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

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

Gene

mtnN

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

Functioni

Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates.1 Publication

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine.1 Publication
S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine.1 Publication

Enzyme regulationi

Strongly inhibited by aryl-substituted MTA analogs, alkyl-substituted MTA analogs, 5'-methylthioformycin, 5'-chloroformycin, S-formycinylhomocysteine, 5'-methylthiotubercidin, S-tubercidinylhomocysteine and S-8-aza-adenosylhomocysteine. Poorly inhibited by 5'-isobutylthioinosine, 5'-n-butylthioinosine, 5'-methylthio-3-deaza-adenosine, 5'-isobutylthio-3-deaza-adenosine, S-n-6-methyl-3-deaza-adenosylhomocysteine, S-adenosylhomocysteine sulphoxide and Sinefungin.4 Publications

Kineticsi

kcat is 3.0 sec(-1) and 2.6 sec(-1) with 5'-methylthioadenosine and S-adenosylhomocysteine as substrate, respectively.1 Publication

  1. KM=0.43 µM for 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius)3 Publications
  2. KM=0.8 µM for 5'-methylthioadenosine (at pH 7 and 22 degrees Celsius)3 Publications
  3. KM=4.3 µM for S-adenosylhomocysteine (at pH 7 and 37 degrees Celsius)3 Publications
  4. KM=1.3 µM for S-adenosylhomocysteine (at pH 7 and 22 degrees Celsius)3 Publications
  1. Vmax=373 µmol/min/mg enzyme with 5'-methylthioadenosine as substrate (at pH 7 and 37 degrees Celsius)3 Publications
  2. Vmax=156 µmol/min/mg enzyme with S-adenosylhomocysteine as substrate (at pH 7 and 37 degrees Celsius)3 Publications

pH dependencei

Exhibits activity across a broad pH range. Enzyme activity is moderately improved under acidic conditions.2 Publications

Temperature dependencei

Optimum temperature is 37-45 degrees Celsius. Rapidly inactivated after exposure for 10 minutes at 55 degrees Celsius.2 Publications

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121Proton acceptor1 Publication
Binding sitei78 – 781Substrate; via amide nitrogen1 Publication
Binding sitei152 – 1521Substrate; via amide nitrogen and carbonyl oxygen1 Publication
Active sitei197 – 1971Proton donor1 Publication

GO - Molecular functioni

  • adenosylhomocysteine nucleosidase activity Source: EcoCyc
  • methylthioadenosine nucleosidase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11090-MONOMER.
ECOL316407:JW0155-MONOMER.
MetaCyc:EG11090-MONOMER.
BRENDAi3.2.2.30. 2026.
3.2.2.9. 2026.
UniPathwayiUPA00904; UER00871.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC:3.2.2.9)
Short name:
MTA/SAH nucleosidase
Short name:
MTAN
Alternative name(s):
5'-methylthioadenosine nucleosidase
Short name:
MTA nucleosidase
P46
S-adenosylhomocysteine nucleosidase
Short name:
AdoHcy nucleosidase
Short name:
SAH nucleosidase
Short name:
SRH nucleosidase
Gene namesi
Name:mtnN
Synonyms:mtn, pfs, yadA
Ordered Locus Names:b0159, JW0155
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11090. pfs.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91M → A: 13-19% of wild-type catalytic efficiency. 1 Publication
Mutagenesisi12 – 121E → A or Q: Loss of catalytic activity. 1 Publication
Mutagenesisi50 – 501I → A: 12-23% of wild-type catalytic efficiency. 1 Publication
Mutagenesisi76 – 761S → A: 13-23% of wild-type catalytic efficiency. 1 Publication
Mutagenesisi151 – 1511F → A: 0.5% of wild-type catalytic efficiency. 1 Publication
Mutagenesisi173 – 1731M → A: 0.5% of wild-type catalytic efficiency. 1 Publication
Mutagenesisi174 – 1741E → A or Q: Loss of catalytic activity. 1 Publication
Mutagenesisi193 – 1931R → A: 13-28% of wild-type catalytic efficiency. 1 Publication
Mutagenesisi196 – 1961S → A: 2-4% of wild-type catalytic efficiency. 1 Publication
Mutagenesisi197 – 1971D → A or N: Loss of catalytic activity. 1 Publication
Mutagenesisi207 – 2071F → A: 2% of wild-type catalytic efficiency. 1 Publication

Chemistry

ChEMBLiCHEMBL2866.
DrugBankiDB00173. Adenine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2322325'-methylthioadenosine/S-adenosylhomocysteine nucleosidasePRO_0000164439Add
BLAST

Proteomic databases

EPDiP0AF12.
PaxDbiP0AF12.
PRIDEiP0AF12.

