IF2_PROMA
ID IF2_PROMA Reviewed; 1134 AA.
AC Q7VA20;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pro_1649;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00693.1; -; Genomic_DNA.
DR RefSeq; NP_876040.1; NC_005042.1.
DR RefSeq; WP_011125799.1; NC_005042.1.
DR AlphaFoldDB; Q7VA20; -.
DR SMR; Q7VA20; -.
DR STRING; 167539.Pro_1649; -.
DR EnsemblBacteria; AAQ00693; AAQ00693; Pro_1649.
DR GeneID; 54200973; -.
DR KEGG; pma:Pro_1649; -.
DR PATRIC; fig|167539.5.peg.1744; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001420; 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..1134
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137233"
FT DOMAIN 626..798
FT /note="tr-type G"
FT REGION 55..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..642
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 660..664
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 685..688
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 739..742
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 775..777
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 635..642
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 685..689
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 739..742
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1134 AA; 122018 MW; B275B573663C2CA6 CRC64;
MTSSGKIRIY ELSRDLHLEN KDVLDAANKL SISAKSHSSS ISDEDATKIK KLLLAQKSSN
SSSPPAKQKP NKEILTLKKA ITSPPTKSEA NAKTNASLDK TSSLKNKPAS PKKEIPTSPK
PPSAAKQRVD AIKKPTPSIS KNNSLKVQPT IKKPSLVSPK QPNIPSPPIA PNKGIKPTIK
RQDSNNENLE TNKTKAKPNI VSKPQARQIK QSSDLINRSP KTSPKQPIQE IQTNKPKAPQ
RPIAPPPRPK VQSQFNQKPG NNNLRGGPNQ RKGIPQGAPS GQPGSTKHPR NLPTGSYKGN
RVELVGAPIR RNTKPDNGGR GARDGNFRQG GPNQGPPISR QGGARRQEGG GGRGQQMRPR
TGMPPGMRKP VAPGELMQLQ KPTSSATPPI KRGDLNKGPK KDGISTAKPP ANRPTPSAAP
KRPPARTGAP GSSRKRKPDW DDAAKLEALR NKSPQKQRQK VHIIGENDDA LTAETSGFAG
GGQAVVLSAS LARPGKPKAS KKSGSKPTGA LRKRKKESTR QRQRRRAMEL RAAREAKQIR
PEMIVVPEDN ITVQELADKL SVESSEIIKS LFFKGITATV TQSLDLSTIE TVAEEFGVPV
LQDDIEEAAK KTVEMIEETD IKHLTRRPPV VTVMGHVDHG KTSLLDAIRK ARVAAGEAGG
ITQHIGAYQV EVEHEKKLRT LTFLDTPGHE AFTAMRARGT KVTDVAVLVV AADDGVRPQT
LEAISHARAA KVPIVVAINK IDKEGASPDR VKQELSEQEL VAEEWGGDVV MMPVSAIKGE
NIDKLLEMIL LVTEVEDLQA NPARLAKGTV IEAHLDKAKG PVATLLVQNG TLKAGDVVAA
GPVLGKVRAM VDENGKRLKE AGPSCPVEAL GFNEVPTAGD EFEVYPDEKS ARSVVGERAS
DARATRLAQQ MASRRVSLSA MSGQVNDGDL KELNLILKAD VQGSVEAILG SLEQLPKDEV
QVRVLLSAPG EITETDVDLA AASGAVIIGF NTSMASGAKK AADANSVDVR DYEVIYKLLE
DIQLAMEGLL EPDLVEEKIG EAEVRAIFTI GKSAVAGCYI TNGKLQRNCK VRVKRADQIV
FNGDLDSLRR NKDVVKDVSS GFECGIGCDR FANWKEGDTI EGYKLVTQRR KLNT
