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Protein

Outer membrane protein TolC

Gene

tolC

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

Functioni

Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.5 Publications

Enzyme regulationi

In vitro, inhibited by hexaamminecobalt3+.1 Publication

GO - Molecular functioni

  • efflux transmembrane transporter activity Source: EcoCyc
  • identical protein binding Source: IntAct
  • porin activity Source: EcoCyc

GO - Biological processi

  • enterobactin transport Source: EcoliWiki
  • response to antibiotic Source: UniProtKB-KW
  • response to organic cyclic compound Source: EcoliWiki
  • transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Enzyme and pathway databases

BioCyciEcoCyc:EG11009-MONOMER.
ECOL316407:JW5503-MONOMER.
MetaCyc:EG11009-MONOMER.

Protein family/group databases

TCDBi1.B.17.1.1. the outer membrane factor (omf) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Outer membrane protein TolC
Alternative name(s):
Multidrug efflux pump subunit TolC
Outer membrane factor TolC
Gene namesi
Name:tolC
Synonyms:colE1-i, mtcB, mukA, refI, toc, weeA
Ordered Locus Names:b3035, JW5503
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11009. tolC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 6240PeriplasmicAdd
BLAST
Transmembranei63 – 7412Beta stranded; Name=S1Add
BLAST
Topological domaini75 – 828Extracellular
Transmembranei83 – 9614Beta stranded; Name=S2Add
BLAST
Topological domaini97 – 268172PeriplasmicAdd
BLAST
Transmembranei269 – 27911Beta stranded; Name=S4Add
BLAST
Topological domaini280 – 30021ExtracellularAdd
BLAST
Transmembranei301 – 31111Beta stranded; Name=S5Add
BLAST
Topological domaini312 – 493182PeriplasmicAdd
BLAST

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cannot grow on efflux substrates novobiocin or fusidic acid.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi384 – 3841Y → F: Partial channel opening. Increases sensitivity to vancomycin, by allowing its passive diffusion across the outer membrane; when associated with E-389. 1 Publication
Mutagenesisi389 – 3891R → E: Partial channel opening. Increases sensitivity to vancomycin, by allowing its passive diffusion across the outer membrane; when associated with F-382. 1 Publication
Mutagenesisi393 – 3931D → A: Decreases inhibition by hexaamminecobalt(3+). 1 Publication
Mutagenesisi396 – 3961D → A: Decreases inhibition by hexaamminecobalt(3+). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22223 PublicationsAdd
BLAST
Chaini23 – 493471Outer membrane protein TolCPRO_0000013352Add
BLAST

Proteomic databases

EPDiP02930.
PaxDbiP02930.

2D gel databases

SWISS-2DPAGEP02930.

Interactioni

Subunit structurei

Homotrimer. Part of tripartite efflux systems, which are composed of an inner membrane transporter, a periplasmic membrane fusion protein, and an outer membrane component, TolC. The complexes form a large protein conduit and can translocate molecules across both the inner and outer membranes. TolC interacts with the membrane fusion proteins AcrA, EmrA and MacA.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-875614,EBI-875614

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4263248. 380 interactions.
DIPiDIP-11007N.
IntActiP02930. 5 interactions.
STRINGi511145.b3035.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 3511Combined sources
Helixi37 – 5721Combined sources
Helixi58 – 603Combined sources
Beta strandi63 – 7513Combined sources
Beta strandi77 – 793Combined sources
Beta strandi83 – 9816Combined sources
Helixi100 – 16768Combined sources
Beta strandi168 – 1703Combined sources
Helixi173 – 20836Combined sources
Beta strandi213 – 2186Combined sources
Turni220 – 2223Combined sources
Helixi231 – 24111Combined sources
Helixi243 – 26321Combined sources
Helixi264 – 2663Combined sources
Beta strandi269 – 27911Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi288 – 2914Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi302 – 31615Combined sources
Helixi319 – 38567Combined sources
Beta strandi386 – 3883Combined sources
Helixi391 – 42636Combined sources
Helixi431 – 4399Combined sources
Beta strandi441 – 4488Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EK9X-ray2.10A/B/C23-450[»]
1TQQX-ray2.75A/B/C23-493[»]
2VDDX-ray3.30A/B/C1-450[»]
2VDEX-ray3.20A/B/C1-450[»]
2WMZX-ray2.90A/B/C23-450[»]
2XMNX-ray2.85A/B/C23-450[»]
ProteinModelPortaliP02930.
SMRiP02930. Positions 23-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02930.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati23 – 2302081Add
BLAST
Repeati231 – 4462162Add
BLAST

