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Protein

Dihydrofolate reductase

Gene

dfrA

Organism
Bacillus anthracis
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.UniRule annotation

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81NADP; via amide nitrogen and carbonyl oxygen
Binding sitei15 – 151NADP; via carbonyl oxygen
Binding sitei79 – 791NADPCombined sources
Metal bindingi108 – 1081Calcium; via carbonyl oxygenCombined sources
Metal bindingi110 – 1101CalciumCombined sources
Metal bindingi147 – 1471CalciumCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202NADPCombined sources
Nucleotide bindingi45 – 473NADPCombined sources
Nucleotide bindingi63 – 653NADPCombined sources
Nucleotide bindingi98 – 1014NADPCombined sources

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. NADP binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

One-carbon metabolismUniRule annotation

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources, NADPCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciANTHRA:DFRA-MONOMER.
BANT260799:GJAJ-2151-MONOMER.
BANT261594:GJ7F-2226-MONOMER.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductaseUniRule annotation (EC:1.5.1.3UniRule annotation)
Gene namesi
Name:dfrAImported
Synonyms:dfrDImported
Ordered Locus Names:BA_2237Imported, BAS2083Imported, GBAA_2237Imported
ORF Names:DH23_2166Imported, DJ42_799Imported, DJ43_1447Imported, DJ44_442Imported, DJ45_3684Imported, DJ48_2031Imported, DJ49_2771Imported, HYU01_11160Imported, NX97_15125Imported, OY21_16995Imported, OY22_09325Imported, OY23_07725Imported, OY24_16705Imported, OY25_06805Imported, OY27_10805Imported, OY28_04730Imported, OY29_19330Imported, OY30_25630Imported, OY32_19775Imported, OY34_12150Imported, OY35_10095Imported, OY36_26740Imported, OY37_23510Imported, OY38_24710Imported, OY39_08650Imported, OY40_14725Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi198094.BA_2237.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KGKNMR-A1-162[»]
2QK8X-ray2.40A1-162[»]
3DATX-ray2.30A1-162[»]
3E0BX-ray2.25A/B1-162[»]
3FL8X-ray2.29A/B/C/D/E/F/G/H1-162[»]
3FL9X-ray2.40A/B/C/D/E/F/G/H1-162[»]
3JVXX-ray2.25A/B1-162[»]
3JW3X-ray2.57A/B1-162[»]
3JW5X-ray2.89A/B1-162[»]
3JWCX-ray2.57A/B1-162[»]
3JWFX-ray2.57A/B1-162[»]
3JWKX-ray2.08A/B1-162[»]
3JWMX-ray2.57A/B1-162[»]
3S9UX-ray1.90A/B1-162[»]
3SA1X-ray2.50A/B1-162[»]
3SA2X-ray2.25A/B1-162[»]
3SAIX-ray2.25A/B1-162[»]
4ELBX-ray2.60A/B/C/D/E/F/G/H1-162[»]
4ELEX-ray2.35A/B/C/D/E/F/G/H1-162[»]
4ELFX-ray2.30A/B/C/D/E/F/G/H1-162[»]
4ELGX-ray2.10A/B/C/D/E/F/G/H1-162[»]
4ELHX-ray2.10A/B/C/D/E/F/G/H1-162[»]
ProteinModelPortaliQ81R22.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81R22.

