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Protein

Beta-D-glucopyranosyl abscisate beta-glucosidase

Gene

BGLU18

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes abscisic acid glucose ester (ABA-GE) which represents the predominant form of conjugated ABA (biologically inactive). No activity with beta-D-glucopyranosyl zeatin. The hydrolysis of ABA-GE in the endoplasmic reticulum (ER) forms free ABA and contributes to increase its cellular levels under dehydration conditions. ABA-GE hydrolyzing activity is enhanced by dehydration stress-induced polymerization into higher molecular weight forms. The ABA produced by BGLU18 contributes to the initiation of intracellular signaling as well as the increase in the extracellular ABA level.2 Publications

Catalytic activityi

D-glucopyranosyl abscisate + H2O = D-glucose + abscisate.1 Publication

Kineticsi

  1. KM=0.41 mM for ABA-beta-D-glucopyranosyl ester1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581SubstrateBy similarity
Binding sitei161 – 1611SubstrateBy similarity
Binding sitei206 – 2061SubstrateBy similarity
Active sitei207 – 2071Proton donorCurated
Binding sitei351 – 3511SubstrateBy similarity
Active sitei422 – 4221NucleophileBy similarity
Binding sitei473 – 4731SubstrateBy similarity

GO - Molecular functioni

  1. abscisic acid glucose ester beta-glucosidase activity Source: TAIR
  2. beta-glucosidase activity Source: UniProtKB
  3. identical protein binding Source: TAIR

GO - Biological processi

  1. abscisic acid-activated signaling pathway Source: UniProtKB-KW
  2. abscisic acid metabolic process Source: TAIR
  3. carbohydrate metabolic process Source: InterPro
  4. defense response to fungus Source: TAIR
  5. positive regulation of abscisic acid-activated signaling pathway Source: UniProtKB
  6. protein polymerization Source: UniProtKB
  7. regulation of stomatal movement Source: UniProtKB
  8. response to abiotic stimulus Source: UniProtKB
  9. response to abscisic acid Source: UniProtKB
  10. response to insect Source: TAIR
  11. response to salt stress Source: TAIR
  12. response to water deprivation Source: TAIR
  13. water homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Abscisic acid signaling pathway

Enzyme and pathway databases

BioCyciARA:AT1G52400-MONOMER.
ARA:GQT-1542-MONOMER.
ARA:GQT-1543-MONOMER.
MetaCyc:AT1G52400-MONOMER.
BRENDAi3.2.1.175. 399.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-D-glucopyranosyl abscisate beta-glucosidase (EC:3.2.1.175)
Alternative name(s):
Beta-glucosidase 1
Short name:
AtBG1
Beta-glucosidase 18
Short name:
AtBGLU18
Beta-glucosidase homolog 1
Gene namesi
Name:BGLU18
Synonyms:BG1, BGL1
Ordered Locus Names:At1g52400
ORF Names:F19K6.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G52400.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation2 Publications
Note: Located in ER bodies.

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. endoplasmic reticulum Source: TAIR
  3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  4. ER body Source: TAIR
  5. nucleus Source: TAIR
  6. peroxisome Source: TAIR
  7. plasmodesma Source: TAIR
  8. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Reduced growth, yellow leaf, defective stomatal closure in the dark, increased transpirational water loss, sensitive response to dehydration, lower germination efficiency and decreased ABA levels.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi207 – 2071E → Q: Loss of activity towards ABA-GE. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 528502Beta-D-glucopyranosyl abscisate beta-glucosidasePRO_0000011766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi226 ↔ 237By similarity
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9SE50.
PRIDEiQ9SE50.

2D gel databases

SWISS-2DPAGEQ9SE50.

Expressioni

Tissue specificityi

Seeds and hydathodes of rosette and cauline leaves.1 Publication

Inductioni

By ABA, dehydration, wounding and salt treatment.3 Publications

Gene expression databases

ExpressionAtlasiQ9SE50. baseline and differential.
GenevestigatoriQ9SE50.

