IF2_PROMP
ID IF2_PROMP Reviewed; 1169 AA.
AC Q7UZZ9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PMM1494;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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; BX548174; CAE19953.1; -; Genomic_DNA.
DR RefSeq; WP_011133122.1; NC_005072.1.
DR AlphaFoldDB; Q7UZZ9; -.
DR SMR; Q7UZZ9; -.
DR STRING; 59919.PMM1494; -.
DR EnsemblBacteria; CAE19953; CAE19953; PMM1494.
DR KEGG; pmm:PMM1494; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_7_0_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001026; 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..1169
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137235"
FT DOMAIN 661..838
FT /note="tr-type G"
FT REGION 69..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..677
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 695..699
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 720..723
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 774..777
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 810..812
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 670..677
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 720..724
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 774..777
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1169 AA; 127148 MW; 0705D909F5377562 CRC64;
MTISDKIRVY ELSRDLKLEN KDILDAAQKL SISVKSHSSS ISLEDAKKIK NLINKNSSKK
ILSVSKSAIK AKNENPKNND NKNNKNFSNP SHPEKLSKEG LNKKPLLIKP TNKVVNSLVS
SNIKNPNPPT IVSNLKSQAL SKNQNKTNTS VITTPNLKDK KNPSALQDKK PLKNSSGSPA
KTTARPPIQL IEKPKNLANS NRNINANKIN NSVNQKAQSL NRADNNKLSR ADNNNFPKKN
LNSPNVKSTP ELVGAPIRRE DPKINTNRPN SNSRQPSSNT QISANRPGGQ NRQGVPNREG
GPYRQGSPNR PGTPYRQGAP NRPGGQNRQG VPNREGGGPY RQGSPNRPGT PNRPGTPYRQ
GAPNRPGGQN RQGVPNREGG GPYRQGSPNR PGTPYRQGAS GIRKPVAPNE LMQLQKTNAS
NKEKPNISNV NKQKIEGANQ KTKAPNSRLN TSPSPTAKKP ARSFASNTKK PGRTDWDDSA
KLEALRNKNP QKQRQKVHII GENDDSLTSE TSGYSGEKVS ILSASLARPK KEKSEEIKSQ
KPSKQFKKKK KETTRQRQKR RAMELRAAKD AKQVRPEMII IPEDNLTVQE LADKLSLESS
EIIKSLFFKG ITATVTQSLD LATIETVAEE FGVPVLQDDV QEAAKKTVDM IETDDIESLI
KRPPVITVMG HVDHGKTSLL DSIRESRVAS GEAGGITQHI GAYQVEFEHE SKKKKLTFLD
TPGHEAFTAM RARGTKVTDV AVLVVAADDG CRPQTLEAIS HARAAKVPIV VAINKIDKEG
ASPDRVKQEL SEKDLIAEDW GGDVVMVPVS AIKKQNIDKL LEMILLVSEV EDLQANPERL
AKGTVIEAHL DKAKGPVATL LVQNGTLKAG DVLAAGSVLG KIRAMVDEHG NRIKEAGPSC
PVEALGFSEV PTAGDEFEVY RDEKSARAIV GDRATDARAT KLAQQMASRR VSLSSLSTQA
NDGELKELNL ILKADVQGSV EAILGSLEQL PKNEVQVRVL LSAPGEITET DIDLAAASGS
VIIGFNTSLA SGAKRAADAN DVDIREYEVI YKLLEDIQSA MEGLLEPDLV EESLGQAEVR
ATFAVGKGAI AGCYIQSGKL QRNCSLRVLR SDKVIFEGNL DSLKRSKDDV KEVNTGFECG
VGCDKFSTWS EGDIISAFKF VTKKRTLNK