Family & Domainsi

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.UniRule annotation

Phylogenomic databases

KOiK00287.
OMAiDNDLPWH.
OrthoDBiEOG6KT2V2.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81R22-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIVSFMVAMD ENRVIGKDNN LPWRLPSELQ YVKKTTMGHP LIMGRKNYEA
60 70 80 90 100
IGRPLPGRRN IIVTRNEGYH VEGCEVAHSV EEVFELCKNE EEIFIFGGAQ
110 120 130 140 150
IYDLFLPYVD KLYITKIHHA FEGDTFFPEM DMTNWKEVFV EKGLTDEKNP
160
YTYYYHVYEK QQ
Length:162
Mass (Da):19,125
Last modified:June 1, 2003 - v1
Checksum:i4259925DD9A1365A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP26114.1.
AE017334 Genomic DNA. Translation: AAT31357.1.
AY569129 Genomic DNA. Translation: AAT40581.1.
AE017225 Genomic DNA. Translation: AAT54397.1.
CP008846 Genomic DNA. Translation: AIF56465.1.
CP007660 Genomic DNA. Translation: AIK08291.1.
CP007618 Genomic DNA. Translation: AIK33852.1.
CP008752 Genomic DNA. Translation: AIK54032.1.
CP007704 Genomic DNA. Translation: AIK57700.1.
JNOD01000013 Genomic DNA. Translation: KFJ81276.1.
JMPV01000008 Genomic DNA. Translation: KFL65433.1.
JMPU01000016 Genomic DNA. Translation: KFL69605.1.
JTAQ01000028 Genomic DNA. Translation: KGZ46380.1.
JTAR01000041 Genomic DNA. Translation: KGZ48612.1.
JTAS01000050 Genomic DNA. Translation: KGZ52451.1.
JSZR01000024 Genomic DNA. Translation: KGZ66505.1.
JSZQ01000036 Genomic DNA. Translation: KGZ68589.1.
JSZP01000022 Genomic DNA. Translation: KGZ71566.1.
JSZT01000035 Genomic DNA. Translation: KGZ85346.1.
JSZU01000018 Genomic DNA. Translation: KGZ87656.1.
JSZW01000042 Genomic DNA. Translation: KGZ94037.1.
JSZV01000039 Genomic DNA. Translation: KGZ95202.1.
JSZY01000050 Genomic DNA. Translation: KGZ97845.1.
JTAC01000081 Genomic DNA. Translation: KHA13418.1.
JTAB01000044 Genomic DNA. Translation: KHA14048.1.
JTAA01000027 Genomic DNA. Translation: KHA14636.1.
JTAD01000041 Genomic DNA. Translation: KHA23004.1.
JTAE01000054 Genomic DNA. Translation: KHA23935.1.
JTAG01000058 Genomic DNA. Translation: KHA40924.1.
JTAF01000019 Genomic DNA. Translation: KHA42670.1.
RefSeqiNP_844628.1. NC_003997.3.
YP_018882.1. NC_007530.2.
YP_028346.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP26114; AAP26114; BA_2237.
AAT31357; AAT31357; GBAA_2237.
AAT54397; AAT54397; BAS2083.
GeneIDi1085515.
2814627.
2849969.
KEGGiban:BA_2237.
bar:GBAA_2237.
