Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

50S ribosomal protein L3

Gene

rplC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

One of two assembly initiator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10866-MONOMER.
ECOL316407:JW3282-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L3
Gene namesi
Name:rplC
Ordered Locus Names:b3320, JW3282
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10866. rplC.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20920950S ribosomal protein L3PRO_0000077098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysine1 Publication
Modified residuei150 – 1501N5-methylglutamine1 Publication

Post-translational modificationi

Methylated by PrmB.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP60438.
PRIDEiP60438.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.

Protein-protein interaction databases

DIPiDIP-10744N.
IntActiP60438. 144 interactions.
MINTiMINT-1302843.
STRINGi511145.b3320.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1512Combined sources
Turni17 – 193Combined sources
Beta strandi21 – 288Combined sources
Beta strandi32 – 387Combined sources
Turni40 – 434Combined sources
Beta strandi47 – 537Combined sources
Helixi57 – 593Combined sources
Helixi62 – 7110Combined sources
Beta strandi77 – 837Combined sources
Turni91 – 933Combined sources
Helixi98 – 1014Combined sources
Turni102 – 1043Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi115 – 1195Combined sources
Helixi121 – 1255Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1423Combined sources
Turni150 – 1523Combined sources
Helixi155 – 1573Combined sources
Beta strandi163 – 18119Combined sources
Helixi182 – 1843Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi199 – 2057Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
2J28electron microscopy8.00D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J7Zelectron microscopy3.90D1-209[»]
3J9Yelectron microscopy3.90D1-209[»]
4CSUelectron microscopy5.50D1-209[»]
4U1UX-ray2.95BD/DD1-209[»]
4U1VX-ray3.00BD/DD1-209[»]
4U20X-ray2.90BD/DD1-209[»]
4U24X-ray2.90BD/DD1-209[»]
4U25X-ray2.90BD/DD1-209[»]
4U26X-ray2.80BD/DD1-209[»]
4U27X-ray2.80BD/DD1-209[»]
4UY8electron microscopy3.80D1-209[»]
4V47electron microscopy12.30AB1-209[»]
4V48electron microscopy11.50AB1-209[»]
4V4HX-ray3.46BD/DD1-209[»]
4V4QX-ray3.46BD/DD1-209[»]
4V4Velectron microscopy15.00BB1-209[»]
4V4Welectron microscopy15.00BB1-209[»]
4V50X-ray3.22BD/DD1-209[»]
4V52X-ray3.21BD/DD1-209[»]
4V53X-ray3.54BD/DD1-209[»]
4V54X-ray3.30BD/DD1-209[»]
4V55X-ray4.00BD/DD1-209[»]
4V56X-ray3.93BD/DD1-209[»]
4V57X-ray3.50BD/DD1-209[»]
4V5BX-ray3.74AD/CD1-209[»]
4V5Helectron microscopy5.80BD1-209[»]
4V5YX-ray4.45BD/DD1-209[»]
4V64X-ray3.50BD/DD1-209[»]
4V65electron microscopy9.00BY1-209[»]
4V66electron microscopy9.00BY1-209[»]
4V69electron microscopy6.70BD1-209[»]
4V6CX-ray3.19BD/DD1-209[»]
4V6DX-ray3.81BD/DD1-209[»]
4V6EX-ray3.71BD/DD1-209[»]
4V6Kelectron microscopy8.25AE1-209[»]
4V6Lelectron microscopy13.20BE1-209[»]
4V6Melectron microscopy7.10BD1-209[»]
4V6Nelectron microscopy12.10AE1-209[»]
4V6Oelectron microscopy14.70BE1-209[»]
4V6Pelectron microscopy13.50BE1-209[»]
4V6Qelectron microscopy11.50BE1-209[»]
4V6Relectron microscopy11.50BE1-209[»]
4V6Selectron microscopy13.10AE1-209[»]
4V6Telectron microscopy8.30BD1-209[»]
4V6Velectron microscopy9.80BE1-209[»]
4V6Yelectron microscopy12.00BD1-209[»]
4V6Zelectron microscopy12.00BD1-209[»]
4V70electron microscopy17.00BD1-209[»]
4V71electron microscopy20.00BD1-209[»]
4V72electron microscopy13.00BD1-209[»]
4V73electron microscopy15.00BD1-209[»]
4V74electron microscopy17.00BD1-209[»]
4V75electron microscopy12.00BD1-209[»]
4V76electron microscopy17.00BD1-209[»]
4V77electron microscopy17.00BD1-209[»]
4V78electron microscopy20.00BD1-209[»]
4V79electron microscopy15.00BD1-209[»]
4V7Aelectron microscopy9.00BD1-209[»]
4V7Belectron microscopy6.80BD1-209[»]
4V7Celectron microscopy7.60BE1-209[»]
4V7Delectron microscopy7.60AE1-209[»]
4V7Ielectron microscopy9.60AD1-209[»]
4V7SX-ray3.25BD/DD1-209[»]
4V7TX-ray3.19BD/DD1-209[»]
4V7UX-ray3.10BD/DD1-209[»]
4V7VX-ray3.29BD/DD1-209[»]
4V85X-ray3.20D1-209[»]
4V89X-ray3.70BD1-209[»]
4V9CX-ray3.30BD/DD1-209[»]
4V9DX-ray3.00CD/DD1-209[»]
4V9OX-ray2.90AD/CD/ED/GD1-209[»]
4V9PX-ray2.90AD/CD/ED/GD1-209[»]
4WF1X-ray3.09BD/DD1-209[»]
4WWWX-ray3.10RD/YD1-209[»]
4YBBX-ray2.10CD/DD1-209[»]
5AFIelectron microscopy2.90D1-209[»]
5AKAelectron microscopy5.70D1-209[»]
ProteinModelPortaliP60438.
SMRiP60438. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60438.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiCOG0087.
HOGENOMiHOG000100368.
InParanoidiP60438.
KOiK02906.
OMAiVFKGLRM.
OrthoDBiEOG6WDSMH.
PhylomeDBiP60438.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B.
InterProiIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60438-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGLVGKKVG MTRIFTEDGV SIPVTVIEVE ANRVTQVKDL ANDGYRAIQV
60 70 80 90 100
TTGAKKANRV TKPEAGHFAK AGVEAGRGLW EFRLAEGEEF TVGQSISVEL
110 120 130 140 150
FADVKKVDVT GTSKGKGFAG TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ
160 170 180 190 200
TPGKVFKGKK MAGQMGNERV TVQSLDVVRV DAERNLLLVK GAVPGATGSD

