IF2_DESPS
ID IF2_DESPS Reviewed; 939 AA.
AC Q6AJY4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=DP2613;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(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; CR522870; CAG37342.1; -; Genomic_DNA.
DR RefSeq; WP_011189854.1; NC_006138.1.
DR AlphaFoldDB; Q6AJY4; -.
DR SMR; Q6AJY4; -.
DR STRING; 177439.DP2613; -.
DR EnsemblBacteria; CAG37342; CAG37342; DP2613.
DR KEGG; dps:DP2613; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; MYCETSA; -.
DR OrthoDB; 244339at2; -.
DR Proteomes; UP000000602; 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; 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; Reference proteome.
FT CHAIN 1..939
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228191"
FT DOMAIN 437..606
FT /note="tr-type G"
FT REGION 51..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..453
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 471..475
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 492..495
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 546..549
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 582..584
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 446..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 492..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 546..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 939 AA; 101215 MW; A0A66F33B593F95F CRC64;
MSRIRIYELA KEAGMSGKAF ADKLIKKGYQ IKGHSSTVDD ATADEIRRTF LGTKESGQDT
GQATNEAAAA HRPTTVIGGK KVDEPVVPEK IVEEVQAVSV EVPKEVVAEE VKKSEPVKAE
KSEPVIQEVA PVVEELVTNK EAPTAPLERE EESQLKAQKP TIEKEESAAV AKPEVVSAGS
NEKKAGAPEI KRAEHTETVE KSKTAVDSKK VATPASTDKK VKPAQQPYRS GGVRVIGRVE
LPIQREEPSR PRRKPTRPPV NRSPRPSTPS PNRSAGGPPK PAAPATPAQD DSRNRKKKGR
RDEKPAERDS RPKAKGKKGV KFTHFGTDYQ NRGRRPRRGK RDAQTLPPSE MKASKKHVKV
YDTITVGDLA GRMKVKASDV IGKLMGLGLM ATINQSVDID TATLIATEYG YEVDQGITDE
LGIQLLTEAE EGGIEVGRCP VVTVMGHVDH GKTSILDAIR KTDVADGEAG GITQHIGAYH
VKAASGDVTF VDTPGHAAFT EMRSRGAQVT DIVILVVAAD DGVMDQTREA IRHSQAANVP
IIVAVNKIDK DNADVERVKR ELAELDLSPE EWGGTTMYCE TSAKQQIGID ELMESVQLAA
EMLELKANPD RKVIGRVLEA QLDKGRGPVA TILVQAGTLA KGDHFVVGQH SGKVRAMLDY
RGRSLAEAGP SIPVEVQGLS GVPSAGDEFV VVTDEKMAKA VSHDRAMKAR EAELGASTKI
SLDKLFEQMS EGEVRELRVV LRADVQGTLE AFAKAAADLS TKAIKVRLLH EGTGTITDSD
ILLASASDAI IIGFNVRPSA KVKALADKEH VDVRSYDVIY HALDDIRDAM VGMLDPTFEE
EIIGDAEVRD IFSVPKIGVI GGCYVTSGKI QRNAGVRVLR EGVVLYTGKI GSLRRFKDDA
KEVASGYECG IGVENFNNIK IGDVLEAFIM NEVAATLGE
