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Protein

30S ribosomal protein S6

Gene

rpsF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds together with S18 to 16S ribosomal RNA.

GO - Molecular functioni

  • mRNA 5'-UTR binding Source: EcoCyc
  • small ribosomal subunit rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10905-MONOMER.
ECOL316407:JW4158-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S6
Cleaved into the following 2 chains:
Gene namesi
Name:rpsF
Ordered Locus Names:b4200, JW4158
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10905. rpsF.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13513530S ribosomal protein S6, fully modified isoformPRO_0000030640Add
BLAST
Chaini1 – 13113130S ribosomal protein S6, non-modified isoformPRO_0000030641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931N6-acetyllysine1 Publication

Post-translational modificationi

5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form S6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the RimK enzyme.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP02358.
PRIDEiP02358.

2D gel databases

SWISS-2DPAGEP02358.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Interacts weakly with L2 in one of the 3.5 A resolved structures (PubMed:16272117).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsRP0A7T74EBI-543068,EBI-548844

Protein-protein interaction databases

DIPiDIP-10782N.
IntActiP02358. 57 interactions.
MINTiMINT-1279331.
STRINGi511145.b4200.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Beta strandi7 – 104Combined sources
Helixi13 – 175Combined sources
Helixi18 – 3114Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 456Combined sources
Beta strandi51 – 533Combined sources
Beta strandi57 – 615Combined sources
Beta strandi64 – 663Combined sources
Helixi70 – 8011Combined sources
Beta strandi82 – 887Combined sources
Beta strandi89 – 913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50C1-97[»]
1M5Gmodel-F1-100[»]
2YKRelectron microscopy9.80F1-100[»]
3IY8electron microscopy14.10F2-100[»]
3J9Yelectron microscopy3.90f1-135[»]
4A2Ielectron microscopy16.50F1-100[»]
4ADVelectron microscopy13.50F1-135[»]
4U1UX-ray2.95AF/CF1-100[»]
4U1VX-ray3.00AF/CF1-100[»]
4U20X-ray2.90AF/CF1-100[»]
4U24X-ray2.90AF/CF1-100[»]
4U25X-ray2.90AF/CF1-100[»]
4U26X-ray2.80AF/CF1-100[»]
4U27X-ray2.80AF/CF1-100[»]
4V47electron microscopy12.30BF1-135[»]
4V48electron microscopy11.50BF1-135[»]
4V4HX-ray3.46AF/CF1-135[»]
4V4QX-ray3.46AF/CF1-135[»]
4V4Velectron microscopy15.00AF1-95[»]
4V4Welectron microscopy15.00AF1-95[»]
4V50X-ray3.22AF/CF1-135[»]
4V52X-ray3.21AF/CF1-135[»]
4V53X-ray3.54AF/CF1-135[»]
4V54X-ray3.30AF/CF1-135[»]
4V55X-ray4.00AF/CF1-135[»]
4V56X-ray3.93AF/CF1-135[»]
4V57X-ray3.50AF/CF1-135[»]
4V5BX-ray3.74BF/DF1-135[»]
4V5Helectron microscopy5.80AF1-100[»]
4V5YX-ray4.45AF/CF1-135[»]
4V64X-ray3.50AF/CF1-135[»]
4V65electron microscopy9.00AT1-135[»]
4V66electron microscopy9.00AT1-135[»]
4V69electron microscopy6.70AF1-100[»]
4V6CX-ray3.19AF/CF1-135[»]
4V6DX-ray3.81AF/CF1-135[»]
4V6EX-ray3.71AF/CF1-135[»]
4V6Kelectron microscopy8.25BJ1-135[»]
4V6Lelectron microscopy13.20AJ1-135[»]
4V6Melectron microscopy7.10AF1-135[»]
4V6Nelectron microscopy12.10BI1-135[»]
4V6Oelectron microscopy14.70AI1-135[»]
4V6Pelectron microscopy13.50AI1-135[»]
4V6Qelectron microscopy11.50AI1-135[»]
4V6Relectron microscopy11.50AI1-135[»]
4V6Selectron microscopy13.10BH1-135[»]
4V6Telectron microscopy8.30AF1-100[»]
4V6Velectron microscopy9.80AF1-135[»]
4V6Yelectron microscopy12.00AF1-100[»]
4V6Zelectron microscopy12.00AF1-100[»]
4V70electron microscopy17.00AF1-100[»]
4V71electron microscopy20.00AF1-100[»]
4V72electron microscopy13.00AF1-100[»]
4V73electron microscopy15.00AF1-100[»]
4V74electron microscopy17.00AF1-100[»]
4V75electron microscopy12.00AF1-100[»]
4V76electron microscopy17.00AF1-100[»]
4V77electron microscopy17.00AF1-100[»]
4V78electron microscopy20.00AF1-100[»]
4V79electron microscopy15.00AF1-100[»]
4V7Aelectron microscopy9.00AF1-100[»]
4V7Belectron microscopy6.80AF1-135[»]
4V7Celectron microscopy7.60AF1-131[»]
4V7Delectron microscopy7.60BF1-131[»]
4V7Ielectron microscopy9.60BF1-135[»]
4V7SX-ray3.25AF/CF1-100[»]
4V7TX-ray3.19AF/CF1-100[»]
4V7UX-ray3.10AF/CF1-100[»]
4V7VX-ray3.29AF/CF1-100[»]
4V85X-ray3.20F1-131[»]
4V89X-ray3.70AF1-135[»]
4V9CX-ray3.30AF/CF1-135[»]
4V9DX-ray3.00AF/BF1-100[»]
4V9OX-ray2.90BF/DF/FF/HF1-135[»]
4V9PX-ray2.90BF/DF/FF/HF1-135[»]
4WF1X-ray3.09AF/CF1-100[»]
4WWWX-ray3.10QF/XF1-100[»]
4YBBX-ray2.10AF/BF1-106[»]
5AFIelectron microscopy2.90f1-135[»]
ProteinModelPortaliP02358.
SMRiP02358. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02358.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S6P family.Curated

