ID   IF2_DINSH               Reviewed;         832 AA.
AC   A8LQ56;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=Dshi_3563;
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
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; CP000830; ABV95296.1; -; Genomic_DNA.
DR   RefSeq; WP_012180219.1; NC_009952.1.
DR   AlphaFoldDB; A8LQ56; -.
DR   SMR; A8LQ56; -.
DR   STRING; 398580.Dshi_3563; -.
DR   KEGG; dsh:Dshi_3563; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_10_1_5; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000006833; 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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
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..832
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000075604"
FT   DOMAIN          329..497
FT                   /note="tr-type G"
FT   REGION          1..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..345
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          363..367
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          385..388
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          439..442
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          475..477
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         338..345
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         385..389
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         439..442
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   832 AA;  89918 MW;  D82A655A1AA34A03 CRC64;
     MSDTDGKKTL GLRGGSRTGQ VKQSFSHGRT KNVVVETKRK RVLVPKPGAS ASGGRGSDPK
     KPGNATDAEM ERRLRALRAA KANESEEAER RAAEEKAREE ERARRRAEIE AKEREEQERE
     ERARQKAEEE EEARKKAEAD ASSKPAAARS KADDPATMDP AAAQAAEARG AGKTGSGPRK
     ERTADRAQPR KEQKGKGDDR RRSGKLTLNQ ALSGDGGRQK SMAAMKRKQE RERRKAMGGS
     QEREKIVRDV QLPETIVVQE LANRMAERVA DVVKALMKMG MMVTQNQSID ADTAELIIEE
     FGHKVVRVSD ADVEDVIATV EDDPADMQPR PPVITVMGHV DHGKTSLLDA IRNAKVVAGE
     AGGITQHIGA YQVTTDDGTK LSFLDTPGHA AFTSMRARGA QVTDIVVLVV AADDAVMPQT
     IEAINHAKAA KVPMIVAINK IDRPEANPDK VRTDLLQHEV IVEKLSGDVQ DVEVSAINGT
     GLDQLLESIA LQAEILELKA NPDRAAEGAV IEAQLDVGRG PVATVLVQKG TLRRGDIFVV
     GEQWGKVRAL INDQGERVDE AGPSVPVEVL GLNGTPEAGD VLNVVETEAQ AREIAEYRES
     AAKEKRAAAG AATTLEQLMA KAKSDETVAE LPIVVKADVQ GSAEAIVQTM EKIGNEEVRV
     RVLHSGVGAI TESDIGLAEA SGAPVFGFNV RANAPARNAA QQKGVEIRYY SIIYDLVDDV
     KAAASGLLSA EVRENFIGYA EIREVFKVSG VGKVAGCLVT DGIARRSAGV RLLRDNVVIH
     EGTLKTLKRF KDEVKEVQSG QECGMAFENY DDIRPGDVIE IFEREEVERN LE
//