(data stored in ACNUC7421 zone)

SWISSPROT: IF2_EDWI9

ID   IF2_EDWI9               Reviewed;         901 AA.
AC   C5BFB7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 56.
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=NT01EI_0467;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the essential components for the initiation of
CC       protein synthesis. Protects formylmethionyl-tRNA from spontaneous
CC       hydrolysis and promotes its binding to the 30S ribosomal subunits.
CC       Also involved in the hydrolysis of GTP during the formation of the
CC       70S ribosomal 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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00100}.
DR   EMBL; CP001600; ACR67703.1; -; Genomic_DNA.
DR   RefSeq; WP_015869905.1; NC_012779.2.
DR   ProteinModelPortal; C5BFB7; -.
DR   SMR; C5BFB7; -.
DR   STRING; 634503.NT01EI_0467; -.
DR   PRIDE; C5BFB7; -.
DR   EnsemblBacteria; ACR67703; ACR67703; NT01EI_0467.
DR   GeneID; 7961290; -.
DR   KEGG; eic:NT01EI_0467; -.
DR   PATRIC; fig|634503.3.peg.424; -.
DR   eggNOG; ENOG4107QHU; Bacteria.
DR   eggNOG; COG0532; LUCA.
DR   HOGENOM; HOG000076907; -.
DR   KO; K02519; -.
DR   OMA; DNRTGGY; -.
DR   OrthoDB; POG091H00EY; -.
DR   Proteomes; UP000001485; 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:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR013575; IF2_assoc_dom_bac.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR009000; Transl_B-barrel.
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;
DR   PRODOM; C5BFB7.
DR   SWISS-2DPAGE; C5BFB7.
KW   Complete proteome; Cytoplasm; GTP-binding; Initiation factor;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    901       Translation initiation factor IF-2.
FT                                /FTId=PRO_1000202771.
FT   DOMAIN      400    569       tr-type G.
FT   NP_BIND     409    416       GTP. {ECO:0000255|HAMAP-Rule:MF_00100}.
FT   NP_BIND     455    459       GTP. {ECO:0000255|HAMAP-Rule:MF_00100}.
FT   NP_BIND     509    512       GTP. {ECO:0000255|HAMAP-Rule:MF_00100}.
FT   REGION      409    416       G1. {ECO:0000250}.
FT   REGION      434    438       G2. {ECO:0000250}.
FT   REGION      455    458       G3. {ECO:0000250}.
FT   REGION      509    512       G4. {ECO:0000250}.
FT   REGION      545    547       G5. {ECO:0000250}.
SQ   SEQUENCE   901 AA;  98216 MW;  1AED0DB028854646 CRC64;
     MAEVTVKSLA AEIQTSVERL VQQLADAGIN KSPDDSVSPQ EREALLAHLN REHGGSSDKL
     TLQRKTRSTL SVPGTGGKSK SVQIEVRKKR TYVKSDAAAQ QAEAEALAKR EAEEQVKREA
     EEQTQRDMAE LAKREAAEQA KRQQEEQAKR EAAEKAKREA AEKEKVTNQH IDEKTKAAQA
     EKAKREAEAA ELKRKAEEEA RRKLEEDARK VAEEARRMAE ANEGKWTENA SEEDNSDYHV
     TTSHHAREAE DENDRQVEGD RRARGRGGKA AKQKKGSKLS ESKADREEAR AVNRGGKGGK
     RKPSSLQQGF TKPAQAVNRD VVIGETITVA ELANKMAVKG SQVIKAMMKM GAMATINQVI
     DQETAQLVAE DMGHKVILRR ENELEEAVLS DRDTGAAAEP RAPVVTIMGH VDHGKTSLLD
     YIRSTKVAAG EAGGITQHIG AYHVQTDNGM ITFLDTPGHA AFTAMRARGA QATDIVVLVV
     AADDGVMPQT IEAVQHAKAA GVPLVVAVNK IDKPEADPDR VKNELSQYGV MPEEWGGEAQ
     FVHVSAKAGT GIDELLDAIL LQAEVLELKA VRNGMASGVV IESFLDKGRG PVATVLVREG
     TLNKGDIVLC GFEYGRVRAM RDELGREITE AGPSIPVEIL GMSGVPAAGD EATVVRDEKK
     AREVALYRQG KFREVKLARQ QKAKLENMFS NMVEGEVSEL NIVLKADVQG SVEAIADSLR
     KLSTDEVKVK IVGSGVGGIT ETDATLAAAS NAILLGFNVR ADASARRVVE AENLDLRYYS
     VIYDLIDEVK QAMSGMLAPE YKQEIIGLAE VRDVFKSPKF GAIAGCMVTE GVVKRHSPIR
     VLRENVVIYE GELESLRRFK DDVNEVRNGM ECGIGVKNYN DVRPGDVIEV FETIEVKRTI
     D
//

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