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IF2_NOSP7
ID   IF2_NOSP7               Reviewed;        1056 AA.
AC   B2J955;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, 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}; OrderedLocusNames=Npun_R5773;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001037; ACC84071.1; -; Genomic_DNA.
DR   RefSeq; WP_012412014.1; NC_010628.1.
DR   AlphaFoldDB; B2J955; -.
DR   SMR; B2J955; -.
DR   STRING; 63737.Npun_R5773; -.
DR   EnsemblBacteria; ACC84071; ACC84071; Npun_R5773.
DR   KEGG; npu:Npun_R5773; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3266; Bacteria.
DR   HOGENOM; CLU_006301_7_0_3; -.
DR   OMA; NIAVKSH; -.
DR   OrthoDB; 347113at2; -.
DR   PhylomeDB; B2J955; -.
DR   Proteomes; UP000001191; 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..1056
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093808"
FT   DOMAIN          550..723
FT                   /note="tr-type G"
FT   REGION          60..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..566
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          584..588
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          609..612
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          663..666
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          699..701
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        62..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..146
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         559..566
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         609..613
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         663..666
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1056 AA;  114029 MW;  D461C43D67DF72E1 CRC64;
     MTNGKVRIYE LSKELNLDNK ELLAICDQLS IAVKSHSSTI SESEAENIRT AAEKLAATNV
     SAKKELGTTS HKPNSPPNGG RNRPAAPHKQ QILEIRKPKI LRNTTSNAPE ASVANNTQAA
     LSEANPPSPP RPFATPASPM KPAAPTRPVP RTQSETQEQP PVTDLEQTPN PSQAPEKVAS
     QKPEKVVPPR PKSEKPQKPQ LVAPPARPAA EVAQAEVAQV SDEPVSQADK PILKRDQRLR
     PVEGDREQIK PRVAKLPTDQ SPQSAPQRQA RPTPAPTRPE QRGNRPSAPS QLGEGQRPRP
     ARPGESVAAA MPIATPPRQM SGIAGKSQGL GDEPVTPDLL DLKRPSPPRP TKGGKKWVEE
     EIIDEVKEKA KAGVKGKRIK PILDDEFEED LLDDDDIDSP ATVQVSLSIA RPPKPKATRP
     VQMPGASLAS APTARGSRKP GSKSGSNRDH HNNRRQQEAD TKRDRPEKVT ITGPLTVQEL
     SDVLAVPDTE IVKILFLKGM AVSITQNLDI PTITLVGKEL EIEVETVERE AEARKITEMV
     GAEDQEYLHR RPPVVTIMGH VDHGKTTLLD SIRKTKVAAG EAGGITQHIG AYHVDVVHEG
     KPQQIVFLDT PGHEAFTAMR ARGARVTDIA VLVVAADDGV RPQTIEAISH AQAAGVPIVV
     AINKIDKEGA QPERVKQELT QYGLTAEDWG GETIMVPVSA IRGENLDTLL EMILLVAEVG
     ELSANPDRTA KGTVIEAHLD KAKGAVATLL IQNGTLHVGD ILVAGSAFGK VRAMVDDRGK
     RVDIASPSFA VEVLGLSDVP AAGDEFEVFQ NEKEARSLAS DRADRQRLSR LLQGRVTLTT
     LSAQAQEGEL KELNLILKGD VQGSVEAIVG ALKQIPQNEV QIRMLLATAG EITETDIDLA
     AASNAVIIGF NTTFASGARQ AADEAGVDVR EYNVIYKLLE DIQDALEGLL EPELVEEPLG
     QTEVRAVFPV GRGAVAGCYV QSGKLVRNCK VRVRRGGKVI YEGVLDSLKR MKEDAREVNA
     GYECGVGMDK FNDWVEGDII ESYQMVTKRR TLTLTR
 
 
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