LIVKPAVKA
Length:209
Mass (Da):22,244
Last modified:July 21, 1986 - v1
Checksum:iEA8E10EDD2C0A8FD
GO

Mass spectrometryi

Molecular mass is 22257.2 Da from positions 1 - 209. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26460.1.
U18997 Genomic DNA. Translation: AAA58117.1.
U00096 Genomic DNA. Translation: AAC76345.1.
AP009048 Genomic DNA. Translation: BAE77971.1.
V00344 Genomic DNA. Translation: CAA23634.1.
PIRiA02757. R5EC3.
RefSeqiNP_417779.1. NC_000913.3.
WP_000579833.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneIDi947817.
KEGGieco:b3320.
PATRICi32122072. VBIEscCol129921_3413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26460.1.
U18997 Genomic DNA. Translation: AAA58117.1.
U00096 Genomic DNA. Translation: AAC76345.1.
AP009048 Genomic DNA. Translation: BAE77971.1.
V00344 Genomic DNA. Translation: CAA23634.1.
PIRiA02757. R5EC3.
RefSeqiNP_417779.1. NC_000913.3.
WP_000579833.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
2J28electron microscopy8.00D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J7Zelectron microscopy3.90D1-209[»]
3J9Yelectron microscopy3.90D1-209[»]
4CSUelectron microscopy5.50D1-209[»]
4U1UX-ray2.95BD/DD1-209[»]
4U1VX-ray3.00BD/DD1-209[»]
4U20X-ray2.90BD/DD1-209[»]
4U24X-ray2.90BD/DD1-209[»]
4U25X-ray2.90BD/DD1-209[»]
4U26X-ray2.80BD/DD1-209[»]
4U27X-ray2.80BD/DD1-209[»]
4UY8electron microscopy3.80D1-209[»]
4V47electron microscopy12.30AB1-209[»]
4V48electron microscopy11.50AB1-209[»]
4V4HX-ray3.46BD/DD1-209[»]
4V4QX-ray3.46BD/DD1-209[»]
4V4Velectron microscopy15.00BB1-209[»]
4V4Welectron microscopy15.00BB1-209[»]
4V50X-ray3.22BD/DD1-209[»]
4V52X-ray3.21BD/DD1-209[»]
4V53X-ray3.54BD/DD1-209[»]
4V54X-ray3.30BD/DD1-209[»]
4V55X-ray4.00BD/DD1-209[»]
4V56X-ray3.93BD/DD1-209[»]
4V57X-ray3.50BD/DD1-209[»]
4V5BX-ray3.74AD/CD1-209[»]
4V5Helectron microscopy5.80BD1-209[»]
4V5YX-ray4.45BD/DD1-209[»]
4V64X-ray3.50BD/DD1-209[»]
4V65electron microscopy9.00BY1-209[»]
4V66electron microscopy9.00BY1-209[»]
4V69electron microscopy6.70BD1-209[»]
4V6CX-ray3.19BD/DD1-209[»]
4V6DX-ray3.81BD/DD1-209[»]
4V6EX-ray3.71BD/DD1-209[»]
4V6Kelectron microscopy8.25AE1-209[»]
4V6Lelectron microscopy13.20BE1-209[»]
4V6Melectron microscopy7.10BD1-209[»]
4V6Nelectron microscopy12.10AE1-209[»]
4V6Oelectron microscopy14.70BE1-209[»]
4V6Pelectron microscopy13.50BE1-209[»]
4V6Qelectron microscopy11.50BE1-209[»]
4V6Relectron microscopy11.50BE1-209[»]
4V6Selectron microscopy13.10AE1-209[»]
4V6Telectron microscopy8.30BD1-209[»]
4V6Velectron microscopy9.80BE1-209[»]
4V6Yelectron microscopy12.00BD1-209[»]
4V6Zelectron microscopy12.00BD1-209[»]
4V70electron microscopy17.00BD1-209[»]
4V71electron microscopy20.00BD1-209[»]
4V72electron microscopy13.00BD1-209[»]
4V73electron microscopy15.00BD1-209[»]
4V74electron microscopy17.00BD1-209[»]
4V75electron microscopy12.00BD1-209[»]
4V76electron microscopy17.00BD1-209[»]
4V77electron microscopy17.00BD1-209[»]
4V78electron microscopy20.00BD1-209[»]
4V79electron microscopy15.00BD1-209[»]
4V7Aelectron microscopy9.00BD1-209[»]
4V7Belectron microscopy6.80BD1-209[»]
4V7Celectron microscopy7.60BE1-209[»]
4V7Delectron microscopy7.60AE1-209[»]
4V7Ielectron microscopy9.60AD1-209[»]
4V7SX-ray3.25BD/DD1-209[»]
