IF2_CYAP4
ID IF2_CYAP4 Reviewed; 1005 AA.
AC B8HUA9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Cyan7425_2091;
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX NCBI_TaxID=395961;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7425 / ATCC 29141;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001344; ACL44454.1; -; Genomic_DNA.
DR RefSeq; WP_012627533.1; NC_011884.1.
DR AlphaFoldDB; B8HUA9; -.
DR SMR; B8HUA9; -.
DR STRING; 395961.Cyan7425_2091; -.
DR EnsemblBacteria; ACL44454; ACL44454; Cyan7425_2091.
DR KEGG; cyn:Cyan7425_2091; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; NIAVKSH; -.
DR OrthoDB; 347113at2; -.
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..1005
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118758"
FT DOMAIN 495..668
FT /note="tr-type G"
FT REGION 54..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..511
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 529..533
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 554..557
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 608..611
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 644..646
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 70..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 554..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 608..611
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1005 AA; 108397 MW; 34189E8AFDF548A7 CRC64;
MSNNKVRIYD LSRDLNLDNR DVLIICEQLN IPVKSHSSTI SESEADRIRA AAEKYVPSPS
THSMPPTRPT SHSRPLPPQP GKPQPKVPQT KVPQILELRR HQTPAEPATG SAGSSVAPVS
RSPVEPQAGL PKTASPQRPV RPAAPGSNSP SHSESTPVTP PAISKPAVSS SPARTEPLRP
AVPPPKAAPS PAAMAGRAEP SQPGPQKPVL KRPKVESPQA EVESAPVATA TPAPASPRAE
LTPPPRRELP QLKAPPRPRS ETSEDGARRG EKLVARAPEP PGTETDAIEV LQNVSLPKLA
GRGAKRPKTK AEEEDELQEE LAAKTPKTAT KLKRRPQLKL EDEDDVDFAA EVNVQAVVDV
SQSLVRPPKP KAAKSAKPAA VATTRISAPK TGGRKLSRRD RRQQEETQER PTSVVLSGDL
TVQELANRLA LPTSEIIKTL FFKGIAATIN QMLDLETASM VAREMGMEVE TPEVESTARK
VTEMLEAQDL ENLQRRPPVV TIMGHVDHGK TTLLDAIRQT KVAQGEAGGI TQHIGAYHVD
VEHEDQVQQV VFLDTPGHEA FTAMRARGAR VTDIAILVVA ADDGVRPQTV EAISHAQAAE
VPIVVAINKI DKPTAQPDRV KQELTEYNLV PEEWGGDTIM VPVSAINREN LDTLLEMILL
VSEVEDLYAN PDRSARGTVI EAHLDKARGP VATLLVQNGT LRVGDILLAG SALGKVRAMI
DDRGQRVEAA TPSFAVEVLG LGDVPAAGDE FEVFNDEREA RAIANERANQ QRLSRLQQAL
SSRRVSLTSL SDQAREGELK ELNLILKADV QGSVEAILNA LGQIPQNEVQ LRVLYAAPGE
VTETDVDLAA ASNAVVIGFN TTLASGSRAS ADQTGVDIRE YNIIYKLLDD IEGAMEGLLE
PELVEEPLGQ AQVRAVFPVG KGFVAGCYVQ SGKLIRNCKI RVLRSGNLVH SGTLNSLKRI
KEDAREVNAG YECGIRLDDF QGWAEGDQIE AYQMVTKRRT LNPNA
