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Protein

50S ribosomal protein L4

Gene

rplD

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

Functioni

One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.2 Publications
Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).4 Publications
Forms part of the polypeptide exit tunnel.2 Publications
Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.1 Publication

GO - Molecular functioni

  • endoribonuclease inhibitor activity Source: EcoCyc
  • RNA binding Source: GO_Central
  • rRNA binding Source: UniProtKB-HAMAP
  • structural constituent of ribosome Source: GO_Central
  • translation repressor activity Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance, Transcription, Transcription regulation, Transcription termination, Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10867-MONOMER.
ECOL316407:JW3281-MONOMER.
MetaCyc:EG10867-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L4
Gene namesi
Name:rplD
Synonyms:eryA
Ordered Locus Names:b3319, JW3281
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10867. rplD.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40 – 88Missing : Regulates the S10 operon normally. Assembles into ribosomes in vivo. 1 PublicationAdd BLAST49
Mutagenesisi67 – 103Missing : Regulates the S10 operon normally. Does not assemble into ribosomes in vivo. 1 PublicationAdd BLAST37
Mutagenesisi93 – 101Missing : Regulates the S10 operon normally. Not stably associated with the ribosome in vivo. 1 Publication9
Mutagenesisi131T → I: Does not regulate the S10 operon; assembles into ribosomes in vivo. 1 Publication1
Mutagenesisi134L → P: Does not regulate the S10 operon in vivo. 1 Publication1
Mutagenesisi160A → V: Does not regulate the S10 operon; assembles into ribosomes in vivo. 1 Publication1
Mutagenesisi167V → D: Does not regulate the S10 operon in vivo. 1 Publication1
Mutagenesisi171 – 201DATGI…EEMLA → RRSK: Loss of S10 operon regulation. Assembles into ribosomes in vivo. 1 PublicationAdd BLAST31

Chemistry databases

DrugBankiDB01361. Troleandomycin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001292151 – 20150S ribosomal protein L4Add BLAST201

Proteomic databases

EPDiP60723.
PaxDbiP60723.
PRIDEiP60723.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

BioGridi4261291. 50 interactors.
DIPiDIP-35791N.
IntActiP60723. 214 interactors.
MINTiMINT-1219709.
STRINGi511145.b3319.

