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IF2_CORGL
ID   IF2_CORGL               Reviewed;        1004 AA.
AC   Q8NP40;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=Cgl1985, cg2176;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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; BA000036; BAB99378.1; -; Genomic_DNA.
DR   EMBL; BX927153; CAF20326.1; -; Genomic_DNA.
DR   RefSeq; NP_601191.1; NC_003450.3.
DR   RefSeq; WP_011014802.1; NC_003450.3.
DR   AlphaFoldDB; Q8NP40; -.
DR   SMR; Q8NP40; -.
DR   STRING; 196627.cg2176; -.
DR   KEGG; cgb:cg2176; -.
DR   KEGG; cgl:Cgl1985; -.
DR   PATRIC; fig|196627.13.peg.1924; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_9_0_11; -.
DR   OMA; QVRPEMI; -.
DR   Proteomes; UP000000582; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1004
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137197"
FT   DOMAIN          499..671
FT                   /note="tr-type G"
FT   REGION          36..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..515
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          533..537
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          558..561
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          612..615
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          648..650
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        76..96
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..196
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..234
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         508..515
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         558..562
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         612..615
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   CONFLICT        81
FT                   /note="P -> R (in Ref. 2; CAF20326)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1004 AA;  103413 MW;  FC159DE2AE29283F CRC64;
     MPGKLRVHEL AKQLGITSKE LLATLKDKGE FVKTASSTIE PPVVKRMQEH YGSSGSDKSD
     TAAKPAAAKP AAPKPAASAA PKPGAPAKPA APAAKPAPAA PSAASAAKPG AAPKPGVQAK
     PAAAAKPGAP AKPAAPAAPS AAKSGSAPKP AAAAKPAFSG PTPGDAAKKA EPAAKPGAEA
     PRPGGMPRPM GKPAPKPGAR APRVANNPFS TGGGERPAPR PGGGPRPGGG PRPGGGPRPQ
     GQGRPGGQRD GQRDGQRDGQ GNRGGQRQGA GAGGPRPQGG PRPQGGSRPQ GGSAQGAQGA
     PSQERQGGGR RPSPAMMPPT PGQMPAKAPG KGGRGGQAGG GAGGGFNRGG GTGGGAGRGG
     RRGGTAGAFG RPGGAPRRGR KSKRQKRNEY ESMQAPNVIG GVRLPDGKGA TIRLARGASL
     ADFADKIGAD AAALVQALFN LGEMVTATAS VSDETLQLLG EEMNYKVQVV SPEDEDRELL
     ESFDLQFGED EGGEADLAKR PPVVTVMGHV DHGKTRLLDT IRKANVGSDE AGGITQGIGA
     YQVKVNVEDT ERTITFLDTP GHEAFTAMRA RGAKSTDIAV LVVAADDGVM PQTVEAINHA
     KAADVPIVVA VNKIDKPEAS PEKIRGQLTE YGLIPEEYGG DTIFVDISAK QGLNIDELLA
     SVCLTADAEL DLVANPEMDA QGVAIEAHLD RGRGPVATVI VQRGTLRVGD SIVAGDTYGR
     VRRMVDEYGR DVEEAGPSRP VQVQGLNGVP GAGDNLLVVE DDRIARQIAN QRNARKRNAL
     AARSRKRVSL EDLDSVLKEH STLNLILKGD NAGSVEALEE ALLKIEMDDE VQLNIIDRGV
     GAVTQTNVTL AAASDAVIIA FNVRAEGKAT EEANAEGVDV RYYTIIYRAI EEVEAALKGM
     LKPIYEERVI GHAEIRAIFK ASSVGLIAGC MVEDGKVRRN ATVRIIRDGN VIAENAKIVS
     LRREKDDATE VSAGYECGMV LSYPDISVDD KIEVYEMVEV PREA
 
 
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