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Protein

30S ribosomal protein S4

Gene

rpsD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the body and platform of the 30S subunit. Binds mRNA in the 70S ribosome, positioning it for translation.1 Publication

Cofactori

Zn2+1 Publication, [4Fe-4S] cluster2 PublicationsNote: Binds 1 zinc ion per subunit (PubMed:11866529). In a number of structures (e.g. 4Y4O, 5FDV) a 4Fe-4S cluster is seen in place of the zinc cofactor (PubMed:25775268, PubMed:26792896).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9Zinc1 Publication1
Metal bindingi12Zinc1 Publication1
Metal bindingi26Zinc1 Publication1
Metal bindingi31Zinc1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, RNA-binding, rRNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S4
Gene namesi
Name:rpsD
Synonyms:rps4
Ordered Locus Names:TTHA1665
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001324832 – 20930S ribosomal protein S4Add BLAST208

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:11014182, PubMed:11007480, PubMed:11163189, PubMed:11014183, PubMed:11511350, PubMed:11296217, PubMed:11228145, PubMed:11228145, PubMed:11283358, PubMed:11340196, PubMed:11866529, PubMed:25775268, PubMed:26792896). Contacts protein S5 (PubMed:11340196). The interaction surface between S4 and S5 is involved in control of translational fidelity.12 Publications

Protein-protein interaction databases

STRINGi300852.TTHA1665.

