IF2_PROMS
ID IF2_PROMS Reviewed; 1126 AA.
AC A2BT70;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=A9601_16981;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
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; CP000551; ABM70981.1; -; Genomic_DNA.
DR RefSeq; WP_011819109.1; NC_008816.1.
DR AlphaFoldDB; A2BT70; -.
DR SMR; A2BT70; -.
DR STRING; 146891.A9601_16981; -.
DR PRIDE; A2BT70; -.
DR EnsemblBacteria; ABM70981; ABM70981; A9601_16981.
DR KEGG; pmb:A9601_16981; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002590; 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..1126
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335500"
FT DOMAIN 618..790
FT /note="tr-type G"
FT REGION 63..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..634
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 652..656
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 677..680
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 731..734
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 767..769
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 627..634
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 677..681
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 731..734
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1126 AA; 123346 MW; 66644A55F26C1641 CRC64;
MTISDKIRIY ELSRDLNLEN KDILDAAQKL SISVKSHSSS ISSEEAKKIK NLINKKNPDK
TILSINKPSI KKDNFKQNKE DKSPVLSSKQ GKPLKNNSNK KPLLIKPLNK PESVKKISNQ
LQNPNKPNIV NSSQSRANLT NTNSKPSQNF NQDKKTFVNN TPPPIKSPAK PPIQLIAKPK
NINNNVKSSE SSQNIARAED KRRLSSKPDQ NTNKPKTKNF NNRKNTPELV GAPIRREDPI
INPNKQNNNK QNIAFKQTAS NRPGSPNRPG MPNRPGLRNK PSDQGRPGSF NRQGNPNRPG
SPNRPGMPNR PGLRNKPSDQ GRPGSFNRQG NPNRPGSPNG PGMPNNRPGS KFNGQNSSGI
RKPVSPNELL QLQKNNNSEK DKIGIKNNSK QNIEVPKQKA KAPNNRPNAT PSSKKPPHRT
FSNSSKKPGK TDWDDSAKLE ALRSKNTQKQ RQKVHIIGEN DDSLTSETSG YSGEKISILS
ASLARPKKGK SDESKSQKTI KQFKKKKKET TRQRQKRRAM ELKAAKEAKQ VRPEMIIVPE
DNLTVQELAD KLSLESSEII KSLFFKGITA TVTQSLDLAT IETVAEEFGV PVLQDDIQEA
AEKTVDMIES EDIDNLIRRP PVITVMGHVD HGKTSLLDSI RESRIASGEA GGITQHIGAY
QVEFEHESQK KKLTFLDTPG HEAFTAMRAR GTKVTDVAVL VVAADDGCRP QTLEAISHAR
AAKVPIVVAI NKIDKEGASP ERVKQELSEK DLIAEDWGGD TVMVPVSAIK KQNIDKLLEM
ILLVSDVEDL QANPDRFAKG TVIEAHLDKA KGPVATLLVQ NGTLKSGDVL AAGSVLGKIR
AMVDEHGNRI KEAGPSFPVE ALGFSEVPTA GDEFEVYPDE KTARAIVGER ATDARATKLA
QQMASRRVSL SSLSTQANDG ELKELNLILK ADVQGSVEAI LGSLEQLPKN EVQVRVLLSA
PGEITETDID LAAASGSVIV GFNTSLASGA KRAADANDVD IREYEVIYKL LEDIQLAMEG
LLEPDLVEES LGQAEVRATF SVGKGAIAGC YIQTGKLQRN CSLRVIRSEK VIFEGNLDSL
KRVKDDVKEV NTGFECGVGC DKFSSWVEGD VIEAFKFVTK KRTLSQ