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni6 – 8Combined sources3
Helixi16 – 19Combined sources4
Beta strandi22 – 24Combined sources3
Helixi25 – 39Combined sources15
Turni49 – 51Combined sources3
Beta strandi52 – 54Combined sources3
Beta strandi62 – 67Combined sources6
Beta strandi78 – 80Combined sources3
Beta strandi83 – 85Combined sources3
Helixi98 – 114Combined sources17
Beta strandi118 – 122Combined sources5
Beta strandi127 – 129Combined sources3
Helixi131 – 141Combined sources11
Beta strandi144 – 152Combined sources9
Helixi155 – 159Combined sources5
Turni160 – 163Combined sources4
Beta strandi164 – 166Combined sources3
Beta strandi167 – 171Combined sources5
Helixi172 – 174Combined sources3
Helixi179 – 182Combined sources4
Beta strandi183 – 189Combined sources7
Helixi190 – 200Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00E1-201[»]
2RDOelectron microscopy9.10E1-201[»]
3BBXelectron microscopy10.00E1-201[»]
3J5Lelectron microscopy6.60E1-201[»]
3J7Zelectron microscopy3.90E1-201[»]
3J8Gelectron microscopy5.00E1-201[»]
3J9Yelectron microscopy3.90E1-201[»]
3J9Zelectron microscopy3.60L61-201[»]
3JA1electron microscopy3.60LF1-201[»]
3JBUelectron microscopy3.64e1-201[»]
3JBVelectron microscopy3.32e1-201[»]
3JCDelectron microscopy3.70E1-201[»]
3JCEelectron microscopy3.20E1-201[»]
3JCJelectron microscopy3.70D1-201[»]
3JCNelectron microscopy4.60E1-201[»]
4CSUelectron microscopy5.50E1-201[»]
4U1UX-ray2.95BE/DE1-201[»]
4U1VX-ray3.00BE/DE1-201[»]
4U20X-ray2.90BE/DE1-201[»]
4U24X-ray2.90BE/DE1-201[»]
4U25X-ray2.90BE/DE1-201[»]
4U26X-ray2.80BE/DE1-201[»]
4U27X-ray2.80BE/DE1-201[»]
4UY8electron microscopy3.80E1-201[»]
4V47electron microscopy12.30AC1-201[»]
4V48electron microscopy11.50AC1-201[»]
4V4HX-ray3.46BE/DE1-201[»]
4V4QX-ray3.46BE/DE1-201[»]
4V4Velectron microscopy15.00BC1-198[»]
4V4Welectron microscopy15.00BC1-198[»]
4V50X-ray3.22BE/DE1-201[»]
4V52X-ray3.21BE/DE1-201[»]
4V53X-ray3.54BE/DE1-201[»]
4V54X-ray3.30BE/DE1-201[»]
4V55X-ray4.00BE/DE1-201[»]
4V56X-ray3.93BE/DE1-201[»]
4V57X-ray3.50BE/DE1-201[»]
4V5BX-ray3.74AE/CE1-201[»]
4V5Helectron microscopy5.80BE1-201[»]
4V5YX-ray4.45BE/DE1-201[»]
4V64X-ray3.50BE/DE1-201[»]
4V65electron microscopy9.00B11-201[»]
4V66electron microscopy9.00B11-201[»]
4V69electron microscopy6.70BE1-201[»]
4V6CX-ray3.19BE/DE1-201[»]
4V6DX-ray3.81BE/DE1-201[»]
4V6EX-ray3.71BE/DE1-201[»]
4V6Kelectron microscopy8.25AF1-201[»]
4V6Lelectron microscopy13.20BF1-201[»]
4V6Melectron microscopy7.10BE1-201[»]
4V6Nelectron microscopy12.10AF1-201[»]
4V6Oelectron microscopy14.70BF1-201[»]
4V6Pelectron microscopy13.50BF1-201[»]
4V6Qelectron microscopy11.50BF1-201[»]
4V6Relectron microscopy11.50BF1-201[»]
4V6Selectron microscopy13.10AF1-201[»]
4V6Telectron microscopy8.30BE1-201[»]
4V6Velectron microscopy9.80BF1-201[»]
4V6Yelectron microscopy12.00BE1-201[»]