Phylogenomic databases

eggNOGiCOG0360.
HOGENOMiHOG000040438.
InParanoidiP02358.
KOiK02990.
OMAiITEASPM.
PhylomeDBiP02358.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
HAMAPiMF_00360. Ribosomal_S6.
InterProiIPR000529. Ribosomal_S6.
IPR020815. Ribosomal_S6_CS.
IPR020814. Ribosomal_S6_plastid/chlpt.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
[Graphical view]
PfamiPF01250. Ribosomal_S6. 1 hit.
[Graphical view]
SUPFAMiSSF54995. SSF54995. 1 hit.
TIGRFAMsiTIGR00166. S6. 1 hit.
PROSITEiPS01048. RIBOSOMAL_S6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02358-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHYEIVFMV HPDQSEQVPG MIERYTAAIT GAEGKIHRLE DWGRRQLAYP
60 70 80 90 100
INKLHKAHYV LMNVEAPQEV IDELETTFRF NDAVIRSMVM RTKHAVTEAS
110 120 130
PMVKAKDERR ERRDDFANET ADDAEAGDSE EEEEE
Length:135
Mass (Da):15,703
Last modified:July 21, 1986 - v1
Checksum:iF4CC629711C1FD0E
GO

Sequence cautioni

The sequence AAA97096.1 differs from that shown.Up to 4 Glu residues can be added post-translationally.Curated
The sequence AAC77157.5 differs from that shown.Up to 4 Glu residues can be added post-translationally.Curated
The sequence BAE78201.1 differs from that shown.Up to 4 Glu residues can be added post-translationally.Curated
The sequence CAA27652.1 differs from that shown.Up to 4 Glu residues can be added post-translationally.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141Q → T AA sequence (PubMed:9868784).Curated
Sequence conflicti20 – 201G → A AA sequence (PubMed:9868784).Curated