4V7TX-ray3.19BD/DD1-209[»]
4V7UX-ray3.10BD/DD1-209[»]
4V7VX-ray3.29BD/DD1-209[»]
4V85X-ray3.20D1-209[»]
4V89X-ray3.70BD1-209[»]
4V9CX-ray3.30BD/DD1-209[»]
4V9DX-ray3.00CD/DD1-209[»]
4V9OX-ray2.90AD/CD/ED/GD1-209[»]
4V9PX-ray2.90AD/CD/ED/GD1-209[»]
4WF1X-ray3.09BD/DD1-209[»]
4WWWX-ray3.10RD/YD1-209[»]
4YBBX-ray2.10CD/DD1-209[»]
5AFIelectron microscopy2.90D1-209[»]
5AKAelectron microscopy5.70D1-209[»]
ProteinModelPortaliP60438.
SMRiP60438. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10744N.
IntActiP60438. 144 interactions.
MINTiMINT-1302843.
STRINGi511145.b3320.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP60438.
PRIDEiP60438.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneIDi947817.
KEGGieco:b3320.
PATRICi32122072. VBIEscCol129921_3413.

Organism-specific databases

EchoBASEiEB0859.
EcoGeneiEG10866. rplC.

Phylogenomic databases

eggNOGiCOG0087.
HOGENOMiHOG000100368.
InParanoidiP60438.
KOiK02906.
OMAiVFKGLRM.
OrthoDBiEOG6WDSMH.
PhylomeDBiP60438.

Enzyme and pathway databases

BioCyciEcoCyc:EG10866-MONOMER.
ECOL316407:JW3282-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60438.
PROiP60438.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B.
InterProiIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of ribosomal protein L3 from Escherichia coli 70 S ribosomes."
    Muranova T.A., Muranov A.V., Markova L.F., Ovchinnikov Y.A.
    FEBS Lett. 96:301-305(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, METHYLATION AT GLN-150.
    Strain: MRE-600.
  2. "Structure of the Escherichia coli S10 ribosomal protein operon."
    Zurawski G., Zurawski S.M.
    Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Regulation of the S10 ribosomal protein operon in E. coli: nucleotide sequence at the start of the operon."
    Olins P.O., Nomura M.
    Cell 26:205-211(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
  6. "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.
  7. "Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes."
    Nowotny V., Nierhaus K.H.
    Proc. Natl. Acad. Sci. U.S.A. 79:7238-7242(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS AN ASSEMBLY INITIATOR PROTEIN.
  8. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
    Strain: K12.
  9. "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.
  10. "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.
  11. "The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors."
    Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.
    EMBO J. 21:769-778(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION BY PRMB.
    Strain: K12.
  12. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-38.
    Strain: K12.
  13. "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.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  15. "Molecular basis for the ribosome functioning as an L-tryptophan sensor."
    Bischoff L., Berninghausen O., Beckmann R.
    Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL3_ECOLI
AccessioniPrimary (citable) accession number: P60438
Secondary accession number(s): P02386, Q2M6Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 123 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.