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Protein

Glucan 1,3-beta-glucosidase

Gene

XOG1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major glucan 1,3-beta-glucosidase required for cell wall integrity. Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Can also function biosynthetically as a transglycosylase. Functions to deliver glucan from the cell to the extracellular matrix. Does not appear to impact cell wall glucan content of biofilm cells, nor is it necessary for filamentation or biofilm formation. Involved in cell-substrate and cell-cell adhesion. Adhesion to host-cell surfaces is the first critical step during mucosal infection. XOG1 is target of human antimicrobial peptide LL-37 for inhibition of cell adhesion.2 Publications

Catalytic activityi

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.3 Publications

Enzyme regulationi

Binding of human antimicrobial peptide LL-37 decreases the catalytic activity, which leads to the decrease of cell adhesion.1 Publication

Kineticsi

  1. KM=23.0 mM for laminaribiose1 Publication
  2. KM=12.7 mM for laminaritriose1 Publication
  3. KM=5.0 mM for laminaritetraose1 Publication
  4. KM=2.6 mM for laminaripentaose1 Publication
  5. KM=2.7 mM for laminarihexaose1 Publication
  6. KM=2.4 mM for laminariheptaose1 Publication
  7. KM=3.9 mM for laminarin1 Publication
  8. KM=17.9 mM for pustulan1 Publication
  9. KM=260 mM for gentiobiose1 Publication
  10. KM=120 mM for gentiotriose1 Publication
  11. KM=70 mM for cellobiose1 Publication
  12. KM=9.4 mM for cellotetraose1 Publication
  13. KM=12.0 mM for cellohexaose1 Publication
  14. KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei65 – 651Substrate1 Publication
    Binding sitei67 – 671Substrate1 Publication
    Active sitei230 – 2301Proton donorBy similarity
    Binding sitei230 – 2301Substrate1 Publication
    Binding sitei293 – 2931Substrate1 Publication
    Binding sitei300 – 3001Substrate1 Publication
    Active sitei330 – 3301Nucleophile1 Publication

    GO - Molecular functioni

    • cell adhesion molecule binding Source: CGD
    • glucan exo-1,3-beta-glucosidase activity Source: CGD
    • transferase activity Source: UniProtKB-KW

    GO - Biological processi

    • cell-substrate adhesion Source: CGD
    • cellular glucan metabolic process Source: CGD
    • fungal-type cell wall organization Source: CGD
    • pathogenesis Source: UniProtKB-KW
    • single-species biofilm formation in or on host organism Source: CGD
    • single-species biofilm formation on inanimate substrate Source: CGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Transferase

    Keywords - Biological processi

    Cell adhesion, Cell wall biogenesis/degradation, Virulence

    Enzyme and pathway databases

    BRENDAi3.2.1.58. 1096.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEXG5A_CANAL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase (EC:2.4.1.-, EC:3.2.1.58)
    Alternative name(s):
    Exo-1,3-beta-glucanase
    Gene namesi
    Name:XOG1
    Synonyms:EXG, EXG1, XOG
    ORF Names:Ca49C10.05, CaO19.10507, CaO19.2990
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
    ProteomesiUP000000559 Componenti: Unassembled WGS sequence

    Subcellular locationi

    GO - Cellular componenti

    • cell surface Source: CGD
    • cell wall Source: UniProtKB-SubCell
    • extracellular region Source: CGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell wall, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Leads to enhanced susceptibility to the commonly used antifungal, fluconazole, during biofilm growth only.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi182 – 1821F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296. 1 Publication
    Mutagenesisi267 – 2671F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296 or Ser-330. 1 Publication
    Mutagenesisi296 – 2961F → A: Impairs catalytic activity; when associated with Ala-182. 1 Publication
    Mutagenesisi296 – 2961F → W or I: Decreases catalytic activity. 1 Publication
    Mutagenesisi330 – 3301E → Q: Impairs catalytic activity. 1 Publication
    Mutagenesisi330 – 3301E → S: Impairs catalytic activity; when associated with Ala-267. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Or 25Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 38172 PublicationsPRO_0000007878Add
    BLAST
    Chaini39 – 438400Glucan 1,3-beta-glucosidasePRO_0000007879Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi313 ↔ 4351 Publication
    Disulfide bondi338 ↔ 3641 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Miscellaneous databases

    PMAP-CutDBP29717.