Mass spectrometryi

Molecular mass is 15187.2 Da from positions 1 - 131. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA. Translation: CAA27652.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97096.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC77157.5. Sequence problems.
AP009048 Genomic DNA. Translation: BAE78201.1. Sequence problems.
PIRiC65231. R3EC6.
RefSeqiNP_418621.5. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC77157; AAC77157; b4200.
BAE78201; BAE78201; BAE78201.
GeneIDi948723.
KEGGieco:b4200.
PATRICi48667972. VBIEscCol107702_4239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA. Translation: CAA27652.1. Sequence problems.
U14003 Genomic DNA. Translation: AAA97096.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC77157.5. Sequence problems.
AP009048 Genomic DNA. Translation: BAE78201.1. Sequence problems.
PIRiC65231. R3EC6.
RefSeqiNP_418621.5. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50C1-97[»]
1M5Gmodel-F1-100[»]
2YKRelectron microscopy9.80F1-100[»]
3IY8electron microscopy14.10F2-100[»]
3J9Yelectron microscopy3.90f1-135[»]
4A2Ielectron microscopy16.50F1-100[»]
4ADVelectron microscopy13.50F1-135[»]
4U1UX-ray2.95AF/CF1-100[»]
4U1VX-ray3.00AF/CF1-100[»]
4U20X-ray2.90AF/CF1-100[»]
4U24X-ray2.90AF/CF1-100[»]
4U25X-ray2.90AF/CF1-100[»]
4U26X-ray2.80AF/CF1-100[»]
4U27X-ray2.80AF/CF1-100[»]
4V47electron microscopy12.30BF1-135[»]
4V48electron microscopy11.50BF1-135[»]
4V4HX-ray3.46AF/CF1-135[»]
4V4QX-ray3.46AF/CF1-135[»]
4V4Velectron microscopy15.00AF1-95[»]
4V4Welectron microscopy15.00AF1-95[»]
4V50X-ray3.22AF/CF1-135[»]
4V52X-ray3.21AF/CF1-135[»]
4V53X-ray3.54AF/CF1-135[»]
4V54X-ray3.30AF/CF1-135[»]
4V55X-ray4.00AF/CF1-135[»]
4V56X-ray3.93AF/CF1-135[»]
4V57X-ray3.50AF/CF1-135[»]
4V5BX-ray3.74BF/DF1-135[»]
4V5Helectron microscopy5.80AF1-100[»]
4V5YX-ray4.45AF/CF1-135[»]
4V64X-ray3.50AF/CF1-135[»]
4V65electron microscopy9.00AT1-135[»]
4V66electron microscopy9.00AT1-135[»]
4V69electron microscopy6.70AF1-100[»]
4V6CX-ray3.19AF/CF1-135[»]
4V6DX-ray3.81AF/CF1-135[»]
4V6EX-ray3.71AF/CF1-135[»]
4V6Kelectron microscopy8.25BJ1-135[»]
4V6Lelectron microscopy13.20AJ1-135[»]
4V6Melectron microscopy7.10AF1-135[»]
4V6Nelectron microscopy12.10BI1-135[»]
4V6Oelectron microscopy14.70AI1-135[»]
4V6Pelectron microscopy13.50AI1-135[»]
4V6Qelectron microscopy11.50AI1-135[»]
4V6Relectron microscopy11.50AI1-135[»]
4V6Selectron microscopy13.10BH1-135[»]
4V6Telectron microscopy8.30AF1-100[»]
4V6Velectron microscopy9.80AF1-135[»]
4V6Yelectron microscopy12.00AF1-100[»]
4V6Zelectron microscopy12.00AF1-100[»]
4V70electron microscopy17.00AF1-100[»]
4V71electron microscopy20.00AF1-100[»]
4V72electron microscopy13.00AF1-100[»]
4V73electron microscopy15.00AF1-100[»]
4V74electron microscopy17.00AF1-100[»]
4V75electron microscopy12.00AF1-100[»]
4V76electron microscopy17.00AF1-100[»]
4V77electron microscopy17.00AF1-100[»]
4V78electron microscopy20.00AF1-100[»]
4V79electron microscopy15.00AF1-100[»]
4V7Aelectron microscopy9.00AF1-100[»]
4V7Belectron microscopy6.80AF1-135[»]
4V7Celectron microscopy7.60AF1-131[»]
4V7Delectron microscopy7.60BF1-131[»]
4V7Ielectron microscopy9.60BF1-135[»]
4V7SX-ray3.25AF/CF1-100[»]
4V7TX-ray3.19AF/CF1-100[»]
4V7UX-ray3.10AF/CF1-100[»]
4V7VX-ray3.29AF/CF1-100[»]
4V85X-ray3.20F1-131[»]
4V89X-ray3.70AF1-135[»]
4V9CX-ray3.30AF/CF1-135[»]
4V9DX-ray3.00AF/BF1-100[»]
4V9OX-ray2.90BF/DF/FF/HF1-135[»]
4V9PX-ray2.90BF/DF/FF/HF1-135[»]
4WF1X-ray3.09AF/CF1-100[»]
4WWWX-ray3.10QF/XF1-100[»]
4YBBX-ray2.10AF/BF1-106[»]
5AFIelectron microscopy2.90f1-135[»]
ProteinModelPortaliP02358.
SMRiP02358. Positions 1-100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10782N.
IntActiP02358. 57 interactions.
MINTiMINT-1279331.
STRINGi511145.b4200.

Chemistry

ChEMBLiCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP02358.

Proteomic databases

PaxDbiP02358.
PRIDEiP02358.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77157; AAC77157; b4200.
BAE78201; BAE78201; BAE78201.
GeneIDi948723.
KEGGieco:b4200.
PATRICi48667972. VBIEscCol107702_4239.

Organism-specific databases

EchoBASEiEB0898.
EcoGeneiEG10905. rpsF.

Phylogenomic databases

eggNOGiCOG0360.
HOGENOMiHOG000040438.
InParanoidiP02358.
KOiK02990.
OMAiITEASPM.
PhylomeDBiP02358.

Enzyme and pathway databases

BioCyciEcoCyc:EG10905-MONOMER.
ECOL316407:JW4158-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02358.
PROiP02358.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
HAMAPiMF_00360. Ribosomal_S6.
InterProiIPR000529. Ribosomal_S6.
IPR020815. Ribosomal_S6_CS.
IPR020814. Ribosomal_S6_plastid/chlpt.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
[Graphical view]
PfamiPF01250. Ribosomal_S6. 1 hit.
[Graphical view]
SUPFAMiSSF54995. SSF54995. 1 hit.
TIGRFAMsiTIGR00166. S6. 1 hit.
PROSITEiPS01048. RIBOSOMAL_S6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Determination of the complete amino-acid sequence of protein S6 from the wild-type and a mutant of Escherichia coli."
    Hitz H., Schaefer D., Wittmann-Liebold B.
    Eur. J. Biochem. 75:497-512(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: K.
  2. "The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame."
    Schnier J., Kitakawa M., Isono K.
    Mol. Gen. Genet. 204:126-132(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
  3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-131.
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-131.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-131.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
    Strain: K12.
  7. Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  9. Cited for: PROTEIN SEQUENCE OF 1-4.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  11. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  12. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  13. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  14. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS6_ECOLI
AccessioniPrimary (citable) accession number: P02358
Secondary accession number(s): Q2M6A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 169 of the entry and version 1 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.