IF2_DINSH
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 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Dshi_3563;
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Proteobacteria; 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 EnsemblBacteria; ABV95296; ABV95296; Dshi_3563.
DR KEGG; dsh:Dshi_3563; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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; 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; 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; 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..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