Structurei

Secondary structure

1209
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 15Combined sources7
Beta strandi21 – 23Combined sources3
Beta strandi26 – 28Combined sources3
Helixi29 – 31Combined sources3
Helixi33 – 35Combined sources3
Turni42 – 45Combined sources4
Helixi53 – 68Combined sources16
Helixi72 – 84Combined sources13
Beta strandi85 – 87Combined sources3
Helixi89 – 98Combined sources10
Helixi101 – 107Combined sources7
Beta strandi110 – 113Combined sources4
Helixi114 – 122Combined sources9
Turni123 – 125Combined sources3
Beta strandi126 – 128Combined sources3
Beta strandi131 – 133Combined sources3
Beta strandi145 – 148Combined sources4
Helixi150 – 152Combined sources3
Helixi156 – 164Combined sources9
Turni165 – 167Combined sources3
Beta strandi174 – 177Combined sources4
Turni178 – 181Combined sources4
Beta strandi182 – 184Combined sources3
Helixi191 – 193Combined sources3
Helixi200 – 206Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00D1-209[»]
1FKAX-ray3.30D1-209[»]
1HNWX-ray3.40D1-209[»]
1HNXX-ray3.40D1-209[»]
1HNZX-ray3.30D1-209[»]
1HR0X-ray3.20D1-209[»]
1I94X-ray3.20D2-209[»]
1I95X-ray4.50D2-209[»]
1I96X-ray4.20D2-209[»]
1I97X-ray4.50D2-209[»]
1IBKX-ray3.31D1-209[»]
1IBLX-ray3.11D1-209[»]
1IBMX-ray3.31D1-209[»]
1J5EX-ray3.05D2-209[»]
1JGOX-ray5.60G1-209[»]
1JGPX-ray7.00G1-209[»]
1JGQX-ray5.00G1-209[»]
1L1Umodel-D1-209[»]
1ML5electron microscopy14.00G1-209[»]
1N32X-ray3.00D2-209[»]
1N33X-ray3.35D2-209[»]
1N34X-ray3.80D2-209[»]
1N36X-ray3.65D2-209[»]
1QD7X-ray5.50C60-155[»]
1TWTmodel-G2-209[»]
1VVJX-ray3.44QD/XD1-209[»]
1VY4X-ray2.60AD/CD1-209[»]
1VY5X-ray2.55AD/CD1-209[»]
1VY6X-ray2.90AD/CD1-209[»]
1VY7X-ray2.80AD/CD1-209[»]
1XMOX-ray3.25D1-209[»]
1XMQX-ray3.00D1-209[»]
1XNQX-ray3.05D1-209[»]
1XNRX-ray3.10D1-209[»]
2E5LX-ray3.30D2-209[»]
2F4VX-ray3.80D1-209[»]
2HHHX-ray3.35D1-209[»]
2UU9X-ray3.10D2-209[»]
2UUAX-ray2.90D2-209[»]
2UUBX-ray2.80D2-209[»]
2UUCX-ray3.10D2-209[»]
2UXBX-ray3.10D2-209[»]
2UXCX-ray2.90D2-209[»]
2UXDX-ray3.20D2-209[»]
2VQEX-ray2.50D1-209[»]
2VQFX-ray2.90D1-209[»]
2ZM6X-ray3.30D2-209[»]
3OTOX-ray3.69D1-209[»]
3T1HX-ray3.11D1-209[»]
3T1YX-ray2.80D1-209[»]
4AQYX-ray3.50D2-209[»]
4B3MX-ray2.90D2-209[»]
4B3RX-ray3.00D2-209[»]
4B3SX-ray3.15D2-209[»]
4B3TX-ray3.00D2-209[»]
4DR1X-ray3.60D1-209[»]
4DR2X-ray3.25D1-209[»]
4DR3X-ray3.35D1-209[»]
4DR4X-ray3.97D1-209[»]
4DR5X-ray3.45D1-209[»]
4DR6X-ray3.30D1-209[»]
4DR7X-ray3.75D1-209[»]
4DUYX-ray3.39D1-209[»]
4DUZX-ray3.65D1-209[»]
4DV0X-ray3.85D1-209[»]
4DV1X-ray3.85D1-209[»]
4DV2X-ray3.65D1-209[»]
4DV3X-ray3.55D1-209[»]
4DV4X-ray3.65D1-209[»]
4DV5X-ray3.68D1-209[»]
