IF2_PROMT
ID IF2_PROMT Reviewed; 1183 AA.
AC Q46J13;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PMN2A_1025;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
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; CP000095; AAZ58515.1; -; Genomic_DNA.
DR RefSeq; WP_011295370.1; NC_007335.2.
DR AlphaFoldDB; Q46J13; -.
DR SMR; Q46J13; -.
DR STRING; 59920.PMN2A_1025; -.
DR PRIDE; Q46J13; -.
DR EnsemblBacteria; AAZ58515; AAZ58515; PMN2A_1025.
DR KEGG; pmn:PMN2A_1025; -.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR PhylomeDB; Q46J13; -.
DR Proteomes; UP000002535; 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; Reference proteome.
FT CHAIN 1..1183
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228226"
FT DOMAIN 675..847
FT /note="tr-type G"
FT REGION 65..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..691
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 709..713
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 734..737
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 788..791
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 824..826
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 65..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 684..691
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 734..738
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 788..791
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1183 AA; 128121 MW; 7ECFDD0DC206B4C0 CRC64;
MTSSGKIRIY ELSKDLSLDN KDVLDAARKL AIAAKSHSSS ISSLEANQIK DFLKKSNTIN
TTIKSSKNLD KQILSVKKNP VKTQKDQKTE PKKKNHDQTE LSQAKLNTLL KPSQTLIKSQ
GSSQANNQKA LKNKFPAKQQ ITSPSKPNKP LPPNPRVEVK PIISKPLTQA ERAIPQSEQK
KDGQFINQPK RSELAKKSIG QPKQINPQEP KRPLAPPSRP KIDIQDKKPL QPNNQKAKTR
INQGEISPQK VGQGNIQKIK SQNKQNAPSR TPQPPTKGNT LELVGAPIRK EKPVNKPHTN
EVRNKPVMPS RPGAPKPPTA ANRQGLSNRP GSNNRIGGTG RPGSPNRQGP NRGGVANRTT
QGQNRPGANN RAGAPVRSGS PNRGGMQNRP GVPTRSLGGP NRSNNRPGVP SGMRKPVAPS
ELMQLQKPQA RPNAPQRKTD SPTSLRPKRE NSTGARPPVN RPTPAAPKKP AHRPGGTAAA
PRRTGRPDWD DSAKLDALRN KSPQKQRQKV HIIGENDDAL TAERGGFAGE QQAVVLSASL
ARPSKPKVGK RNNGKPLTAL KKRKKETTRQ RQRRRAMELR ASREAKLVRP EMIVVPEDNL
TVQELADMLS VESSEIIKSL FFKGITATVT QSLDLATIET VAEEFGVPVL QDDVEEAAKK
TVEMIEEGDL KYLIRRPPVV TVMGHVDHGK TSLLDAIRKA RVAAGEAGGI TQHIGAYQIE
TEHDGSTKKL TFLDTPGHEA FTAMRARGTR VTDVAILVVA ADDGVRPQTL EAISHARAAK
VPIVVAINKI DKEGSSPDRV KQELSEQDLL SEEWGGDVVM VPVSAIKGEN IDKLLEMVLL
VTEVEDLQAN PDRLAKGTVI EAHLDKAKGP VATLLVQNGT LKSGDVVAAG PVLGKVRAMV
DENGSRIKEA GPSCPVEALG FSEVPTAGDE FEVYPDEKAA RAVVGERATD ARAARLAQQM
ASRRVSLSSM SGQASEGELK ELNIILKADV QGSLEAILGS LEQLPKDEVQ VRVLLSAPGE
ITETDIDLAA ASGAVIVGFN TSMASGAKRA ADANGVDVRE YEVIYKLLED IQLAMEGLLE
PEMIEEALGV AEVRAIFSIG KSAVAGCYVT NGKIQRNCRA RVKRGKQIVF EGDLDSLKRN
KDDVKDVSTG FECGIGCDRF ANWEEGDQIE AFKLVTQRRK LNN