Domaini

Forms a continuous, solvent-accessible conduit: a 'channel-tunnel' over 140 Angstroms long that spans both the outer membrane and periplasmic space. The periplasmic or proximal end of the tunnel is sealed by sets of coiled helices.1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4105DFG. Bacteria.
COG1538. LUCA.
HOGENOMiHOG000283506.
InParanoidiP02930.
KOiK12340.
OMAiAMSQAEN.
OrthoDBiEOG6JHRGC.
PhylomeDBiP02930.

Family and domain databases

InterProiIPR003423. OMP_efflux.
IPR010130. T1SS_OMP_TolC.
[Graphical view]
PANTHERiPTHR30026:SF3. PTHR30026:SF3. 1 hit.
PfamiPF02321. OEP. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01844. type_I_sec_TolC. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P02930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLLPILIG LSLSGFSSLS QAENLMQVYQ QARLSNPELR KSAADRDAAF
60 70 80 90 100
EKINEARSPL LPQLGLGADY TYSNGYRDAN GINSNATSAS LQLTQSIFDM
110 120 130 140 150
SKWRALTLQE KAAGIQDVTY QTDQQTLILN TATAYFNVLN AIDVLSYTQA
160 170 180 190 200
QKEAIYRQLD QTTQRFNVGL VAITDVQNAR AQYDTVLANE VTARNNLDNA
210 220 230 240 250
VEQLRQITGN YYPELAALNV ENFKTDKPQP VNALLKEAEK RNLSLLQARL
260 270 280 290 300
SQDLAREQIR QAQDGHLPTL DLTASTGISD TSYSGSKTRG AAGTQYDDSN
310 320 330 340 350
MGQNKVGLSF SLPIYQGGMV NSQVKQAQYN FVGASEQLES AHRSVVQTVR
360 370 380 390 400
SSFNNINASI SSINAYKQAV VSAQSSLDAM EAGYSVGTRT IVDVLDATTT
410 420 430 440 450
LYNAKQELAN ARYNYLINQL NIKSALGTLN EQDLLALNNA LSKPVSTNPE
460 470 480 490
NVAPQTPEQN AIADGYAPDS PAPVVQQTSA RTTTSNGHNP FRN
Length:493
Mass (Da):53,741
Last modified:June 27, 2006 - v3
Checksum:i6F97B4C62A848FE1
GO