4V6Zelectron microscopy12.00BE1-201[»]
4V70electron microscopy17.00BE1-201[»]
4V71electron microscopy20.00BE1-201[»]
4V72electron microscopy13.00BE1-201[»]
4V73electron microscopy15.00BE1-201[»]
4V74electron microscopy17.00BE1-201[»]
4V75electron microscopy12.00BE1-201[»]
4V76electron microscopy17.00BE1-201[»]
4V77electron microscopy17.00BE1-201[»]
4V78electron microscopy20.00BE1-201[»]
4V79electron microscopy15.00BE1-201[»]
4V7Aelectron microscopy9.00BE1-201[»]
4V7Belectron microscopy6.80BE1-201[»]
4V7Celectron microscopy7.60BF1-201[»]
4V7Delectron microscopy7.60AF1-201[»]
4V7Ielectron microscopy9.60AE1-201[»]
4V7SX-ray3.25BE/DE1-201[»]
4V7TX-ray3.19BE/DE1-201[»]
4V7UX-ray3.10BE/DE1-201[»]
4V7VX-ray3.29BE/DE1-201[»]
4V85X-ray3.20E1-201[»]
4V89X-ray3.70BE1-201[»]
4V9CX-ray3.30BE/DE1-201[»]
4V9DX-ray3.00CE/DE1-201[»]
4V9OX-ray2.90AE/CE/EE/GE1-201[»]
4V9PX-ray2.90AE/CE/EE/GE1-201[»]
4WF1X-ray3.09BE/DE1-201[»]
4WOIX-ray3.00BE/CE1-201[»]
4WWWX-ray3.10RE/YE1-201[»]
4YBBX-ray2.10CE/DE1-201[»]
5ADYelectron microscopy4.50E1-201[»]
5AFIelectron microscopy2.90E1-201[»]
5AKAelectron microscopy5.70E1-201[»]
5GADelectron microscopy3.70E1-201[»]
5GAEelectron microscopy3.33E1-201[»]
5GAFelectron microscopy4.30E1-201[»]
5GAGelectron microscopy3.80E1-201[»]
5GAHelectron microscopy3.80E1-201[»]
5IQRelectron microscopy3.00D1-201[»]
5IT8X-ray3.12CE/DE1-201[»]
5J5BX-ray2.80CE/DE1-201[»]
5J7LX-ray3.00CE/DE1-201[»]
5J88X-ray3.32CE/DE1-201[»]
5J8AX-ray3.10CE/DE1-201[»]
5J91X-ray2.96CE/DE1-201[»]
5JC9X-ray3.03CE/DE1-201[»]
5JTEelectron microscopy3.60BE1-201[»]
5JU8electron microscopy3.60BE1-201[»]
5KCRelectron microscopy3.601F1-201[»]
5KCSelectron microscopy3.901F1-201[»]
5KPSelectron microscopy3.90D1-201[»]
5KPVelectron microscopy4.10C1-201[»]
5KPWelectron microscopy3.90C1-201[»]
5KPXelectron microscopy3.90C1-201[»]
5L3Pelectron microscopy3.70F1-201[»]
DisProtiDP00600.
ProteinModelPortaliP60723.
SMRiP60723.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60723.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiCOG0088. LUCA.
HOGENOMiHOG000248766.
InParanoidiP60723.
KOiK02926.
OMAiGVSHGPS.
PhylomeDBiP60723.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
HAMAPiMF_01328_B. Ribosomal_L4_B. 1 hit.
InterProiIPR002136. Ribosomal_L4/L1e.
IPR023574. Ribosomal_L4_dom.
IPR013005. Ribosomal_uL4/L1e.
[Graphical view]
PANTHERiPTHR10746. PTHR10746. 1 hit.
PfamiPF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
TIGRFAMsiTIGR03953. rplD_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P60723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA
60 70 80 90 100
EVTGSGKKPW RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM
110 120 130 140 150
YRGALKSILS ELVRQDRLIV VEKFSVEAPK TKLLAQKLKD MALEDVLIIT
160 170 180 190 200
GELDENLFLA ARNLHKVDVR DATGIDPVSL IAFDKVVMTA DAVKQVEEML

