVKDL
NAIVKGDVQG SVEAVAESLR KLSTDAIRLN VLHASVGAIT ETDVNLASAS NAIILGFNVR
PEVKAAALAE KEGVDVRLYN IIYDAVDDIK KAMEGLLEPT FKEKYLGRAE IREVFSVPKA
GMVAGSYVTD GKIVRNAQVR LLRDNMVVYE GKLGSLRRFK DDVKEVATGY ECGMSLENYN
DLKVGDIFEC FEMEKVAGKL