    Expressioni

    Inductioni

    Expression is maximal during the early rapid growth phase and increases during biofilm growth. Induced by caspofungin. Transcripts is also regulated by RCK2, SIT4, and HTG4.6 Publications

    Interactioni

    Subunit structurei

    Monomer. Interacts with the human antimicrobial peptide LL-37.3 Publications

    Structurei

    Secondary structure

    1
    438
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni48 – 503Combined sources
    Beta strandi53 – 575Combined sources
    Beta strandi61 – 633Combined sources
    Turni66 – 683Combined sources
    Helixi70 – 723Combined sources
    Helixi74 – 763Combined sources
    Helixi89 – 11224Combined sources
    Helixi115 – 1239Combined sources
    Beta strandi128 – 1347Combined sources
    Helixi135 – 1373Combined sources
    Helixi150 – 16314Combined sources
    Beta strandi167 – 1748Combined sources
    Helixi183 – 1853Combined sources
    Helixi198 – 21316Combined sources
    Helixi216 – 2183Combined sources
    Turni219 – 2213Combined sources
    Beta strandi222 – 2276Combined sources
    Helixi233 – 2353Combined sources
    Helixi238 – 25417Combined sources
    Beta strandi261 – 2644Combined sources
    Turni270 – 2756Combined sources
    Helixi279 – 2813Combined sources
    Beta strandi285 – 2928Combined sources
    Helixi298 – 3014Combined sources
    Helixi305 – 32117Combined sources
    Beta strandi323 – 3319Combined sources
    Beta strandi335 – 3373Combined sources
    Turni340 – 3434Combined sources
    Helixi365 – 3673Combined sources
    Helixi370 – 3723Combined sources
    Helixi375 – 39319Combined sources
    Turni394 – 3963Combined sources
    Beta strandi397 – 4015Combined sources
    Helixi409 – 4113Combined sources
    Helixi413 – 4186Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CZ1X-ray1.85A45-438[»]
    1EQCX-ray1.85A45-438[»]
    1EQPX-ray1.90A45-438[»]
    2PB1X-ray1.90A39-438[»]
    2PBOX-ray1.85A39-438[»]
    2PC8X-ray1.80A39-438[»]
    2PF0X-ray1.90A39-438[»]
    3N9KX-ray1.70A40-438[»]
    3O6AX-ray2.00A40-438[»]
    4M80X-ray1.86A40-438[»]
    4M81X-ray1.86A40-438[»]
    4M82X-ray1.59A40-438[»]
    ProteinModelPortaliP29717.
    SMRiP29717. Positions 45-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29717.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    InParanoidiP29717.
    KOiK01210.
    OrthoDBiEOG7JT75H.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29717-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN
    60 70 80 90 100
    NVIRGVNLGG WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA
    110 120 130 140 150
    ASRILQKHWS TWITEQDFKQ ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ
    160 170 180 190 200
    VQYLEKALGW ARKNNIRVWI DLHGAPGSQN GFDNSGLRDS YNFQNGDNTQ
    210 220 230 240 250
    VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK LKQFFLDGYN
    260 270 280 290 300
    SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE
    310 320 330 340 350
    LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR
    360 370 380 390 400
    YEGAYDNAPY IGSCQPLLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF
    410 420 430
    WSWKTENAPE WSFQTLTYNG LFPQPVTDRQ FPNQCGFH
    Length:438
    Mass (Da):50,038
    Last modified:March 3, 2009 - v4
    Checksum:i9BAFEBC484B0121D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021S → L in CAA21969 (Ref. 2) Curated
    Sequence conflicti193 – 1931F → S in CAA21969 (Ref. 2) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti367 – 3671L → M in allele CaO19.10507.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X56556 Genomic DNA. Translation: CAA39908.1.
    AL033497 Genomic DNA. Translation: CAA21969.1.
    AACQ01000015 Genomic DNA. Translation: EAL02690.1.
    AACQ01000017 Genomic DNA. Translation: EAL02409.1.
    PIRiA47702.
    T52149.
    RefSeqiXP_721216.1. XM_716123.1.
    XP_721488.1. XM_716395.1.

    Genome annotation databases

    GeneIDi3636837.
    3637158.
    KEGGical:CaO19.10507.
    cal:CaO19.2990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X56556 Genomic DNA. Translation: CAA39908.1.
    AL033497 Genomic DNA. Translation: CAA21969.1.
    AACQ01000015 Genomic DNA. Translation: EAL02690.1.
    AACQ01000017 Genomic DNA. Translation: EAL02409.1.
    PIRiA47702.
    T52149.
    RefSeqiXP_721216.1. XM_716123.1.
    XP_721488.1. XM_716395.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CZ1X-ray1.85A45-438[»]
    1EQCX-ray1.85A45-438[»]
    1EQPX-ray1.90A45-438[»]
    2PB1X-ray1.90A39-438[»]
    2PBOX-ray1.85A39-438[»]
    2PC8X-ray1.80A39-438[»]
    2PF0X-ray1.90A39-438[»]
    3N9KX-ray1.70A40-438[»]
    3O6AX-ray2.00A40-438[»]
    4M80X-ray1.86A40-438[»]
    4M81X-ray1.86A40-438[»]
    4M82X-ray1.59A40-438[»]
    ProteinModelPortaliP29717.
    SMRiP29717. Positions 45-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEXG5A_CANAL.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi3636837.
    3637158.
    KEGGical:CaO19.10507.
    cal:CaO19.2990.

    Phylogenomic databases

    eggNOGiCOG2730.
    HOGENOMiHOG000114462.
    InParanoidiP29717.
    KOiK01210.
    OrthoDBiEOG7JT75H.

    Enzyme and pathway databases

    BRENDAi3.2.1.58. 1096.