2D gel databases

SWISS-2DPAGEP0AF12.

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

BioGridi4260991. 6 interactions.
DIPiDIP-10270N.
IntActiP0AF12. 7 interactions.
STRINGi511145.b0159.

Chemistry

BindingDBiP0AF12.

Structurei

Secondary structure

1
232
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi10 – 178Combined sources
Beta strandi21 – 288Combined sources
Beta strandi31 – 388Combined sources
Beta strandi41 – 477Combined sources
Helixi52 – 6615Combined sources
Beta strandi69 – 7911Combined sources
Beta strandi89 – 9911Combined sources
Helixi103 – 1053Combined sources
Beta strandi117 – 1204Combined sources
Helixi123 – 13513Combined sources
Beta strandi140 – 1478Combined sources
Helixi155 – 16410Combined sources
Beta strandi168 – 1747Combined sources
Helixi175 – 18511Combined sources
Beta strandi189 – 1979Combined sources
Helixi203 – 23129Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JYSX-ray1.90A/B1-232[»]
1NC1X-ray2.00A/B1-232[»]
1NC3X-ray2.20A/B1-232[»]
1Y6QX-ray2.20A/B1-232[»]
1Y6RX-ray2.20A/B1-232[»]
1Z5NX-ray2.10A/B1-232[»]
1Z5OX-ray2.00A/B1-232[»]
1Z5PX-ray2.00A1-232[»]
3O4VX-ray1.75A/B1-232[»]
4WKCX-ray1.64A1-232[»]
4YMLX-ray1.75A1-232[»]
ProteinModelPortaliP0AF12.
SMRiP0AF12. Positions 1-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AF12.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 1742Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
HOGENOMiHOG000259346.
InParanoidiP0AF12.
KOiK01243.
OMAiLLERCKP.
OrthoDBiEOG64JFVR.
PhylomeDBiP0AF12.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01684. Salvage_MtnN.
InterProiIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERiPTHR21234. PTHR21234. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01704. MTA/SAH-Nsdase. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AF12-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI
60 70 80 90 100
GKVAAALGAT LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA
110 120 130 140 150
DVTAFGYEYG QLPGCPAGFK ADDKLIAAAE ACIAELNLNA VRGLIVSGDA
160 170 180 190 200
FINGSVGLAK IRHNFPQAIA VEMEATAIAH VCHNFNVPFV VVRAISDVAD
210 220 230
QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG
Length:232
Mass (Da):24,354
Last modified:December 20, 2005 - v1
Checksum:i9B1FF9BEC39D4F2C
GO

