ID IF2_PROM2 Reviewed; 1119 AA.
AC A8G6Z5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=P9215_17631;
OS Prochlorococcus marinus (strain MIT 9215).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93060;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9215;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000825; ABV51376.1; -; Genomic_DNA.
DR RefSeq; WP_012008392.1; NC_009840.1.
DR AlphaFoldDB; A8G6Z5; -.
DR SMR; A8G6Z5; -.
DR STRING; 93060.P9215_17631; -.
DR KEGG; pmh:P9215_17631; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000002014; 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; 1.10.10.2480; -; 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; 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; PF04760; IF2_N; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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.
FT CHAIN 1..1119
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057660"
FT DOMAIN 610..782
FT /note="tr-type G"
FT REGION 64..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..626
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 644..648
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 669..672
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 723..726
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 759..761
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 619..626
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 669..673
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 723..726
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1119 AA; 122886 MW; 986210AB529AE03E CRC64;
MTISDKIRIY ELSRDLNLDN KDILGAAQKL SISVKSHSSS ISAEEAEKIK NLINKKNPDK
KILSIKKPSI KKDNYKQNKE DKSSLISSVE EKPFKDNPEK KPLLKKPLNK PESLKIISNQ
PKSLNKPTIT NSSQSQANLT NQNLNSKTSQ NLNQDKRNFR NNLTPPIKSP TKPPIQLIAK
PKNTTKNVQS NESSQNILNS GGGRQISNKP DQNSSKSKTK NINNRMSPPE LVGAPIRREG
PNKQNNKQKT SFKQTVPNRP GMLNRPGLRN KPSDQGRPGS FNRQTNTNRP GAPSSNKPGM
PNRPGLRNKP SDQGRPGSFN RQVNTNRSGA PIRPGMPNRP GSKFNGPKSP GMRKPVSPNE
LLKLQKTNKS ENDKQVINNN EKQNSETTKQ KVKAPNSRPH TAPNSKKLPH RTFSNNSKKP
GKTDWDDSAK LEALRNKNPQ KQRQKVRIIG ENDDSLTSET SGYSGEKFSI LSASLARPKK
EKSDESKSQK TIKQFKKKKK ETTRQRQKRR AMELKAAKEA KQIRPEMIIV PEDNLTVQEL
ADKLSLESSE IIKSLFFKGI TATVTQSLDL ATIETVAEEF GVPVLQDDIQ EAAEKTVDMI
ESEDLDNLIK RPPVITVMGH VDHGKTSLLD SIRESRVASG EAGGITQHIG AYQVEFEHES
KKKKLTFLDT PGHEAFTAMR ARGTKVTDVA VLVVAADDGC RPQTLEAISH ARAAKVPIVV
AINKIDKEGA SPDRVKQELS EKNLIAEDWG GDTVMVPVSA IKKQNINKLL EMILLVSEVE
DLQANPDRFA KGTVIEAHLD KAKGPVATLL VQNGTLKSGD VLAAGSVLGK IRAMVDEHGN
RIKDAGPSFP VEALGFSEVP TAGDEFEVYP DEKTARAIVG ERATDARATK LAQQMASRRV
SLSSLSTQAN DGELKELNLI LKADVQGSVE AILGSLEQLP KNEVQVRVLL SAPGEITETD
IDLAAASGSV IIGFNTSLAS GAKKAADAND VDVREYEVIY KLLEDIQLAM EGLLEPDLVE
ESLGKAEVRA TFSVGKGAIA GCYIQTGKLQ RNCSLRVIRS EKVIFEGNLD SLKRSKDDVK
EVNTGFECGV GCDKFSSWIE GDIIEAFKFV TKKRTLTQE
//