4DV6X-ray3.30D1-209[»]
4DV7X-ray3.29D1-209[»]
4GKJX-ray3.30D2-209[»]
4GKKX-ray3.20D2-209[»]
4JI0X-ray3.49D1-209[»]
4JI1X-ray3.14D1-209[»]
4JI2X-ray3.64D1-209[»]
4JI3X-ray3.35D1-209[»]
4JI4X-ray3.69D1-209[»]
4JI5X-ray3.85D1-209[»]
4JI6X-ray3.55D1-209[»]
4JI7X-ray3.50D1-209[»]
4JI8X-ray3.74D1-209[»]
4JV5X-ray3.16D2-209[»]
4JYAX-ray3.10D2-209[»]
4K0KX-ray3.40D2-209[»]
4KHPX-ray3.10D2-209[»]
4L47X-ray3.22QD/XD1-209[»]
4L71X-ray3.90QD/XD1-209[»]
4LELX-ray3.90QD/XD1-209[»]
4LF4X-ray3.34D1-209[»]
4LF5X-ray3.75D1-209[»]
4LF6X-ray3.31D1-209[»]
4LF7X-ray3.15D1-209[»]
4LF8X-ray3.15D1-209[»]
4LF9X-ray3.28D1-209[»]
4LFAX-ray3.65D1-209[»]
4LFBX-ray3.01D1-209[»]
4LFCX-ray3.60D1-209[»]
4LFZX-ray3.92QD/XD1-209[»]
4LNTX-ray2.94QD/XD1-209[»]
4LSKX-ray3.48QD/XD1-209[»]
4LT8X-ray3.14QD/XD1-209[»]
4NXMX-ray3.65D1-209[»]
4NXNX-ray3.54D1-209[»]
4OX9X-ray3.80D2-209[»]
4P6FX-ray3.60QD/XD1-209[»]
4P70X-ray3.68QD/XD1-209[»]
4TUAX-ray3.60QD/XD1-209[»]
4TUBX-ray3.60QD/XD1-209[»]
4TUCX-ray3.60QD/XD1-209[»]
4TUDX-ray3.60QD/XD1-209[»]
4TUEX-ray3.50QD/XD1-209[»]
4V42X-ray5.50AG1-209[»]
4V49X-ray8.70D2-209[»]
4V4AX-ray9.50D2-209[»]
4V4IX-ray3.71e1-209[»]
4V4PX-ray5.50BG1-209[»]
4V4RX-ray5.90AD1-209[»]
4V4SX-ray6.76AD1-209[»]
4V4TX-ray6.46AD1-209[»]
4V4XX-ray5.00AG1-209[»]
4V4YX-ray5.50AG1-209[»]
4V4ZX-ray4.51AG1-209[»]
4V51X-ray2.80AD/CD2-209[»]
4V5AX-ray3.50AD/CD2-209[»]
4V5CX-ray3.30AD/CD1-209[»]
4V5DX-ray3.50AD/CD1-209[»]
4V5EX-ray3.45AD/CD1-209[»]
4V5FX-ray3.60AD/CD1-209[»]
4V5GX-ray3.60AD/CD1-209[»]
4V5JX-ray3.10AD/CD1-209[»]
4V5KX-ray3.20AD/CD1-209[»]
4V5LX-ray3.10AD1-209[»]
4V5Melectron microscopy7.80AD1-209[»]
4V5Nelectron microscopy7.60AD1-209[»]
4V5PX-ray3.10AD/CD1-209[»]
4V5QX-ray3.10AD/CD1-209[»]
4V5RX-ray3.10AD/CD1-209[»]
4V5SX-ray3.10AD/CD1-209[»]
4V5Zelectron microscopy8.70d1-209[»]
4V68electron microscopy6.40AD2-209[»]
4V6AX-ray3.10AD/CD1-209[»]
4V6FX-ray3.10BG/CG1-209[»]
4V6GX-ray3.50AG/CG1-209[»]
4V7JX-ray3.30Ad/Bd1-209[»]
4V7KX-ray3.60Ad/Bd1-209[»]
4V7LX-ray3.00AD/CD1-209[»]
4V7MX-ray3.45AD/CD1-209[»]
4V7WX-ray3.00AD/CD1-209[»]
4V7XX-ray3.00AD/CD1-209[»]
4V7YX-ray3.00AD/CD1-209[»]
4V7ZX-ray3.10AD/CD1-209[»]
4V87X-ray3.10BG/CG2-209[»]
4V8AX-ray3.20CD/DD1-209[»]
4V8BX-ray3.00AG/CG2-209[»]
4V8CX-ray3.30CG/DG2-209[»]
4V8DX-ray3.00AG/CG2-209[»]
4V8EX-ray3.30BG/DG2-209[»]
4V8FX-ray3.30BG/CG2-209[»]
4V8GX-ray3.00AD/CD1-209[»]
4V8HX-ray3.10AD/CD1-209[»]
4V8IX-ray2.70AD/CD1-209[»]
4V8JX-ray3.90AD/CD1-209[»]
4V8NX-ray3.10AD/CD1-209[»]
4V8OX-ray3.80AD1-209[»]
4V8QX-ray3.10BD1-209[»]
4V8UX-ray3.70AD/CD1-209[»]
4V8XX-ray3.35AD/CD1-209[»]
4V90X-ray2.95AD1-209[»]
