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IF2_SOLUE
ID   IF2_SOLUE               Reviewed;        1001 AA.
AC   Q01W31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Acid_5181;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Bryobacterales; Solibacteraceae;
OC   Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP000473; ABJ86134.1; -; Genomic_DNA.
DR   RefSeq; WP_011686879.1; NC_008536.1.
DR   AlphaFoldDB; Q01W31; -.
DR   SMR; Q01W31; -.
DR   STRING; 234267.Acid_5181; -.
DR   PRIDE; Q01W31; -.
DR   EnsemblBacteria; ABJ86134; ABJ86134; Acid_5181.
DR   KEGG; sus:Acid_5181; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3266; Bacteria.
DR   HOGENOM; CLU_006301_5_1_0; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
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   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.
FT   CHAIN           1..1001
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008342"
FT   DOMAIN          499..668
FT                   /note="tr-type G"
FT   REGION          56..418
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          554..557
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          608..611
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          644..646
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        60..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..215
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..328
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..355
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..407
FT                   /note="Basic and acidic 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         554..558
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         608..611
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1001 AA;  107507 MW;  AEB82602AA7AD11B CRC64;
     MKKIRINELA RELEVKAHEI LERLPELGVT EKKTHSSSID EDVAIKLRQY YGQDVPDYVH
     DPNAVDEPAT EAHEERHEHE EAHEPAAAPK AAVEPETPVA PAPEAAPAAK EERPAPEEPA
     RPMAPIRPPL ASGRPIHPPV GATPPPRPEG PRAAPAPPLP PPAPQVPHAP SPAASSPAMP
     ARPEPPAHHP PSQTPPAAVF APGRPAPPSA KPLPTTTPRP GQVLSGPRQP FPSSPAPGAP
     QRPQAIPRPP QQVRPESQRP SGPGAPSAPQ RPLAGQPAAR PVVPPRPDLV AKLSAPRAPV
     MPQQPAAPRP GVPKAPSAPV PGQPIYRGPI RPGQPMVAKP GVRPGMPPSR PGGPRPQHPT
     SRGRIEPGMG APPPPAEPSR GRPGDRRPVR QQRERTEEEK ILRPQRRHVE AGPPPISREI
     TISEGITVKE LSEKLDVKAN LVMKKLMDRG IFVAINQTLD GKLATEVARD FGASTATVSY
     EVEAMQSVEE AQDTTDLERR APVVTIMGHV DHGKTSLLDA IREANVAGRE AGGITQHIGA
     YQVEMKGRKI VFIDTPGHEA FTRMRSRGAK VTDIVILVVA ADDGVMPQTL EAIDHAKAAA
     VPIIVAINKI DKADAQPERI KQQLSDRGLL PEDWGGDVVM VPVSARTQQG LPDLLEMILL
     VADMQDLKAN PSRPAMGTVI EAQLDRGRGP VATVLVRNGT LSVGDFFICG AVFGKVRAML
     NDRGTQIRKA EPSTPVEVLG LDSLPEAGDD FQVVTDTAKA KQIVNFRDQR QKEAALAKSS
     RITLEQLHQQ MREGEVKELP VIIKADVGGS AEVLKETLEK LSNDKVKVRV IHSGVGAINE
     SDILLASASN AIVIGFNVRP ERNAAATAEQ EKVDVRLHTI IYNLTDEIKR AMSGLLAPVF
     KEVYRGKAEV RETFRISKVG AVAGCQVIDG SIPRDSECRV LRDNIVVHTG KIGSLRRFKD
     DVSEVKIGME CGITLANFAD LKQGDIIEAF ATERVATEVF A
 
 
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