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IF2_UREU1
ID   IF2_UREU1               Reviewed;         614 AA.
AC   B5ZBC9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=UUR10_0326;
OS   Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=565575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33699 / Western;
RA   Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT   "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001184; ACI60166.1; -; Genomic_DNA.
DR   RefSeq; WP_012560304.1; NC_011374.1.
DR   AlphaFoldDB; B5ZBC9; -.
DR   SMR; B5ZBC9; -.
DR   STRING; 565575.UUR10_0326; -.
DR   EnsemblBacteria; ACI60166; ACI60166; UUR10_0326.
DR   GeneID; 45015873; -.
DR   KEGG; uue:UUR10_0326; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_14; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002018; 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; 1.
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.
FT   CHAIN           1..614
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093842"
FT   DOMAIN          115..283
FT                   /note="tr-type G"
FT   REGION          124..131
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          149..153
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          170..173
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          224..227
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          260..262
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..131
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         170..174
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         224..227
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   614 AA;  67760 MW;  FDE14FE88A7AB9D2 CRC64;
     MAKKNIKQKK DNRIAIDVKK HIKKVDVGVF GGTFVFTSPL SIAELAPKLN KSTNEIIMRY
     FKKGVVYNLN TILDEEQIGE LCLEYDLDFK IEKNVNTENL LENIAFDDLE ADLVARAPIV
     TIMGHVDHGK TTLLDTIRKS SVTASEAGGI TQHIGAYQIL KGDKPITFID TPGHEAFTEM
     RARGANLTDI VILVVAADDG IKMQTEEAID HAKAANVPII VFVNKMDKYE ANPDKVLNQL
     SAKEIVAEEL GGDIVFVKGS ALKNEGIFEL LDSILLIAEL NDYKANPNRL AYGTTIEANL
     DKGHGPLATL LVQNGTLRKG DYLVVGSTYG KIRNMFDEYD NEIEMALPSK PVKVSGFEEV
     PTAGDKFLAL ADEKQARAIA NDVKQKKIRL ERSMLQSSDI RAKIANGELK NINLIIKADV
     QGSLEALKGI FNSINIEGVT TTLVRSAIGT ISESDVRLAQ TSDAIIIGFN VRANRIIKDL
     ADSVGVQIMN YDIIYKFKED LEAWMKGTLD PIIVEEVIGE AKVLKLFKHS QVGTICGCRV
     INGKIKRNAL VRVLRDGIVI YNSKIATLQH NKDSVNEVIA DKECGLTIAN FNDVKENDII
     EVYVKVEKNH DEVK
 
 
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