IF2_PROM9
ID IF2_PROM9 Reviewed; 1128 AA.
AC Q318P8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=PMT9312_1587;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) 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}.
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DR EMBL; CP000111; ABB50647.1; -; Genomic_DNA.
DR RefSeq; WP_011377129.1; NC_007577.1.
DR AlphaFoldDB; Q318P8; -.
DR SMR; Q318P8; -.
DR STRING; 74546.PMT9312_1587; -.
DR EnsemblBacteria; ABB50647; ABB50647; PMT9312_1587.
DR KEGG; pmi:PMT9312_1587; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002715; 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 PRINTS; PR00315; ELONGATNFCT.
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..1128
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008300"
FT DOMAIN 620..792
FT /note="tr-type G"
FT REGION 57..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..636
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 654..658
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 679..682
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 733..736
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 769..771
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 629..636
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 679..683
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 733..736
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1128 AA; 123936 MW; E9EEA8A72EE5AE7E CRC64;
MTISDKIRIY ELSRDLNLEN KDILDAAQKL SISVKSHSSS ISVEEAKKIK NLINKKNSDK
QILSINKPSN KKDNYKQNKE DKSPVISSVK GKPLKDNSNK KQLLNKPLNK PESLKVIPNQ
LKNPNKPNIY NSSQSQANLT NQNTKSKPSE HFNKDKKTFR NNTIPPIKTP AKPPIQLIAK
PKNINNNLKS NESSKNIPNS GDKRELSLKP DQNRNKPKPK NSNNRRNTPE LVGAPIRRDD
PNKQNNKQNI TFKQTVSNRP GTPNRPGTPN RPGMPNRPGL RNKPTDQGRP GSFNRQANPN
RAGAPNRPGM PNRPGLRNKP TDQGRPGSFN RQANPNRAGA PNRPGMPNRP GSRFNSQKST
GIRKPVSPNE LLQLQKTNKS EKDTLAKTNN QKQNIESPKQ KAKAPASRPN AVPSSKKPPH
RPFSNSSKKP GRKDWDDSAK LEALRNKNPQ KQRQKVHIIG ENDDSLTSET SGYSGEKISI
LSASLARPKK EKSEESKSHK STKQFKKKKK ETTRQRQKRR AMELKAAKEA KQVRPEMIIV
PEDNLTVQEL ADKLSLESSE IIKSLFFKGI TATVTQSLDL ATIETVAEEF GVPVLQDDIQ
EAAEKTVDMI ESDDFDSLIK RPPVITVMGH VDHGKTSLLD SIRESRVASG EAGGITQHIG
AYQVEFKHES KKKKLTFLDT PGHEAFTAMR ARGTKVTDVA VLVVAADDGC RPQTLEAISH
ARAAKVPIVV AINKIDKEGA SPERVKQELS EKDLIAEDWG GDTVMVPVSA IKKQNIDKLL
EMILLVSEVE DLQANPDRSA KGTVIEAHLD KAKGPVATLL VQNGTLKSGD VLAAGSVLGK
IRAMVDEHGN RIKEAGPSFP VEALGFSEVP TAGDEFEVYP DEKTARAIVG DRATDARATK
LAQQMASRRV TLSSLSTQAN DGELKELNLI LKADVQGSVE AILGSLEQLP KNEVQVRVLL
SAPGEITETD IDLAAASGSV IIGFNTSLAS GAKRAADAND VDIREYEVIY KLLEDIQLAM
EGLLEPDLVE ESLGKAEVRA TFAVGKGAIA GCYIQTGKLQ RNCSLRVIRS DKVIFEGNLD
SLKRSKDDVK EVNTGFECGV GCDKFSSWTE GDIIEAFKFV TKKRTLTQ
