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RS4_CENSY
ID   RS4_CENSY               Reviewed;         205 AA.
AC   A0RY02;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=CENSYa_1599;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01306}.
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC       interaction surface between S4 and S5 is involved in control of
CC       translational fidelity. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01306}.
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DR   EMBL; DP000238; ABK78219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RY02; -.
DR   SMR; A0RY02; -.
DR   STRING; 414004.CENSYa_1599; -.
DR   EnsemblBacteria; ABK78219; ABK78219; CENSYa_1599.
DR   KEGG; csy:CENSYa_1599; -.
DR   PATRIC; fig|414004.10.peg.1462; -.
DR   HOGENOM; CLU_089738_1_1_2; -.
DR   OMA; ARQFITH; -.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   HAMAP; MF_01306_A; Ribosomal_S4_A; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR022802; Ribosomal_S4_arc.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR11831; PTHR11831; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01018; uS4_arch; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..205
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000293401"
FT   DOMAIN          103..173
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT   REGION          174..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  22648 MW;  EB810641636829FF CRC64;
     MGDPKLPRRM WRKPKRPFNY DLKMEELRTL GTFGLRTKRE LWKAHTELSR VRNQARSLLA
     LGQEVRERKE PVLLRSLARI GLVGKDASLD DVLNLQVNDL LGRRLQTIVM KKLGFSTPYQ
     ARQAVVHGHI TISDRVVTIP SYTVYVEEEG DIKLTGGSAF ATILEKSKRA EAAAREAAAE
     AAEAEQAAAQ AAAPTPAPAA AAPKQ
 
 
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