bat:BAS2083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP26114.1.
AE017334 Genomic DNA. Translation: AAT31357.1.
AY569129 Genomic DNA. Translation: AAT40581.1.
AE017225 Genomic DNA. Translation: AAT54397.1.
CP008846 Genomic DNA. Translation: AIF56465.1.
CP007660 Genomic DNA. Translation: AIK08291.1.
CP007618 Genomic DNA. Translation: AIK33852.1.
CP008752 Genomic DNA. Translation: AIK54032.1.
CP007704 Genomic DNA. Translation: AIK57700.1.
JNOD01000013 Genomic DNA. Translation: KFJ81276.1.
JMPV01000008 Genomic DNA. Translation: KFL65433.1.
JMPU01000016 Genomic DNA. Translation: KFL69605.1.
JTAQ01000028 Genomic DNA. Translation: KGZ46380.1.
JTAR01000041 Genomic DNA. Translation: KGZ48612.1.
JTAS01000050 Genomic DNA. Translation: KGZ52451.1.
JSZR01000024 Genomic DNA. Translation: KGZ66505.1.
JSZQ01000036 Genomic DNA. Translation: KGZ68589.1.
JSZP01000022 Genomic DNA. Translation: KGZ71566.1.
JSZT01000035 Genomic DNA. Translation: KGZ85346.1.
JSZU01000018 Genomic DNA. Translation: KGZ87656.1.
JSZW01000042 Genomic DNA. Translation: KGZ94037.1.
JSZV01000039 Genomic DNA. Translation: KGZ95202.1.
JSZY01000050 Genomic DNA. Translation: KGZ97845.1.
JTAC01000081 Genomic DNA. Translation: KHA13418.1.
JTAB01000044 Genomic DNA. Translation: KHA14048.1.
JTAA01000027 Genomic DNA. Translation: KHA14636.1.
JTAD01000041 Genomic DNA. Translation: KHA23004.1.
JTAE01000054 Genomic DNA. Translation: KHA23935.1.
JTAG01000058 Genomic DNA. Translation: KHA40924.1.
JTAF01000019 Genomic DNA. Translation: KHA42670.1.
RefSeqiNP_844628.1. NC_003997.3.
YP_018882.1. NC_007530.2.
YP_028346.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KGKNMR-A1-162[»]
2QK8X-ray2.40A1-162[»]
3DATX-ray2.30A1-162[»]
3E0BX-ray2.25A/B1-162[»]
3FL8X-ray2.29A/B/C/D/E/F/G/H1-162[»]
3FL9X-ray2.40A/B/C/D/E/F/G/H1-162[»]
3JVXX-ray2.25A/B1-162[»]
3JW3X-ray2.57A/B1-162[»]
3JW5X-ray2.89A/B1-162[»]
3JWCX-ray2.57A/B1-162[»]
3JWFX-ray2.57A/B1-162[»]
3JWKX-ray2.08A/B1-162[»]
3JWMX-ray2.57A/B1-162[»]
3S9UX-ray1.90A/B1-162[»]
3SA1X-ray2.50A/B1-162[»]
3SA2X-ray2.25A/B1-162[»]
3SAIX-ray2.25A/B1-162[»]
4ELBX-ray2.60A/B/C/D/E/F/G/H1-162[»]
4ELEX-ray2.35A/B/C/D/E/F/G/H1-162[»]
4ELFX-ray2.30A/B/C/D/E/F/G/H1-162[»]
4ELGX-ray2.10A/B/C/D/E/F/G/H1-162[»]
4ELHX-ray2.10A/B/C/D/E/F/G/H1-162[»]
ProteinModelPortaliQ81R22.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_2237.