    Miscellaneous databases

    EvolutionaryTraceiP29717.
    PMAP-CutDBP29717.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "An exo-beta-(1,3)-glucanase of Candida albicans: purification of the enzyme and molecular cloning of the gene."
      Chambers R.S., Broughton M.J., Cannon R.D., Carne A., Emerson G.W., Sullivan P.A.
      J. Gen. Microbiol. 139:325-334(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-73.
      Strain: ATCC 10261 / CBS 2718 / NBRC 1061.
    2. "Candida albicans strain 1161 genome pilot sequencing project."
      Taylor K., Harris D., Barrell B.G., Rajandream M.A.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE CAO19.10507).
      Strain: 1161.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.
    4. "The major exoglucanase from Candida albicans: a non-glycosylated secretory monomer related to its counterpart from Saccharomyces cerevisiae."
      Luna-Arias J.P., Analuz E., Ridruejo J.C., Olivero I., Larriba G.
      Yeast 7:833-841(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 39-73, SUBCELLULAR LOCATION, SUBUNIT.
      Strain: 3153A.
    5. "Identification of Glu-330 as the catalytic nucleophile of Candida albicans exo-beta-(1,3)-glucanase."
      MacKenzie L.F., Brooke G.S., Cutfield J.F., Sullivan P.A., Withers S.G.
      J. Biol. Chem. 272:3161-3167(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE GLU-330.
    6. "Hydrolase and transferase activities of the beta-1,3-exoglucanase of Candida albicans."
      Stubbs H.J., Brasch D.J., Emerson G.W., Sullivan P.A.
      Eur. J. Biochem. 263:889-895(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "The serine/threonine protein phosphatase SIT4 modulates yeast-to-hypha morphogenesis and virulence in Candida albicans."
      Lee C.M., Nantel A., Jiang L., Whiteway M., Shen S.H.
      Mol. Microbiol. 51:691-709(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. Cited for: INDUCTION.
    9. "Trifluoromethanesulfonic acid-based proteomic analysis of cell wall and secreted proteins of the ascomycetous fungi Neurospora crassa and Candida albicans."
      Maddi A., Bowman S.M., Free S.J.
      Fungal Genet. Biol. 46:768-781(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    10. "The MAP kinase-activated protein kinase Rck2p regulates cellular responses to cell wall stresses, filamentation and virulence in the human fungal pathogen Candida albicans."
      Li X., Du W., Zhao J., Zhang L., Zhu Z., Jiang L.
      FEMS Yeast Res. 10:441-451(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "Identification of Candida albicans exposed surface proteins in vivo by a rapid proteomic approach."
      Hernaez M.L., Ximenez-Embun P., Martinez-Gomariz M., Gutierrez-Blazquez M.D., Nombela C., Gil C.
      J. Proteomics 73:1404-1409(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    12. "Proteomic analysis of proteins released from growth-arrested Candida albicans following exposure to caspofungin."
      Kelly J., Kavanagh K.
      Med. Mycol. 48:598-605(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
    13. "Mass spectrometric analysis of the secretome of Candida albicans."
      Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.
      Yeast 27:661-672(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    14. "Effects of fluconazole on the secretome, the wall proteome, and wall integrity of the clinical fungus Candida albicans."
      Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G., de Koning L.J., Klis F.M.
      Eukaryot. Cell 10:1071-1081(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION.
    15. "Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37."
      Tsai P.W., Yang C.Y., Chang H.T., Lan C.Y.
      PLoS ONE 6:E21394-E21394(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANTIMICROBIAL PEPTIDE LL-37, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION.
    16. "A Candida biofilm-induced pathway for matrix glucan delivery: implications for drug resistance."
      Taff H.T., Nett J.E., Zarnowski R., Ross K.M., Sanchez H., Cain M.T., Hamaker J., Mitchell A.P., Andes D.R.
      PLoS Pathog. 8:E1002848-E1002848(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
    17. "Surface stress induces a conserved cell wall stress response in the pathogenic fungus Candida albicans."
      Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G., Brul S., de Koning L.J., Klis F.M.
      Eukaryot. Cell 12:254-264(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    19. "The structure of the exo-beta-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases."
      Cutfield S.M., Davies G.J., Murshudov G., Anderson B.F., Moody P.C., Sullivan P.A., Cutfield J.F.
      J. Mol. Biol. 294:771-783(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 45-438, DISULFIDE BOND, SUBSTRATE-BINDING.
    20. "Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance."
      Patrick W.M., Nakatani Y., Cutfield S.M., Sharpe M.L., Ramsay R.J., Cutfield J.F.
      FEBS J. 277:4549-4561(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 39-438 IN COMPLEX WITH SUBSTRATE, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-182; PHE-267; PHE-296 AND GLU-330.

    Entry informationi

    Entry nameiEXG1_CANAL
    AccessioniPrimary (citable) accession number: P29717
    Secondary accession number(s): Q5AI63, Q5AIZ3, Q9URL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: March 3, 2009
    Last modified: June 24, 2015
    This is version 114 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.