Sequence cautioni

The sequence AAA69203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA24751.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA37982.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781N → K in CAA24914 (PubMed:6312426).Curated
Sequence conflicti191 – 1911V → L in CAA37982 (PubMed:2216730).Curated
Sequence conflicti203 – 2042QL → HV in CAA24914 (PubMed:6312426).Curated
Sequence conflicti214 – 2152EL → GT in CAA24914 (PubMed:6312426).Curated
Sequence conflicti258 – 27013QIRQA…HLPTL → KFARRRMVTYRLW in CAA24914 (PubMed:6312426).CuratedAdd
BLAST
Sequence conflicti278 – 29518ISDTS…AAGTQ → FLTPLIAVRKPCAAVP in CAA24914 (PubMed:6312426).CuratedAdd
BLAST
Sequence conflicti325 – 3251K → T in CAA24914 (PubMed:6312426).Curated
Sequence conflicti335 – 35420SEQLE…RSSFN → ASTWKVPIVASCQRAFCFS in CAA24914 (PubMed:6312426).CuratedAdd
BLAST
Sequence conflicti365 – 3706AYKQAV → RYTQAA in CAA24914 (PubMed:6312426).Curated
Sequence conflicti400 – 41112TLYNA…ELANA → SCTAQARAGNP in CAA24914 (PubMed:6312426).CuratedAdd
BLAST
Sequence conflicti445 – 4451V → I in CAA24914 (PubMed:6312426).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00016 Genomic DNA. Translation: CAA24914.1.
X54049 Genomic DNA. Translation: CAA37982.1. Different initiation.
U28377 Genomic DNA. Translation: AAA69203.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76071.2.
AP009048 Genomic DNA. Translation: BAE77091.1.
V01505 Genomic DNA. Translation: CAA24751.1. Different initiation.
PIRiA65091. MMECTC.
RefSeqiNP_417507.2. NC_000913.3.
WP_000735278.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76071; AAC76071; b3035.
BAE77091; BAE77091; BAE77091.
GeneIDi947521.
KEGGiecj:JW5503.
eco:b3035.
PATRICi32121480. VBIEscCol129921_3127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00016 Genomic DNA. Translation: CAA24914.1.
X54049 Genomic DNA. Translation: CAA37982.1. Different initiation.
U28377 Genomic DNA. Translation: AAA69203.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76071.2.
AP009048 Genomic DNA. Translation: BAE77091.1.
V01505 Genomic DNA. Translation: CAA24751.1. Different initiation.
PIRiA65091. MMECTC.
RefSeqiNP_417507.2. NC_000913.3.
WP_000735278.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EK9X-ray2.10A/B/C23-450[»]
1TQQX-ray2.75A/B/C23-493[»]
2VDDX-ray3.30A/B/C1-450[»]
2VDEX-ray3.20A/B/C1-450[»]
2WMZX-ray2.90A/B/C23-450[»]
2XMNX-ray2.85A/B/C23-450[»]
ProteinModelPortaliP02930.
SMRiP02930. Positions 23-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263248. 380 interactions.
DIPiDIP-11007N.
IntActiP02930. 5 interactions.
STRINGi511145.b3035.

Protein family/group databases

TCDBi1.B.17.1.1. the outer membrane factor (omf) family.

2D gel databases

SWISS-2DPAGEP02930.

Proteomic databases

EPDiP02930.
PaxDbiP02930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76071; AAC76071; b3035.
BAE77091; BAE77091; BAE77091.
GeneIDi947521.
KEGGiecj:JW5503.
eco:b3035.
PATRICi32121480. VBIEscCol129921_3127.

Organism-specific databases

EchoBASEiEB1002.
EcoGeneiEG11009. tolC.

Phylogenomic databases

eggNOGiENOG4105DFG. Bacteria.
COG1538. LUCA.
HOGENOMiHOG000283506.
InParanoidiP02930.
KOiK12340.
OMAiAMSQAEN.
OrthoDBiEOG6JHRGC.
PhylomeDBiP02930.

Enzyme and pathway databases

BioCyciEcoCyc:EG11009-MONOMER.
ECOL316407:JW5503-MONOMER.
MetaCyc:EG11009-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP02930.
PROiP02930.