Interactioni

Protein-protein interaction databases

BioGridi26895. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9SE50.
SMRiQ9SE50. Positions 40-515.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni480 – 4812Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi525 – 5284Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiQ9SE50.
KOiK15748.
OMAiEQQPNPQ.
PhylomeDBiQ9SE50.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9SE50-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVRFEKVHLV LGLALVLTLV GAPTKAQGPV CGAGLPDKFS RLNFPEGFIW
60 70 80 90 100
GTATAAFQVE GAVNEGCRGP SMWDTFTKKF PHRCENHNAD VAVDFYHRYK
110 120 130 140 150
EDIQLMKDLN TDAFRLSIAW PRIFPHGRMS KGISKVGVQF YHDLIDELLK
160 170 180 190 200
NNIIPLVTVF HWDTPQDLED EYGGFLSGRI VQDFTEYANF TFHEYGHKVK
210 220 230 240 250
HWITFNEPWV FSRAGYDNGK KAPGRCSPYI PGYGQHCQDG RSGYEAYQVS
260 270 280 290 300
HNLLLSHAYA VDAFRNCKQC AGGKIGIAHS PAWFEPQDLE HVGGSIERVL
310 320 330 340 350
DFILGWHLAP TTYGDYPQSM KDRVGHRLPK FTEAEKKLLK GSTDYVGMNY
360 370 380 390 400
YTSVFAKEIS PDPKSPSWTT DSLVDWDSKS VDGYKIGSKP FNGKLDVYSK
410 420 430 440 450
GLRYLLKYIK DNYGDPEVII AENGYGEDLG EKHNDVNFGT QDHNRKYYIQ
460 470 480 490 500
RHLLSMHDAI CKDKVNVTGY FVWSLMDNFE WQDGYKARFG LYYIDFQNNL
510 520
TRHQKVSGKW YSEFLKPQFP TSKLREEL
Length:528
Mass (Da):60,459
Last modified:February 4, 2008 - v2
Checksum:iF148D04C0A6F27B8
GO
Isoform 2 (identifier: Q9SE50-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     461-461: C → W
     462-528: Missing.

Note: Derived from EST data. No experimental confirmation available.

Show »
Length:461
Mass (Da):52,371
Checksum:iA83D86C9F943776D
GO

Sequence cautioni

The sequence BAD94819.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341S → N in AAF22295 (Ref. 2) Curated
Sequence conflicti210 – 2101V → G in AAN60329 (Ref. 6) Curated
Sequence conflicti214 – 2141A → V in AAN60329 (Ref. 6) Curated
Sequence conflicti253 – 2531L → S in AAN31804 (Ref. 6) Curated
Sequence conflicti266 – 2661N → K in CAC19786 (PubMed:11080278).Curated
Sequence conflicti266 – 2661N → K in AAN60329 (Ref. 6) Curated
Sequence conflicti365 – 3651S → N in CAC19786 (PubMed:11080278).Curated
Sequence conflicti431 – 4311E → G in BAD94819 (Ref. 7) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei461 – 4611C → W in isoform 2. CuratedVSP_041996
Alternative sequencei462 – 52867Missing in isoform 2. CuratedVSP_041997Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ251301 mRNA. Translation: CAC19786.1.
AF183827 mRNA. Translation: AAF22295.1.
AC037424 Genomic DNA. Translation: AAG51546.1.
CP002684 Genomic DNA. Translation: AEE32799.1.
CP002684 Genomic DNA. Translation: AEE32800.1.
CP002684 Genomic DNA. Translation: AEE32801.1.
AY039855 mRNA. Translation: AAK63959.1.
AY056415 mRNA. Translation: AAL08271.1.
BT000515 mRNA. Translation: AAN18084.1.
BT000657 mRNA. Translation: AAN31804.1.
AF083771 mRNA. Translation: AAN60329.1.
AK222051 mRNA. Translation: BAD94819.1. Different initiation.
PIRiC96564.
RefSeqiNP_001031175.1. NM_001036098.2. [Q9SE50-2]
NP_001185204.1. NM_001198275.1. [Q9SE50-1]
NP_175649.1. NM_104118.2. [Q9SE50-1]
UniGeneiAt.24169.

