RS5_PYRAB
ID RS5_PYRAB Reviewed; 236 AA.
AC Q9V1V5; G8ZHV5;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=PYRAB03210;
GN ORFNames=PAB2136;
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: 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. Contacts protein S4.
CC {ECO:0000255|HAMAP-Rule:MF_01307}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ248284; CAB49243.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69698.1; -; Genomic_DNA.
DR PIR; D75145; D75145.
DR RefSeq; WP_010867443.1; NC_000868.1.
DR PDB; 6SW9; EM; 4.20 A; F=1-236.
DR PDB; 6SWC; EM; 3.30 A; F=1-236.
DR PDB; 6SWD; EM; 3.20 A; F=1-236.
DR PDBsum; 6SW9; -.
DR PDBsum; 6SWC; -.
DR PDBsum; 6SWD; -.
DR AlphaFoldDB; Q9V1V5; -.
DR SMR; Q9V1V5; -.
DR STRING; 272844.PAB2136; -.
DR EnsemblBacteria; CAB49243; CAB49243; PAB2136.
DR GeneID; 1495211; -.
DR KEGG; pab:PAB2136; -.
DR PATRIC; fig|272844.11.peg.342; -.
DR eggNOG; arCOG04087; Archaea.
DR HOGENOM; CLU_065898_0_1_2; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 60954at2157; -.
DR PhylomeDB; Q9V1V5; -.
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 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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..236
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131655"
FT DOMAIN 61..124
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 58..75
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 78..89
FT /evidence="ECO:0007829|PDB:6SWD"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:6SWD"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6SWC"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:6SWD"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6SWD"
SQ SEQUENCE 236 AA; 26484 MW; 346ABBE23734B4DD CRC64;
MSQEWKEYAK RVLDEWQPKT KLGMLVKEGQ ITDIHEIFRK GYQIKEPEII DVLLPEVNAR
ENQEILDIAL TVRMTDSGRR VRFRVLAAVG NRDGYVGLGI GHGREVGIAI RKAINYAKLN
IIEIKRGCGS WECRCRRPHS VPFTVEGKEG SVRVKLIPGP RGLGLVIGDV GKKILRLAGI
QDVWSQTLGE TRTTVNFAKA VFNALYNTNK VVVTPEMIER YGIVVGRAMP ASFTLE