A
Length:201
Mass (Da):22,087
Last modified:July 21, 1986 - v1
Checksum:i3A953206B0F083B5
GO

Mass spectrometryi

Molecular mass is 22086.2 Da from positions 1 - 201. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti63K → E in strain: N282; confers erythromycin resistance. Ribosomes bind erythromycin poorly and have reduced peptidyltransferase activity. 50S subunits assemble normally, even in the presence of drug, but assembly is cold-sensitive at 20 degrees Celsius. 3 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26461.1.
U18997 Genomic DNA. Translation: AAA58116.1.
U00096 Genomic DNA. Translation: AAC76344.1.
AP009048 Genomic DNA. Translation: BAE77972.1.
PIRiC23129. R5EC4.
RefSeqiNP_417778.1. NC_000913.3.
WP_000424395.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76344; AAC76344; b3319.
BAE77972; BAE77972; BAE77972.
GeneIDi5548703.
947818.
KEGGiecj:JW3281.
eco:b3319.
PATRICi32122070. VBIEscCol129921_3412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02613 Genomic DNA. Translation: CAA26461.1.
U18997 Genomic DNA. Translation: AAA58116.1.
U00096 Genomic DNA. Translation: AAC76344.1.
AP009048 Genomic DNA. Translation: BAE77972.1.
PIRiC23129. R5EC4.
RefSeqiNP_417778.1. NC_000913.3.
WP_000424395.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00E1-201[»]
2RDOelectron microscopy9.10E1-201[»]
3BBXelectron microscopy10.00E1-201[»]
3J5Lelectron microscopy6.60E1-201[»]
3J7Zelectron microscopy3.90E1-201[»]
3J8Gelectron microscopy5.00E1-201[»]
3J9Yelectron microscopy3.90E1-201[»]
3J9Zelectron microscopy3.60L61-201[»]
3JA1electron microscopy3.60LF1-201[»]
3JBUelectron microscopy3.64e1-201[»]
3JBVelectron microscopy3.32e1-201[»]
3JCDelectron microscopy3.70E1-201[»]
3JCEelectron microscopy3.20E1-201[»]
3JCJelectron microscopy3.70D1-201[»]
3JCNelectron microscopy4.60E1-201[»]
4CSUelectron microscopy5.50E1-201[»]
4U1UX-ray2.95BE/DE1-201[»]
4U1VX-ray3.00BE/DE1-201[»]
4U20X-ray2.90BE/DE1-201[»]
4U24X-ray2.90BE/DE1-201[»]
4U25X-ray2.90BE/DE1-201[»]
4U26X-ray2.80BE/DE1-201[»]
4U27X-ray2.80BE/DE1-201[»]
4UY8electron microscopy3.80E1-201[»]
4V47electron microscopy12.30AC1-201[»]
4V48electron microscopy11.50AC1-201[»]
4V4HX-ray3.46BE/DE1-201[»]
4V4QX-ray3.46BE/DE1-201[»]
4V4Velectron microscopy15.00BC1-198[»]
4V4Welectron microscopy15.00BC1-198[»]
4V50X-ray3.22BE/DE1-201[»]
4V52X-ray3.21BE/DE1-201[»]
4V53X-ray3.54BE/DE1-201[»]
4V54X-ray3.30BE/DE1-201[»]
4V55X-ray4.00BE/DE1-201[»]
4V56X-ray3.93BE/DE1-201[»]
4V57X-ray3.50BE/DE1-201[»]
4V5BX-ray3.74AE/CE1-201[»]
4V5Helectron microscopy5.80BE1-201[»]
4V5YX-ray4.45BE/DE1-201[»]
4V64X-ray3.50BE/DE1-201[»]
4V65electron microscopy9.00B11-201[»]
4V66electron microscopy9.00B11-201[»]
4V69electron microscopy6.70BE1-201[»]
4V6CX-ray3.19BE/DE1-201[»]
4V6DX-ray3.81BE/DE1-201[»]
4V6EX-ray3.71BE/DE1-201[»]
4V6Kelectron microscopy8.25AF1-201[»]
4V6Lelectron microscopy13.20BF1-201[»]
4V6Melectron microscopy7.10BE1-201[»]
4V6Nelectron microscopy12.10AF1-201[»]
4V6Oelectron microscopy14.70BF1-201[»]
4V6Pelectron microscopy13.50BF1-201[»]
4V6Qelectron microscopy11.50BF1-201[»]
4V6Relectron microscopy11.50BF1-201[»]
4V6Selectron microscopy13.10AF1-201[»]
4V6Telectron microscopy8.30BE1-201[»]
4V6Velectron microscopy9.80BF1-201[»]
4V6Yelectron microscopy12.00BE1-201[»]
4V6Zelectron microscopy12.00BE1-201[»]
4V70electron microscopy17.00BE1-201[»]
4V71electron microscopy20.00BE1-201[»]
4V72electron microscopy13.00BE1-201[»]
4V73electron microscopy15.00BE1-201[»]
4V74electron microscopy17.00BE1-201[»]
4V75electron microscopy12.00BE1-201[»]
4V76electron microscopy17.00BE1-201[»]
4V77electron microscopy17.00BE1-201[»]
4V78electron microscopy20.00BE1-201[»]
4V79electron microscopy15.00BE1-201[»]
4V7Aelectron microscopy9.00BE1-201[»]
4V7Belectron microscopy6.80BE1-201[»]
4V7Celectron microscopy7.60BF1-201[»]
4V7Delectron microscopy7.60AF1-201[»]
4V7Ielectron microscopy9.60AE1-201[»]
4V7SX-ray3.25BE/DE1-201[»]
4V7TX-ray3.19BE/DE1-201[»]
4V7UX-ray3.10BE/DE1-201[»]
4V7VX-ray3.29BE/DE1-201[»]
4V85X-ray3.20E1-201[»]
4V89X-ray3.70BE1-201[»]
4V9CX-ray3.30BE/DE1-201[»]
4V9DX-ray3.00CE/DE1-201[»]
4V9OX-ray2.90AE/CE/EE/GE1-201[»]
4V9PX-ray2.90AE/CE/EE/GE1-201[»]
4WF1X-ray3.09BE/DE1-201[»]
4WOIX-ray3.00BE/CE1-201[»]
4WWWX-ray3.10RE/YE1-201[»]
4YBBX-ray2.10CE/DE1-201[»]
5ADYelectron microscopy4.50E1-201[»]
5AFIelectron microscopy2.90E1-201[»]
5AKAelectron microscopy5.70E1-201[»]
5GADelectron microscopy3.70E1-201[»]
5GAEelectron microscopy3.33E1-201[»]
5GAFelectron microscopy4.30E1-201[»]
5GAGelectron microscopy3.80E1-201[»]
5GAHelectron microscopy3.80E1-201[»]
5IQRelectron microscopy3.00D1-201[»]
5IT8X-ray3.12CE/DE1-201[»]
5J5BX-ray2.80CE/DE1-201[»]
5J7LX-ray3.00CE/DE1-201[»]
5J88X-ray3.32CE/DE1-201[»]
5J8AX-ray3.10CE/DE1-201[»]
5J91X-ray2.96CE/DE1-201[»]
5JC9X-ray3.03CE/DE1-201[»]
5JTEelectron microscopy3.60BE1-201[»]
5JU8electron microscopy3.60BE1-201[»]
5KCRelectron microscopy3.601F1-201[»]
5KCSelectron microscopy3.901F1-201[»]
5KPSelectron microscopy3.90D1-201[»]
5KPVelectron microscopy4.10C1-201[»]
5KPWelectron microscopy3.90C1-201[»]
5KPXelectron microscopy3.90C1-201[»]
5L3Pelectron microscopy3.70F1-201[»]
DisProtiDP00600.
ProteinModelPortaliP60723.
SMRiP60723.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261291. 50 interactors.
DIPiDIP-35791N.
IntActiP60723. 214 interactors.
MINTiMINT-1219709.
STRINGi511145.b3319.

