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IF2_COLP3
ID   IF2_COLP3               Reviewed;         889 AA.
AC   Q482T9;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CPS_2203;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ24660.1; -; Genomic_DNA.
DR   RefSeq; WP_011043022.1; NC_003910.7.
DR   AlphaFoldDB; Q482T9; -.
DR   SMR; Q482T9; -.
DR   STRING; 167879.CPS_2203; -.
DR   EnsemblBacteria; AAZ24660; AAZ24660; CPS_2203.
DR   KEGG; cps:CPS_2203; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000000547; 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; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF46955; SSF46955; 1.
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..889
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228185"
FT   DOMAIN          389..558
FT                   /note="tr-type G"
FT   REGION          47..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..405
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          423..427
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          444..447
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          498..501
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          534..536
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        47..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         398..405
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         444..448
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         498..501
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   889 AA;  95680 MW;  B124390C4354573E CRC64;
     MADITVAELA KEIGTPVDRL VTQLADSGVN KSATDAISQD EKEALLGHLK KQHGDESEAK
     PNKLTLNRKT KSTLTMGHGS KAKSVNVEVR KKRTYVKRSE VEDEKLAEEA AKAEAEAAIL
     AEADAKAKAE AAAKEAENEK GVAAAKAEVE AERKAEAKIE AAAKAKIAAV EKAKNVEQAP
     EKVAETEEAK KLRLAQEKET LAKVEAEAAA AAEAAKKLAE ENEGRWKEQE AERKAKEKEV
     VHLTSSVYAQ EAEDKSDSAD ESGRRRKKKK APDRNARGRN SGRGKGKTLS SPQSLKHGFT
     KPVETKLQDI RIGETISVAE LANKMSKKGA EVVKAMFKLG AMATINQVID QETAALVAED
     MGFEVVLVKE NALEEAVLAD RNDTGEEITR APVVTIMGHV DHGKTSLLDH IREAKVADGE
     AGGITQHIGA YHVETGHGMI TFLDTPGHAA FTAMRSRGAK ATDIVVIVVA ADDGVMPQTI
     EAIQHAQASE APIIIAVNKM DKESADPDRV KSELSQHGVL SEEWGGEVQF CHVSAKTGLG
     IDELLDSILL QSEVLELTAV VDKMANGVVV ESKLDKGRGP VATVLVQEGT LKQGDIVLCG
     LEYGRVRAMR DENGKTIQSA GPSIPVEIIG LSGVPISGDE ATVVKDEKKA REVALFRQGK
     FRDVKLARQQ KAKLENMFAS MAEGDISEVN VVIKSDVQGS LEAISDSLLK LSTDEVKVKI
     IGSGVGAITE TDATLAAASN AIVVGFNVRA DASARKVIES ENIDLRYYSV IYALIEEVKQ
     AMSGMLAPEF KQEIIGLAQV RDVFKSPKIG AIAGCMVTEG VIKRSAPIRV LRENVVIYEG
     ELESLRRFKD DVQEVRNGTE CGIGVKNYND VRVGDQIEVF ETIEIKRSL
 
 
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