4V95X-ray3.20AD/CD1-209[»]
4V97X-ray3.52AD/CD1-209[»]
4V9AX-ray3.30AG/CG2-209[»]
4V9BX-ray3.10AG/CG2-209[»]
4V9HX-ray2.86AD2-209[»]
4V9IX-ray3.30AD/CD2-209[»]
4V9RX-ray3.00AD/CD1-209[»]
4V9SX-ray3.10AD/CD1-209[»]
4W2EX-ray2.90d1-209[»]
4W2FX-ray2.40AD/CD1-209[»]
4W2GX-ray2.55AD/CD1-209[»]
4W2HX-ray2.70AD/CD1-209[»]
4W2IX-ray2.70AD/CD1-209[»]
4W4GX-ray3.30QD/XD1-209[»]
4WPOX-ray2.80BD/DD1-209[»]
4WQ1X-ray3.1032/3E2-209[»]
4WQFX-ray2.80BD/DD1-209[»]
4WQRX-ray3.1532/3E1-209[»]
4WQUX-ray2.80BD/DD1-209[»]
4WQYX-ray2.80BD/DD1-209[»]
4WR6X-ray3.0532/3E1-209[»]
4WRAX-ray3.0532/3E1-209[»]
4WROX-ray3.0532/3E1-209[»]
4WSDX-ray2.9532/3E1-209[»]
4WSMX-ray3.3032/3E1-209[»]
4WT1X-ray3.0532/3E1-209[»]
4WT8X-ray3.40AD/BD2-209[»]
4WU1X-ray3.2032/3E1-209[»]
4WZDX-ray3.1032/3E1-209[»]
4WZOX-ray3.3032/3E1-209[»]
4X62X-ray3.45D2-209[»]
4X64X-ray3.35D2-209[»]
4X65X-ray3.35D2-209[»]
4X66X-ray3.45D2-209[»]
4Y4OX-ray2.301d/2d1-209[»]
4Y4PX-ray2.501d/2d1-209[»]
4YHHX-ray3.42D2-209[»]
4YPBX-ray3.40QD/XD1-209[»]
4YY3X-ray3.60D1-209[»]
4YZVX-ray3.10QD/XD1-209[»]
4Z3SX-ray2.651d/2d1-209[»]
4Z8CX-ray2.901d/2d1-209[»]
4ZERX-ray3.101d/2d2-209[»]
4ZSNX-ray3.60QD/XD1-209[»]
5A9Zelectron microscopy4.70BH2-209[»]
5AA0electron microscopy5.00BH2-209[»]
5BR8X-ray3.40D1-209[»]
5CZPX-ray3.30QD/XD1-209[»]
5D8BX-ray3.63AC/EA1-209[»]
5DFEX-ray3.10QD/XD1-209[»]
5DOXX-ray3.101d/2d1-209[»]
5DOYX-ray2.601d/2d1-209[»]
5E7KX-ray3.2032/3E1-209[»]
5E81X-ray2.9532/3E1-209[»]
5EL4X-ray3.1532/3E1-209[»]
5EL5X-ray3.1532/3E1-209[»]
5EL6X-ray3.1032/3E1-209[»]
5EL7X-ray3.1532/3E1-209[»]
5F8KX-ray2.801d/2d2-209[»]
5FDUX-ray2.901d/2d2-209[»]
5FDVX-ray2.801d/2d2-209[»]
5HAUX-ray3.001d/2d1-209[»]
5HCPX-ray2.891d/2d1-209[»]
5HCQX-ray2.801d/2d1-209[»]
5HCRX-ray2.801d/2d1-209[»]
5HD1X-ray2.701d/2d1-209[»]
5IB7X-ray2.9932/3E1-209[»]
5IB8X-ray3.1332/3E1-209[»]
5IBBX-ray2.9632/3E1-209[»]
5IMQelectron microscopy3.80H1-209[»]
5IMRelectron microscopy-H1-209[»]
5IWAX-ray3.50D2-209[»]
5J30X-ray3.20QD/XD1-209[»]
5J3CX-ray3.04QD/XD1-209[»]
5J4BX-ray2.601d/2d1-209[»]
5J4CX-ray2.801d/2d1-209[»]
5J8BX-ray2.60d1-209[»]
5LMNelectron microscopy3.55D1-209[»]
5LMOelectron microscopy4.30D1-209[»]
5LMPelectron microscopy5.35D1-209[»]
5LMQelectron microscopy4.20D1-209[»]
5LMRelectron microscopy4.45D1-209[»]
5LMSelectron microscopy5.10D1-209[»]
5LMTelectron microscopy4.15D1-209[»]
5LMUelectron microscopy4.00D1-209[»]
5LMVelectron microscopy4.90D1-209[»]
ProteinModelPortaliP80373.
SMRiP80373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80373.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini99 – 161S4 RNA-bindingAdd BLAST63

