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RS3_THET2
ID   RS3_THET2               Reviewed;         239 AA.
AC   P62663;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=30S ribosomal protein S3;
GN   Name=rpsC; Synonyms=rps3; OrderedLocusNames=TT_C1322;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11296217; DOI=10.1093/emboj/20.8.1829;
RA   Pioletti M., Schluenzen F., Harms J., Zarivach R., Gluehmann M., Avila H.,
RA   Bashan A., Bartels H., Auerbach T., Jacobi C., Hartsch T., Yonath A.,
RA   Franceschi F.;
RT   "Crystal structures of complexes of the small ribosomal subunit with
RT   tetracycline, edeine and IF3.";
RL   EMBO J. 20:1829-1839(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in
CC       the 70S ribosome, positioning it for translation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a tight complex with
CC       proteins S10 and S14 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS3 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ409330; CAC35062.1; -; Genomic_DNA.
DR   EMBL; AE017221; AAS81664.1; -; Genomic_DNA.
DR   RefSeq; WP_008633418.1; NC_005835.1.
DR   PDB; 4KVB; X-ray; 4.20 A; C=1-239.
DR   PDB; 4V4I; X-ray; 3.71 A; d=1-239.
DR   PDB; 4V4J; X-ray; 3.83 A; d=1-239.
DR   PDB; 4V63; X-ray; 3.21 A; AC/CC=1-239.
DR   PDB; 4V67; X-ray; 3.00 A; AC/CC=1-239.
DR   PDB; 4V7P; X-ray; 3.62 A; AC/DC=2-207.
DR   PDB; 4V83; X-ray; 3.50 A; AC/CC=2-207.
DR   PDB; 4V84; X-ray; 3.40 A; AC/CC=2-207.
DR   PDB; 4V9J; X-ray; 3.86 A; AC/CC=2-208.
DR   PDB; 4V9K; X-ray; 3.50 A; AC/CC=2-208.
DR   PDB; 4V9L; X-ray; 3.50 A; AC/CC=2-208.
DR   PDB; 4V9M; X-ray; 4.00 A; AC/CC=2-208.
DR   PDB; 4V9N; X-ray; 3.40 A; AC/CC=2-207.
DR   PDB; 4V9Q; X-ray; 3.40 A; BC/DC=2-207.
DR   PDB; 4W29; X-ray; 3.80 A; AC/CC=2-208.
DR   PDB; 4XEJ; X-ray; 3.80 A; AS03/BS03=2-207.
DR   PDB; 5J4D; X-ray; 3.10 A; LA/QC=1-239.
DR   PDBsum; 4KVB; -.
DR   PDBsum; 4V4I; -.
DR   PDBsum; 4V4J; -.
DR   PDBsum; 4V63; -.
DR   PDBsum; 4V67; -.
DR   PDBsum; 4V7P; -.
DR   PDBsum; 4V83; -.
DR   PDBsum; 4V84; -.
DR   PDBsum; 4V9J; -.
DR   PDBsum; 4V9K; -.
DR   PDBsum; 4V9L; -.
DR   PDBsum; 4V9M; -.
DR   PDBsum; 4V9N; -.
DR   PDBsum; 4V9Q; -.
DR   PDBsum; 4W29; -.
DR   PDBsum; 4XEJ; -.
DR   PDBsum; 5J4D; -.
DR   AlphaFoldDB; P62663; -.
DR   SMR; P62663; -.
DR   IntAct; P62663; 4.
DR   STRING; 262724.TT_C1322; -.
DR   DrugBank; DB08185; 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE.
DR   EnsemblBacteria; AAS81664; AAS81664; TT_C1322.
DR   GeneID; 3168725; -.
DR   KEGG; tth:TT_C1322; -.
DR   eggNOG; COG0092; Bacteria.
DR   HOGENOM; CLU_058591_0_2_0; -.
DR   OMA; KTNPIGN; -.
DR   OrthoDB; 1132353at2; -.
DR   EvolutionaryTrace; P62663; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1140.32; -; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_01309_B; Ribosomal_S3_B; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR005704; Ribosomal_S3_bac-typ.
DR   InterPro; IPR001351; Ribosomal_S3_C.
DR   InterPro; IPR036419; Ribosomal_S3_C_sf.
DR   InterPro; IPR018280; Ribosomal_S3_CS.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   SUPFAM; SSF54821; SSF54821; 1.
DR   TIGRFAMs; TIGR01009; rpsC_bact; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..239
FT                   /note="30S ribosomal protein S3"
FT                   /id="PRO_0000130222"
FT   DOMAIN          40..108
FT                   /note="KH type-2"
FT   REGION          212..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           7..10
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   TURN            11..15
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:4V63"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           29..45
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          52..55
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          57..65
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   TURN            78..81
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           83..92
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          95..98
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:4V9L"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           130..143
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          147..155
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:4V9L"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:4V67"
FT   STRAND          196..203
FT                   /evidence="ECO:0007829|PDB:4V67"
SQ   SEQUENCE   239 AA;  26701 MW;  AD585A1D53AC7F04 CRC64;
     MGNKIHPIGF RLGITRDWES RWYAGKKQYR HLLLEDQRIR GLLEKELYSA GLARVDIERA
     ADNVAVTVHV AKPGVVIGRG GERIRVLREE LAKLTGKNVA LNVQEVQNPN LSAPLVAQRV
     AEQIERRFAV RRAIKQAVQR VMESGAKGAK VIVSGRIGGA EQARTEWAAQ GRVPLHTLRA
     NIDYGFALAR TTYGVLGVKA YIFLGEVIGG QKPKARPELP KAEERPRRRR PAVRVKKEE
 
 
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