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RS4_PYRAB
ID   RS4_PYRAB               Reviewed;         180 AA.
AC   P61992; G8ZGN8; Q9V199;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN   Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=PYRAB05280;
GN   ORFNames=PAB0361;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49450.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69917.1; -; Genomic_DNA.
DR   PIR; C75171; C75171.
DR   RefSeq; WP_010867652.1; NC_000868.1.
DR   PDB; 5JB3; EM; 5.34 A; D=1-180.
DR   PDB; 5JBH; EM; 5.34 A; D=1-180.
DR   PDB; 6SW9; EM; 4.20 A; D=1-180.
DR   PDB; 6SWC; EM; 3.30 A; D=1-180.
DR   PDB; 6SWD; EM; 3.20 A; D=1-180.
DR   PDBsum; 5JB3; -.
DR   PDBsum; 5JBH; -.
DR   PDBsum; 6SW9; -.
DR   PDBsum; 6SWC; -.
DR   PDBsum; 6SWD; -.
DR   AlphaFoldDB; P61992; -.
DR   SMR; P61992; -.
DR   STRING; 272844.PAB0361; -.
DR   EnsemblBacteria; CAB49450; CAB49450; PAB0361.
DR   GeneID; 41713476; -.
DR   KEGG; pab:PAB0361; -.
DR   PATRIC; fig|272844.11.peg.563; -.
DR   eggNOG; arCOG04239; Archaea.
DR   HOGENOM; CLU_089738_1_1_2; -.
DR   OMA; ARQFITH; -.
DR   OrthoDB; 93256at2157; -.
DR   PhylomeDB; P61992; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; IPR018079; Ribosomal_S4_CS.
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; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..180
FT                   /note="30S ribosomal protein S4"
FT                   /id="PRO_0000132515"
FT   DOMAIN          103..174
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   HELIX           20..33
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   HELIX           39..55
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   HELIX           64..79
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:6SWC"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   HELIX           118..126
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:6SWD"
FT   TURN            166..174
FT                   /evidence="ECO:0007829|PDB:6SWD"
SQ   SEQUENCE   180 AA;  21338 MW;  D59E61EF49F6CE57 CRC64;
     MGDPKRQRKK YETPPHPWIK ERLDRERVLM DKYELKNKKE LWKHETQLKN FRRRARRLLA
     ARGKQAEIER EQLLARLKRL GLLPEDAVLD DVLSLTIEDI LERRLQTIVY KKGLARTMRQ
     ARQLIVHGHI EVNGQIIRSP SYLVLKEEED TITYARTSPF ANPQHPERMM IEKAKQGGEA
 
 
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