Sequence cautioni

The sequence AAA23678.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 23221AVAAK…KLAHG → LLPLNSPA in AAA23678 (PubMed:2157212).CuratedAdd
BLAST
Sequence conflicti212 – 23221AVAAK…KLAHG → LLPLNSPA in AAA24322 (PubMed:2157212).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31772 Genomic DNA. Translation: AAA23678.1. Different initiation.
U24438 Genomic DNA. Translation: AAC38291.1.
M83735 Genomic DNA. Translation: AAA24322.1.
U70214 Genomic DNA. Translation: AAB08589.1.
U00096 Genomic DNA. Translation: AAC73270.1.
AP009048 Genomic DNA. Translation: BAB96736.1.
PIRiS45227.
RefSeqiNP_414701.1. NC_000913.3.
WP_000689844.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73270; AAC73270; b0159.
BAB96736; BAB96736; BAB96736.
GeneIDi948542.
KEGGiecj:JW0155.
eco:b0159.
PATRICi32115427. VBIEscCol129921_0165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31772 Genomic DNA. Translation: AAA23678.1. Different initiation.
U24438 Genomic DNA. Translation: AAC38291.1.
M83735 Genomic DNA. Translation: AAA24322.1.
U70214 Genomic DNA. Translation: AAB08589.1.
U00096 Genomic DNA. Translation: AAC73270.1.
AP009048 Genomic DNA. Translation: BAB96736.1.
PIRiS45227.
RefSeqiNP_414701.1. NC_000913.3.
WP_000689844.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JYSX-ray1.90A/B1-232[»]
1NC1X-ray2.00A/B1-232[»]
1NC3X-ray2.20A/B1-232[»]
1Y6QX-ray2.20A/B1-232[»]
1Y6RX-ray2.20A/B1-232[»]
1Z5NX-ray2.10A/B1-232[»]
1Z5OX-ray2.00A/B1-232[»]
1Z5PX-ray2.00A1-232[»]
3O4VX-ray1.75A/B1-232[»]
4WKCX-ray1.64A1-232[»]
4YMLX-ray1.75A1-232[»]
ProteinModelPortaliP0AF12.
SMRiP0AF12. Positions 1-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260991. 6 interactions.
DIPiDIP-10270N.
IntActiP0AF12. 7 interactions.
STRINGi511145.b0159.

Chemistry

BindingDBiP0AF12.
ChEMBLiCHEMBL2866.
DrugBankiDB00173. Adenine.

2D gel databases

SWISS-2DPAGEP0AF12.

Proteomic databases

EPDiP0AF12.
PaxDbiP0AF12.
PRIDEiP0AF12.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73270; AAC73270; b0159.
BAB96736; BAB96736; BAB96736.
GeneIDi948542.
KEGGiecj:JW0155.
eco:b0159.
PATRICi32115427. VBIEscCol129921_0165.

Organism-specific databases

EchoBASEiEB1082.
EcoGeneiEG11090. pfs.

Phylogenomic databases

eggNOGiENOG4105DUF. Bacteria.
COG0775. LUCA.
HOGENOMiHOG000259346.
InParanoidiP0AF12.
KOiK01243.
OMAiLLERCKP.
OrthoDBiEOG64JFVR.
PhylomeDBiP0AF12.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00871.
BioCyciEcoCyc:EG11090-MONOMER.
ECOL316407:JW0155-MONOMER.
MetaCyc:EG11090-MONOMER.
BRENDAi3.2.2.30. 2026.
3.2.2.9. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AF12.
PROiP0AF12.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01684. Salvage_MtnN.
InterProiIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERiPTHR21234. PTHR21234. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli."
    Wurgler S.M., Richardson C.C.
    Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product."
    Cornell K.A., Riscoe M.K.
    Biochim. Biophys. Acta 1396:8-14(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "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.
  7. "Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action."
    Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.
    Biochem. J. 232:335-341(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  8. "Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity."
    Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.
    Biochem. Biophys. Res. Commun. 228:724-732(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  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. "Mutational analysis of a nucleosidase involved in quorum-sensing autoinducer-2 biosynthesis."
    Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
    Biochemistry 44:11049-11057(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF MET-9; GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; ASP-197 AND PHE-207.
  11. "Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases."
    Lee J.E., Cornell K.A., Riscoe M.K., Howell P.L.
    Structure 9:941-953(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.
  12. "Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis."
    Lee J.E., Cornell K.A., Riscoe M.K., Howell P.L.
    J. Biol. Chem. 278:8761-8770(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION.
  13. "Femtomolar transition state analogue inhibitors of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli."
    Singh V., Evans G.B., Lenz D.H., Mason J.M., Clinch K., Mee S., Painter G.F., Tyler P.C., Furneaux R.H., Lee J.E., Howell P.L., Schramm V.L.
    J. Biol. Chem. 280:18265-18273(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION.
  14. "Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis."
    Lee J.E., Smith G.D., Horvatin C., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.
    J. Mol. Biol. 352:559-574(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN-197 AND GLN-12 IN COMPLEX WITH MTA SUBSTRATE OR PRODUCTS, REACTION MECHANISM, ACTIVE SITES.

Entry informationi

Entry nameiMTNN_ECOLI
AccessioniPrimary (citable) accession number: P0AF12
Secondary accession number(s): P24247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 16, 2016
This is version 98 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, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.