Chemistry databases

DrugBankiDB01361. Troleandomycin.

Proteomic databases

EPDiP60723.
PaxDbiP60723.
PRIDEiP60723.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76344; AAC76344; b3319.
BAE77972; BAE77972; BAE77972.
GeneIDi5548703.
947818.
KEGGiecj:JW3281.
eco:b3319.
PATRICi32122070. VBIEscCol129921_3412.

Organism-specific databases

EchoBASEiEB0860.
EcoGeneiEG10867. rplD.

Phylogenomic databases

eggNOGiCOG0088. LUCA.
HOGENOMiHOG000248766.
InParanoidiP60723.
KOiK02926.
OMAiGVSHGPS.
PhylomeDBiP60723.

Enzyme and pathway databases

BioCyciEcoCyc:EG10867-MONOMER.
ECOL316407:JW3281-MONOMER.
MetaCyc:EG10867-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60723.
PROiP60723.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
HAMAPiMF_01328_B. Ribosomal_L4_B. 1 hit.
InterProiIPR002136. Ribosomal_L4/L1e.
IPR023574. Ribosomal_L4_dom.
IPR013005. Ribosomal_uL4/L1e.
[Graphical view]
PANTHERiPTHR10746. PTHR10746. 1 hit.
PfamiPF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
TIGRFAMsiTIGR03953. rplD_bact. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL4_ECOLI
AccessioniPrimary (citable) accession number: P60723
Secondary accession number(s): P02388, Q2M6Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The erythromycin sensitive allele is dominant over the resistant allele.

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

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.