Sequence similaritiesi

Belongs to the ribosomal protein S4P family.Curated
Contains 1 S4 RNA-binding domain.Curated

Phylogenomic databases

eggNOGiENOG4105G6W. Bacteria.
COG0522. LUCA.
HOGENOMiHOG000221004.
KOiK02986.
OMAiRTSDYGN.
PhylomeDBiP80373.

Family and domain databases

Gene3Di1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPiMF_01306_B. Ribosomal_S4_B. 1 hit.
InterProiIPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM01390. Ribosomal_S4. 1 hit.
SM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01017. rpsD_bact. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRYIGPVCR LCRREGVKLY LKGERCYSPK CAMERRPYPP GQHGQKRARR
60 70 80 90 100
PSDYAVRLRE KQKLRRIYGI SERQFRNLFE EASKKKGVTG SVFLGLLESR
110 120 130 140 150
LDNVVYRLGF AVSRRQARQL VRHGHITVNG RRVDLPSYRV RPGDEIAVAE
160 170 180 190 200
KSRNLELIRQ NLEAMKGRKV GPWLSLDVEG MKGKFLRLPD REDLALPVNE

QLVIEFYSR
Length:209
Mass (Da):24,324
Last modified:January 23, 2007 - v3
Checksum:i0FF3911816971236
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12C → S AA sequence (PubMed:7957245).Curated1
Sequence conflicti26C → D AA sequence (PubMed:7957245).Curated1

Mass spectrometryi

Molecular mass is 24192 Da from positions 2 - 209. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024328 Genomic DNA. Translation: BAA75548.1.
AP008226 Genomic DNA. Translation: BAD71488.1.
RefSeqiWP_011173699.1. NC_006461.1.
YP_144931.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71488; BAD71488; BAD71488.
GeneIDi3168006.
KEGGittj:TTHA1665.
PATRICi23958285. VBITheThe93045_1635.