Chemistry

ChEMBLiCHEMBL5270.

Protocols and materials databases

DNASUi1085515.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP26114; AAP26114; BA_2237.
AAT31357; AAT31357; GBAA_2237.
AAT54397; AAT54397; BAS2083.
GeneIDi1085515.
2814627.
2849969.
KEGGiban:BA_2237.
bar:GBAA_2237.
bat:BAS2083.

Phylogenomic databases

KOiK00287.
OMAiDNDLPWH.
OrthoDBiEOG6KT2V2.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BioCyciANTHRA:DFRA-MONOMER.
BANT260799:GJAJ-2151-MONOMER.
BANT261594:GJ7F-2226-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ81R22.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AmesImported and Ames / isolate PortonImported.
  2. "Functional cloning of Bacillus anthracis dihydrofolate reductase and confirmation of natural resistance to trimethoprim."
    Barrow E.W., Bourne P.C., Barrow W.W.
    Antimicrob. Agents Chemother. 48:4643-4649(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: SterneImported.
  3. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SterneImported.
  4. "Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase."
    Bennett B.C., Xu H., Simmerman R.F., Lee R.E., Dealwis C.G.
    J. Med. Chem. 50:4374-4381(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
  5. "Synthetic and crystallographic studies of a new inhibitor series targeting Bacillus anthracis dihydrofolate reductase."
    Beierlein J.M., Frey K.M., Bolstad D.B., Pelphrey P.M., Joska T.M., Smith A.E., Priestley N.D., Wright D.L., Anderson A.C.
    J. Med. Chem. 51:7532-7540(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH NADP.
  6. "Crystal structure of Bacillus anthracis dihydrofolate reductase with the dihydrophthalazine-based trimethoprim derivative RAB1 provides a structural explanation of potency and selectivity."
    Bourne C.R., Bunce R.A., Bourne P.C., Berlin K.D., Barrow E.W., Barrow W.W.
    Antimicrob. Agents Chemother. 53:3065-3073(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH CALCIUM.
  7. "The solution structure of Bacillus anthracis dihydrofolate reductase yields insight into the analysis of structure-activity relationships for novel inhibitors."
    Beierlein J.M., Deshmukh L., Frey K.M., Vinogradova O., Anderson A.C.
    Biochemistry 48:4100-4108(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH NADP.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames AncestorImported and Ames ancestorImported.
  9. "X-ray structure of the ternary MTX.NADPH complex of the anthrax dihydrofolate reductase: a pharmacophore for dual-site inhibitor design."
    Bennett B.C., Wan Q., Ahmad M.F., Langan P., Dealwis C.G.
    J. Struct. Biol. 166:162-171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NADP.
  10. "Mutational Studies into Trimethoprim Resistance in Bacillus anthracis Dihydrofolate Reductase."
    Beierlein J.M., Karri N.G., Anderson A.C.
    Submitted (SEP-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH NADP.
  11. Joardar V., Shrivastava S., Brinkac L.M., Harkins D.M., Durkin A.S., Sutton G.
    Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: AmesImported.
  12. "SAR studies of heterocyclic propargyl-linked TMP analogs targeting Bacillus dihydrofolate reductase."
    Anderson A.C., Beierlein J.M., Viswanathan K., Wright D.L.
    Submitted (JUN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH NADP.
  13. "SAR studies of heterocyclic propargyl-linked TMP analogs to Bacillus dihydrofolate reductase."
    Anderson A.C., Beierlein J.M., Viswanathan K., Wright D.L.
    Submitted (JUN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NADP.
  14. "Structure-Activity Studies of Heterocyclic Propargyl-linked TMP Analogs Targeting Bacillus anthracis Dihydrofolate Reductase."
    Anderson A.C., Beierlein J.M., Viswanathan K., Wright D.L.
    Submitted (JUN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP.
  15. "Structure-activity relationship for enantiomers of potent inhibitors of B. anthracis dihydrofolate reductase."
    Bourne C.R., Wakeham N., Nammalwar B., Tseitin V., Bourne P.C., Barrow E.W., Mylvaganam S., Ramnarayan K., Bunce R.A., Berlin K.D., Barrow W.W.
    Biochim. Biophys. Acta 1834:46-52(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
  16. "Complete Genome Sequence of Bacillus anthracis HYU01, Isolated from Soil Samples in the Korean Peninsula."
    Kim S.K., Chung W.H., Kim S.H., Jung K.H., Kim N., Chai Y.G.
    Genome Announc. 2:e00769-14(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: HYU01Imported.
  17. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 2000031021Imported, A.Br.003Imported, Smith 1013Imported and Zimbabwe 89Imported.
  18. "Draft Genome Sequence of Bacillus anthracis STI."
    Okinaka R.T., Challacombe J.F., Drees K., Birdsell D.N., Janke N., Naumann A., Seymour M., O'Neill H.H., Schupp J., Sahl J., Foster J.T., Pearson T., Keim P.
    Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: STI-1Imported.
  19. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BFVImported.
  20. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Delta SterneImported.
  21. "Centers for Disease Control and Prevention Bacillus anthracis whole genome sequencing."
    Hoffmaster A.R., Marston C.K., Gee J., Tiller R., Beesley C., Bell M., Elrod M., France M., Sammons S., Rodriguez-R L.M., Weigand M.R., Konstantinidis K.T.
    Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 2000031027Imported.
  22. "Centers for Disease Control and Prevention Bacillus anthracis whole genome sequencing."
    Hoffmaster A.R., Marston C.K., Gee J., Tiller R., Beesley C.A., Bell M., Elrod M., France M., Sammons S., Rodriguez-R L.M., Weigand M.R., Konstantinidis K.T.
    Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 2000031006Imported, 2000031023Imported, 2000031031Imported, 2000031038Imported, 2000031039Imported, 2000031075Imported, 2000031709Imported, 2000031765Imported, 2000032819Imported, 2000032879Imported, 2000032951Imported, 2000032967Imported, 2000032968Imported, 2000032975Imported, 2000032979Imported, 2000032989Imported and 2002013094Imported.

Entry informationi

Entry nameiQ81R22_BACAN
AccessioniPrimary (citable) accession number: Q81R22
Secondary accession number(s): E9R6R2
, E9R6R3, E9R6R4, Q68SA0, Q6HZ92, Q6KT86
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: February 4, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.