(data stored in SCRATCH3701 zone)

SWISSPROT: IF2_RICTY

ID   IF2_RICTY               Reviewed;         831 AA.
AC   Q68WI4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RT0539;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU04008.1; -; Genomic_DNA.
DR   RefSeq; WP_011190989.1; NC_006142.1.
DR   SMR; Q68WI4; -.
DR   STRING; 257363.RT0539; -.
DR   EnsemblBacteria; AAU04008; AAU04008; RT0539.
DR   KEGG; rty:RT0539; -.
DR   eggNOG; ENOG4107QHU; Bacteria.
DR   eggNOG; COG0532; LUCA.
DR   HOGENOM; HOG000076906; -.
DR   KO; K02519; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   BioCyc; RTYP257363:G1G0L-546-MONOMER; -.
DR   Proteomes; UP000000604; 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   Gene3D; 3.40.50.10050; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
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; 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; 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; Q68WI4.
DR   SWISS-2DPAGE; Q68WI4.
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..831
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228238"
FT   DOMAIN          329..499
FT                   /note="tr-type G"
FT   NP_BIND         338..345
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   NP_BIND         385..389
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   NP_BIND         439..442
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   REGION          338..345
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          363..367
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          385..388
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          439..442
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          475..477
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   831 AA;  91282 MW;  A74438DBD1749897 CRC64;
     MTDNQEIKPK KLTLGNSKLL LNKSFDSLTG VQSFVNAKSK TLVEVRKSSI GSTTTISLNK
     ERNSLDQTVI DSNKEEFNRR LSILKKAAEQ SKLYDSAQIS TLSKLASINQ SVNSKNEQFT
     TDKAVEQKQQ DIEDTKVEIG TKIVQDDEDI RSQIPNKKKE TFAKSLLVGM RTRYGIEAES
     ALEKIGDNKV VVPKIKLEEP KKFKKADLFN MLSDDENGSG RTRSLASIKR AREKEKRKLV
     SQIPEKVYRE VTIPEVIGVG DLANAMSERV ADVIKELMKL GILANASQTI DADTAELVAT
     NLGHTVTRVQ ESDVENVLIN DDKVEDLRTR APVVTVMGHV DHGKTSLLDA LKSTDIAAGE
     LGGITQHIGA YRVTLSDCKA ITFIDTPGHE AFSEMRSRGA KVTDIVIIVV AADDGIKTQT
     VEAINHAKAA GVPIIVAINK IDKPDIDIER IKNELYVHEI IGEEAGGDVI FIPISALKKI
     NLDKLEEAIL LISEMQDLKA SPFGLAAGVV IESKIEKGRG TLTTILVQRG TLRNGDIIIA
     GTSYGKVKKM INDKGREILE ATPSVPVEIQ GLNEVPFAGD QFNVVQNEKQ AKDIAEYRIR
     LAKEKKISVT SRSSLEELLL KASGNSKIKE LPLIIKCDVQ GSIEAIAGSL LKLPSDEIKL
     RILHSGVGPI TESDVSLAHV SSAIVVGFNV RAGTNALTAA EKTKVDIRYY SIIYNLIDDV
     KAIMSGMLDP IVREQYIGSV EIRQVFNITK IGKIAGSYVT KGIIKKGAGV RLLRDNVVIH
     AGKLKTLKRF KDEVKEVREG YECGIAFENY EDIREGDTVE VFELVQEQRQ L
//

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