Cross-referencesi

Web resourcesi

T.thermophilus ribosome structure and function

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024328 Genomic DNA. Translation: BAA75548.1.
AP008226 Genomic DNA. Translation: BAD71488.1.
RefSeqiWP_011173699.1. NC_006461.1.
YP_144931.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00D1-209[»]
1FKAX-ray3.30D1-209[»]
1HNWX-ray3.40D1-209[»]
1HNXX-ray3.40D1-209[»]
1HNZX-ray3.30D1-209[»]
1HR0X-ray3.20D1-209[»]
1I94X-ray3.20D2-209[»]
1I95X-ray4.50D2-209[»]
1I96X-ray4.20D2-209[»]
1I97X-ray4.50D2-209[»]
1IBKX-ray3.31D1-209[»]
1IBLX-ray3.11D1-209[»]
1IBMX-ray3.31D1-209[»]
1J5EX-ray3.05D2-209[»]
1JGOX-ray5.60G1-209[»]
1JGPX-ray7.00G1-209[»]
1JGQX-ray5.00G1-209[»]
1L1Umodel-D1-209[»]
1ML5electron microscopy14.00G1-209[»]
1N32X-ray3.00D2-209[»]
1N33X-ray3.35D2-209[»]
1N34X-ray3.80D2-209[»]
1N36X-ray3.65D2-209[»]
1QD7X-ray5.50C60-155[»]
1TWTmodel-G2-209[»]
1VVJX-ray3.44QD/XD1-209[»]
1VY4X-ray2.60AD/CD1-209[»]
1VY5X-ray2.55AD/CD1-209[»]
1VY6X-ray2.90AD/CD1-209[»]
1VY7X-ray2.80AD/CD1-209[»]
1XMOX-ray3.25D1-209[»]
1XMQX-ray3.00D1-209[»]
1XNQX-ray3.05D1-209[»]
1XNRX-ray3.10D1-209[»]
2E5LX-ray3.30D2-209[»]
2F4VX-ray3.80D1-209[»]
2HHHX-ray3.35D1-209[»]
2UU9X-ray3.10D2-209[»]
2UUAX-ray2.90D2-209[»]
2UUBX-ray2.80D2-209[»]
2UUCX-ray3.10D2-209[»]
2UXBX-ray3.10D2-209[»]
2UXCX-ray2.90D2-209[»]
2UXDX-ray3.20D2-209[»]
2VQEX-ray2.50D1-209[»]
2VQFX-ray2.90D1-209[»]
2ZM6X-ray3.30D2-209[»]
3OTOX-ray3.69D1-209[»]
3T1HX-ray3.11D1-209[»]
3T1YX-ray2.80D1-209[»]
4AQYX-ray3.50D2-209[»]
4B3MX-ray2.90D2-209[»]
4B3RX-ray3.00D2-209[»]
4B3SX-ray3.15D2-209[»]
4B3TX-ray3.00D2-209[»]
4DR1X-ray3.60D1-209[»]
4DR2X-ray3.25D1-209[»]
4DR3X-ray3.35D1-209[»]
4DR4X-ray3.97D1-209[»]
4DR5X-ray3.45D1-209[»]
4DR6X-ray3.30D1-209[»]
4DR7X-ray3.75D1-209[»]
4DUYX-ray3.39D1-209[»]
4DUZX-ray3.65D1-209[»]
4DV0X-ray3.85D1-209[»]
4DV1X-ray3.85D1-209[»]
4DV2X-ray3.65D1-209[»]
4DV3X-ray3.55D1-209[»]
4DV4X-ray3.65D1-209[»]
4DV5X-ray3.68D1-209[»]
4DV6X-ray3.30D1-209[»]
4DV7X-ray3.29D1-209[»]
4GKJX-ray3.30D2-209[»]
4GKKX-ray3.20D2-209[»]
4JI0X-ray3.49D1-209[»]
4JI1X-ray3.14D1-209[»]
4JI2X-ray3.64D1-209[»]
4JI3X-ray3.35D1-209[»]
4JI4X-ray3.69D1-209[»]
4JI5X-ray3.85D1-209[»]
4JI6X-ray3.55D1-209[»]
4JI7X-ray3.50D1-209[»]
4JI8X-ray3.74D1-209[»]
4JV5X-ray3.16D2-209[»]
4JYAX-ray3.10D2-209[»]
4K0KX-ray3.40D2-209[»]
4KHPX-ray3.10D2-209[»]
4L47X-ray3.22QD/XD1-209[»]
4L71X-ray3.90QD/XD1-209[»]
4LELX-ray3.90QD/XD1-209[»]
4LF4X-ray3.34D1-209[»]
4LF5X-ray3.75D1-209[»]
4LF6X-ray3.31D1-209[»]
4LF7X-ray3.15D1-209[»]
4LF8X-ray3.15D1-209[»]
4LF9X-ray3.28D1-209[»]
4LFAX-ray3.65D1-209[»]
4LFBX-ray3.01D1-209[»]
4LFCX-ray3.60D1-209[»]
