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RS5_PYRFU
ID   RS5_PYRFU               Reviewed;         236 AA.
AC   Q8U017; Q9HH79;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
DE   AltName: Full=PfS5;
DE   AltName: Full=Small ribosomal subunit protein uS5;
GN   Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=PF1804;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=11119702; DOI=10.1016/s0014-5793(00)02293-6;
RA   Furumoto H., Taguchi A., Itoh T., Morinaga T., Itoh T.;
RT   "5S rRNA binding proteins from the hyperthermophilic archaeon, Pyrococcus
RT   furiosus.";
RL   FEBS Lett. 486:195-199(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [3] {ECO:0007744|PDB:4V6U}
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.60 ANGSTROMS) IN THE 70S RIBOSOME, AND
RP   SUBUNIT.
RX   PubMed=23222135; DOI=10.1093/nar/gks1259;
RA   Armache J.P., Anger A.M., Marquez V., Franckenberg S., Frohlich T.,
RA   Villa E., Berninghausen O., Thomm M., Arnold G.J., Beckmann R.,
RA   Wilson D.N.;
RT   "Promiscuous behaviour of archaeal ribosomal proteins: implications for
RT   eukaryotic ribosome evolution.";
RL   Nucleic Acids Res. 41:1284-1293(2013).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:23222135). Contacts
CC       protein S4 (By similarity). {ECO:0000255|HAMAP-Rule:MF_01307,
CC       ECO:0000269|PubMed:23222135}.
CC   -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC       subunit; the C-terminal domain interacts with the body and contacts
CC       protein S4. The interaction surface between S4 and S5 is involved in
CC       control of translational fidelity.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01307}.
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DR   EMBL; AB040118; BAB13704.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81928.1; -; Genomic_DNA.
DR   RefSeq; WP_011012945.1; NZ_CP023154.1.
DR   PDB; 4V6U; EM; 6.60 A; AF=1-236.
DR   PDB; 5JB3; EM; 5.34 A; F=1-236.
DR   PDB; 5JBH; EM; 5.34 A; F=1-236.
DR   PDBsum; 4V6U; -.
DR   PDBsum; 5JB3; -.
DR   PDBsum; 5JBH; -.
DR   AlphaFoldDB; Q8U017; -.
DR   SMR; Q8U017; -.
DR   STRING; 186497.PF1804; -.
DR   EnsemblBacteria; AAL81928; AAL81928; PF1804.
DR   GeneID; 41713623; -.
DR   KEGG; pfu:PF1804; -.
DR   PATRIC; fig|186497.12.peg.1875; -.
DR   eggNOG; arCOG04087; Archaea.
DR   HOGENOM; CLU_065898_0_1_2; -.
DR   OMA; KRGCGSW; -.
DR   OrthoDB; 60954at2157; -.
DR   PhylomeDB; Q8U017; -.
DR   Proteomes; UP000001013; 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   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_A; Ribosomal_S5_A; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..236
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000131657"
FT   DOMAIN          61..124
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT   CONFLICT        69..128
FT                   /note="Missing (in Ref. 1; BAB13704)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="Y -> S (in Ref. 1; BAB13704)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   236 AA;  26551 MW;  57BBC765DF6EC9CA CRC64;
     MSQEWKEYAK RVLDEWEPKT KLGMMVKEGQ ITDIHEIFRR GYQIKEPEII DVLLPEVNAR
     ENQEVLDIAL TVRMTDSGRR VRFRVLAAVG NRDGYVGLGI GHGKEVGIAI RKAINYAKLN
     IIEIKRGCGS WECRCRRPHS VPFAVEGKEG SVRVRLIPGP RGLGLVIGDV GKKILRLAGV
     QDVWSQTFGE TRTTVNFAKA VFNALYNTNR VAISPEMIER YGIVVGRAMP TTFTLE
 
 
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