Genome annotation databases

EnsemblPlantsiAT1G52400.1; AT1G52400.1; AT1G52400. [Q9SE50-1]
AT1G52400.3; AT1G52400.3; AT1G52400. [Q9SE50-1]
GeneIDi841670.
KEGGiath:AT1G52400.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ251301 mRNA. Translation: CAC19786.1.
AF183827 mRNA. Translation: AAF22295.1.
AC037424 Genomic DNA. Translation: AAG51546.1.
CP002684 Genomic DNA. Translation: AEE32799.1.
CP002684 Genomic DNA. Translation: AEE32800.1.
CP002684 Genomic DNA. Translation: AEE32801.1.
AY039855 mRNA. Translation: AAK63959.1.
AY056415 mRNA. Translation: AAL08271.1.
BT000515 mRNA. Translation: AAN18084.1.
BT000657 mRNA. Translation: AAN31804.1.
AF083771 mRNA. Translation: AAN60329.1.
AK222051 mRNA. Translation: BAD94819.1. Different initiation.
PIRiC96564.
RefSeqiNP_001031175.1. NM_001036098.2. [Q9SE50-2]
NP_001185204.1. NM_001198275.1. [Q9SE50-1]
NP_175649.1. NM_104118.2. [Q9SE50-1]
UniGeneiAt.24169.

3D structure databases

ProteinModelPortaliQ9SE50.
SMRiQ9SE50. Positions 40-515.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26895. 1 interaction.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

2D gel databases

SWISS-2DPAGEQ9SE50.

Proteomic databases

PaxDbiQ9SE50.
PRIDEiQ9SE50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G52400.1; AT1G52400.1; AT1G52400. [Q9SE50-1]
AT1G52400.3; AT1G52400.3; AT1G52400. [Q9SE50-1]
GeneIDi841670.
KEGGiath:AT1G52400.

Organism-specific databases

TAIRiAT1G52400.

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiQ9SE50.
KOiK15748.
OMAiEQQPNPQ.
PhylomeDBiQ9SE50.

Enzyme and pathway databases

BioCyciARA:AT1G52400-MONOMER.
ARA:GQT-1542-MONOMER.
ARA:GQT-1543-MONOMER.
MetaCyc:AT1G52400-MONOMER.
BRENDAi3.2.1.175. 399.

Gene expression databases

ExpressionAtlasiQ9SE50. baseline and differential.
GenevestigatoriQ9SE50.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Induced plant defense responses against chewing insects. Ethylene signaling reduces resistance of Arabidopsis against Egyptian cotton worm but not diamondback moth."
    Stotz H.U., Pittendrigh B.R., Kroymann J., Weniger K., Fritsche J., Bauke A., Mitchell-Olds T.
    Plant Physiol. 124:1007-1018(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: cv. Landsberg erecta.
    Tissue: Rosette leaf.
  2. "A transgenic Arabidopsis plant overexpressing an ER localized b-glucosidase homolog that is transcriptionally suppressed by NaCl is hypersensitive to NaCl stress."
    Piao H.L., Hwang I.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  6. "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells."
    Stracke R., Palme K.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-308.
  7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-528 (ISOFORM 1).
    Strain: cv. Columbia.
  8. Cited for: GENE FAMILY, NOMENCLATURE.
  9. "Activation of glucosidase via stress-induced polymerization rapidly increases active pools of abscisic acid."
    Lee K.H., Piao H.L., Kim H.-Y., Choi S.M., Jiang F., Hartung W., Hwang I., Kwak J.M., Lee I.-J., Hwang I.
    Cell 126:1109-1120(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-207.
  10. "Effect of ABA-beta-D-glucopyranosyl ester and activity of ABA-beta-D-glucosidase in Arabidopsis thaliana."
    Kato-Noguchi H., Tanaka Y.
    J. Plant Physiol. 165:788-790(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases."
    Ogasawara K., Yamada K., Christeller J.T., Kondo M., Hatsugai N., Hara-Nishimura I., Nishimura M.
    Plant Cell Physiol. 50:480-488(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  12. "The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for its formation and accumulates specific beta-glucosidases."
    Yamada K., Nagano A.J., Ogasawara K., Hara-Nishimura I., Nishimura M.
    Plant Signal. Behav. 4:849-852(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.

Entry informationi

Entry nameiBGL18_ARATH
AccessioniPrimary (citable) accession number: Q9SE50
Secondary accession number(s): F4ICX8
, Q56WI9, Q8H169, Q8H7A3, Q93V63, Q9FNZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2001
Last sequence update: February 4, 2008
Last modified: March 31, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Polymerization into higher molecular weight forms displays diurnal fluctuation, similar to the ABA level.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. 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.