4LFZX-ray3.92QD/XD1-209[»]
4LNTX-ray2.94QD/XD1-209[»]
4LSKX-ray3.48QD/XD1-209[»]
4LT8X-ray3.14QD/XD1-209[»]
4NXMX-ray3.65D1-209[»]
4NXNX-ray3.54D1-209[»]
4OX9X-ray3.80D2-209[»]
4P6FX-ray3.60QD/XD1-209[»]
4P70X-ray3.68QD/XD1-209[»]
4TUAX-ray3.60QD/XD1-209[»]
4TUBX-ray3.60QD/XD1-209[»]
4TUCX-ray3.60QD/XD1-209[»]
4TUDX-ray3.60QD/XD1-209[»]
4TUEX-ray3.50QD/XD1-209[»]
4V42X-ray5.50AG1-209[»]
4V49X-ray8.70D2-209[»]
4V4AX-ray9.50D2-209[»]
4V4IX-ray3.71e1-209[»]
4V4PX-ray5.50BG1-209[»]
4V4RX-ray5.90AD1-209[»]
4V4SX-ray6.76AD1-209[»]
4V4TX-ray6.46AD1-209[»]
4V4XX-ray5.00AG1-209[»]
4V4YX-ray5.50AG1-209[»]
4V4ZX-ray4.51AG1-209[»]
4V51X-ray2.80AD/CD2-209[»]
4V5AX-ray3.50AD/CD2-209[»]
4V5CX-ray3.30AD/CD1-209[»]
4V5DX-ray3.50AD/CD1-209[»]
4V5EX-ray3.45AD/CD1-209[»]
4V5FX-ray3.60AD/CD1-209[»]
4V5GX-ray3.60AD/CD1-209[»]
4V5JX-ray3.10AD/CD1-209[»]
4V5KX-ray3.20AD/CD1-209[»]
4V5LX-ray3.10AD1-209[»]
4V5Melectron microscopy7.80AD1-209[»]
4V5Nelectron microscopy7.60AD1-209[»]
4V5PX-ray3.10AD/CD1-209[»]
4V5QX-ray3.10AD/CD1-209[»]
4V5RX-ray3.10AD/CD1-209[»]
4V5SX-ray3.10AD/CD1-209[»]
4V5Zelectron microscopy8.70d1-209[»]
4V68electron microscopy6.40AD2-209[»]
4V6AX-ray3.10AD/CD1-209[»]
4V6FX-ray3.10BG/CG1-209[»]
4V6GX-ray3.50AG/CG1-209[»]
4V7JX-ray3.30Ad/Bd1-209[»]
4V7KX-ray3.60Ad/Bd1-209[»]
4V7LX-ray3.00AD/CD1-209[»]
4V7MX-ray3.45AD/CD1-209[»]
4V7WX-ray3.00AD/CD1-209[»]
4V7XX-ray3.00AD/CD1-209[»]
4V7YX-ray3.00AD/CD1-209[»]
4V7ZX-ray3.10AD/CD1-209[»]
4V87X-ray3.10BG/CG2-209[»]
4V8AX-ray3.20CD/DD1-209[»]
4V8BX-ray3.00AG/CG2-209[»]
4V8CX-ray3.30CG/DG2-209[»]
4V8DX-ray3.00AG/CG2-209[»]
4V8EX-ray3.30BG/DG2-209[»]
4V8FX-ray3.30BG/CG2-209[»]
4V8GX-ray3.00AD/CD1-209[»]
4V8HX-ray3.10AD/CD1-209[»]
4V8IX-ray2.70AD/CD1-209[»]
4V8JX-ray3.90AD/CD1-209[»]
4V8NX-ray3.10AD/CD1-209[»]
4V8OX-ray3.80AD1-209[»]
4V8QX-ray3.10BD1-209[»]
4V8UX-ray3.70AD/CD1-209[»]
4V8XX-ray3.35AD/CD1-209[»]
4V90X-ray2.95AD1-209[»]
4V95X-ray3.20AD/CD1-209[»]
4V97X-ray3.52AD/CD1-209[»]
4V9AX-ray3.30AG/CG2-209[»]
4V9BX-ray3.10AG/CG2-209[»]
4V9HX-ray2.86AD2-209[»]
4V9IX-ray3.30AD/CD2-209[»]
4V9RX-ray3.00AD/CD1-209[»]
4V9SX-ray3.10AD/CD1-209[»]
4W2EX-ray2.90d1-209[»]
4W2FX-ray2.40AD/CD1-209[»]
4W2GX-ray2.55AD/CD1-209[»]
4W2HX-ray2.70AD/CD1-209[»]
4W2IX-ray2.70AD/CD1-209[»]
4W4GX-ray3.30QD/XD1-209[»]
4WPOX-ray2.80BD/DD1-209[»]
4WQ1X-ray3.1032/3E2-209[»]
4WQFX-ray2.80BD/DD1-209[»]
4WQRX-ray3.1532/3E1-209[»]
4WQUX-ray2.80BD/DD1-209[»]
4WQYX-ray2.80BD/DD1-209[»]
4WR6X-ray3.0532/3E1-209[»]
4WRAX-ray3.0532/3E1-209[»]
4WROX-ray3.0532/3E1-209[»]
4WSDX-ray2.9532/3E1-209[»]
4WSMX-ray3.3032/3E1-209[»]
4WT1X-ray3.0532/3E1-209[»]
4WT8X-ray3.40AD/BD2-209[»]