Family and domain databases

InterProiIPR003423. OMP_efflux.
IPR010130. T1SS_OMP_TolC.
[Graphical view]
PANTHERiPTHR30026:SF3. PTHR30026:SF3. 1 hit.
PfamiPF02321. OEP. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01844. type_I_sec_TolC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the tolC gene that codes for an outer membrane protein of Escherichia coli K12."
    Hackett J., Reeves P.
    Nucleic Acids Res. 11:6487-6495(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the tolC gene of Escherichia coli."
    Niki H., Imamura R., Ogura T., Hiraga S.
    Nucleic Acids Res. 18:5547-5547(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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. "The TolC protein of Escherichia coli K12 is synthesised in a precursor form."
    Hackett J., Misra R., Reeves P.
    FEBS Lett. 156:307-310(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
    Strain: K12.
  6. "Identification and characterization of the TolC protein, an outer membrane protein from Escherichia coli."
    Morona R., Manning P.A., Reeves P.
    J. Bacteriol. 153:693-699(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-34, FUNCTION, SUBCELLULAR LOCATION.
    Strain: K12.
  7. "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 23-34.
    Strain: K12 / EMG2.
  8. "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
    Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.
    Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-27.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  9. "Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals."
    Koronakis V., Li J., Koronakis E., Stauffer K.
    Mol. Microbiol. 23:617-626(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  10. "Suppression of hypersensitivity of Escherichia coli acrB mutant to organic solvents by integrational activation of the acrEF operon with the IS1 or IS2 element."
    Kobayashi K., Tsukagoshi N., Aono R.
    J. Bacteriol. 183:2646-2653(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACREF-TOLC EFFLUX SYSTEM.
  11. "Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system."
    Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.
    Mol. Microbiol. 53:697-706(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACRAB-TOLC EFFLUX SYSTEM, INTERACTION WITH ACRA, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  12. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    Strain: BL21-DE3.
  13. "MacB ABC transporter is a dimer whose ATPase activity and macrolide-binding capacity are regulated by the membrane fusion protein MacA."
    Lin H.T., Bavro V.N., Barrera N.P., Frankish H.M., Velamakanni S., van Veen H.W., Robinson C.V., Borges-Walmsley M.I., Walmsley A.R.
    J. Biol. Chem. 284:1145-1154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MACAB-TOLC EFFLUX SYSTEM, SUBUNIT, INTERACTION WITH MACA.
  14. "The assembled structure of a complete tripartite bacterial multidrug efflux pump."
    Symmons M.F., Bokma E., Koronakis E., Hughes C., Koronakis V.
    Proc. Natl. Acad. Sci. U.S.A. 106:7173-7178(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  15. Cited for: INTERACTION WITH ACRA; EMRA AND MACA.
  16. "Functional implications of an intermeshing cogwheel-like interaction between TolC and MacA in the action of macrolide-specific efflux pump MacAB-TolC."
    Xu Y., Song S., Moeller A., Kim N., Piao S., Sim S.H., Kang M., Yu W., Cho H.S., Chang I., Lee K., Ha N.C.
    J. Biol. Chem. 286:13541-13549(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MACA.
  17. "Membrane localization of small proteins in Escherichia coli."
    Fontaine F., Fuchs R.T., Storz G.
    J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.
  18. "Pathways of colicin import: utilization of BtuB, OmpF porin and the TolC drug-export protein."
    Zakharov S.D., Sharma O., Zhalnina M., Yamashita E., Cramer W.A.
    Biochem. Soc. Trans. 40:1463-1468(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN COLICIN E1 IMPORT.
  19. "Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export."
    Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C.
    Nature 405:914-919(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-450, DOMAIN.
  20. "Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC."
    Higgins M.K., Eswaran J., Edwards P., Schertler G.F., Hughes C., Koronakis V.
    J. Mol. Biol. 342:697-702(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 23-493 IN COMPLEX WITH HEXAAMMINECOBALT(3+), ENZYME REGULATION, MUTAGENESIS OF ASP-393 AND ASP-396.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 3-450 OF MUTANT PHE-384/GLU-389, MUTAGENESIS OF TYR-384 AND ARG-389.
  22. "Structures of sequential open states in a symmetrical opening transition of the TolC exit duct."
    Pei X.Y., Hinchliffe P., Symmons M.F., Koronakis E., Benz R., Hughes C., Koronakis V.
    Proc. Natl. Acad. Sci. U.S.A. 108:2112-2117(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 23-450 OF MUTANTS.

Entry informationi

Entry nameiTOLC_ECOLI
AccessioniPrimary (citable) accession number: P02930
Secondary accession number(s): Q2M9G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 27, 2006
Last modified: March 16, 2016
This is version 158 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. 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. 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.