4WU1X-ray3.2032/3E1-209[»]
4WZDX-ray3.1032/3E1-209[»]
4WZOX-ray3.3032/3E1-209[»]
4X62X-ray3.45D2-209[»]
4X64X-ray3.35D2-209[»]
4X65X-ray3.35D2-209[»]
4X66X-ray3.45D2-209[»]
4Y4OX-ray2.301d/2d1-209[»]
4Y4PX-ray2.501d/2d1-209[»]
4YHHX-ray3.42D2-209[»]
4YPBX-ray3.40QD/XD1-209[»]
4YY3X-ray3.60D1-209[»]
4YZVX-ray3.10QD/XD1-209[»]
4Z3SX-ray2.651d/2d1-209[»]
4Z8CX-ray2.901d/2d1-209[»]
4ZERX-ray3.101d/2d2-209[»]
4ZSNX-ray3.60QD/XD1-209[»]
5A9Zelectron microscopy4.70BH2-209[»]
5AA0electron microscopy5.00BH2-209[»]
5BR8X-ray3.40D1-209[»]
5CZPX-ray3.30QD/XD1-209[»]
5D8BX-ray3.63AC/EA1-209[»]
5DFEX-ray3.10QD/XD1-209[»]
5DOXX-ray3.101d/2d1-209[»]
5DOYX-ray2.601d/2d1-209[»]
5E7KX-ray3.2032/3E1-209[»]
5E81X-ray2.9532/3E1-209[»]
5EL4X-ray3.1532/3E1-209[»]
5EL5X-ray3.1532/3E1-209[»]
5EL6X-ray3.1032/3E1-209[»]
5EL7X-ray3.1532/3E1-209[»]
5F8KX-ray2.801d/2d2-209[»]
5FDUX-ray2.901d/2d2-209[»]
5FDVX-ray2.801d/2d2-209[»]
5HAUX-ray3.001d/2d1-209[»]
5HCPX-ray2.891d/2d1-209[»]
5HCQX-ray2.801d/2d1-209[»]
5HCRX-ray2.801d/2d1-209[»]
5HD1X-ray2.701d/2d1-209[»]
5IB7X-ray2.9932/3E1-209[»]
5IB8X-ray3.1332/3E1-209[»]
5IBBX-ray2.9632/3E1-209[»]
5IMQelectron microscopy3.80H1-209[»]
5IMRelectron microscopy-H1-209[»]
5IWAX-ray3.50D2-209[»]
5J30X-ray3.20QD/XD1-209[»]
5J3CX-ray3.04QD/XD1-209[»]
5J4BX-ray2.601d/2d1-209[»]
5J4CX-ray2.801d/2d1-209[»]
5J8BX-ray2.60d1-209[»]
5LMNelectron microscopy3.55D1-209[»]
5LMOelectron microscopy4.30D1-209[»]
5LMPelectron microscopy5.35D1-209[»]
5LMQelectron microscopy4.20D1-209[»]
5LMRelectron microscopy4.45D1-209[»]
5LMSelectron microscopy5.10D1-209[»]
5LMTelectron microscopy4.15D1-209[»]
5LMUelectron microscopy4.00D1-209[»]
5LMVelectron microscopy4.90D1-209[»]
ProteinModelPortaliP80373.
SMRiP80373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1665.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71488; BAD71488; BAD71488.
GeneIDi3168006.
KEGGittj:TTHA1665.
PATRICi23958285. VBITheThe93045_1635.

Phylogenomic databases

eggNOGiENOG4105G6W. Bacteria.
COG0522. LUCA.
HOGENOMiHOG000221004.
KOiK02986.
OMAiRTSDYGN.
PhylomeDBiP80373.

Miscellaneous databases

EvolutionaryTraceiP80373.

Family and domain databases

Gene3Di1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPiMF_01306_B. Ribosomal_S4_B. 1 hit.
InterProiIPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM01390. Ribosomal_S4. 1 hit.
SM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01017. rpsD_bact. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS4_THET8
AccessioniPrimary (citable) accession number: P80373
Secondary accession number(s): Q5SHR5, Q9Z9H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.