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Q6FPH0 (Q6FPH0_CANGA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the dihydrofolate reductase family. RuleBase RU004474

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding24 – 252NADP PDB 4HOG
Nucleotide binding56 – 583NADP PDB 4HOG
Nucleotide binding78 – 792NADP PDB 4HOG
Nucleotide binding123 – 1297NADP PDB 4HOG

Sites

Binding site111NADP; via amide nitrogen and carbonyl oxygen PDB 4HOG
Binding site191NADP; via carbonyl oxygen PDB 4HOG
Binding site721Chloride 1 PDB 4HOG
Binding site971Chloride 2 PDB 3ROA PDB 4HOG
Binding site981NADP; via amide nitrogen PDB 3QLX PDB 3CSE PDB 3EEM PDB 3QLY PDB 3QLZ PDB 3ROA PDB 4HOG

Sequences

Sequence LengthMass (Da)Tools
Q6FPH0 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: AF1E7DC86BB5BE80

FASTA21725,050
        10         20         30         40         50         60 
MSKVPVVGIV AALLPEMGIG FQGNLPWRLA KEMKYFREVT TLTNDNSKQN VVIMGRKTWE 

        70         80         90        100        110        120 
SIPQKFRPLP KRINVVVSRS FDGELRKVED GIYHSNSLRN CLTALQSSLA NENKIERIYI 

       130        140        150        160        170        180 
IGGGEIYRQS MDLADHWLIT KIMPLPETTI PQMDTFLQKQ ELEQRFYDNS DKLVDFLPSS 

       190        200        210 
IQLEGRLTSQ EWNGELVKGL PVQEKGYQFY FTLYTKK 

« Hide

References

« Hide 'large scale' references
[1]"Genome evolution in yeasts."
Genolevures
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.
[2]"Structure-guided development of efficacious antifungal agents targeting Candida glabrata dihydrofolate reductase."
Liu J., Bolstad D.B., Smith A.E., Priestley N.D., Wright D.L., Anderson A.C.
Chem. Biol. 15:990-996(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH NADP.
[3]"Probing the active site of Candida glabrata dihydrofolate reductase with high resolution crystal structures and the synthesis of new inhibitors."
Liu J., Bolstad D.B., Smith A.E., Priestley N.D., Wright D.L., Anderson A.C.
Chem. Biol. Drug Des. 73:62-74(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP.
[4]"Crystal structures of Candida albicans dihydrofolate reductase bound to propargyl-linked antifolates reveal the flexibility of active site loop residues critical for ligand potency and selectivity."
Paulsen J.L., Bendel S.D., Anderson A.C.
Chem. Biol. Drug Des. 78:505-512(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH NADP.
[5]"Structural analysis of the active sites of dihydrofolate reductase from two species of Candida uncovers ligand-induced conformational changes shared among species."
Paulsen J.L., Viswanathan K., Wright D.L., Anderson A.C.
Bioorg. Med. Chem. Lett. 23:1279-1284(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 3-217 IN COMPLEX WITH CHLORIDE AND NADP.
[6]"Propargyl-linked antifolates are dual inhibitors of Candida albicans and Candida glabrata."
G-Dayanandan N., Paulsen J.L., Viswanathan K., Keshipeddy S., Lombardo M.N., Zhou W., Lamb K.M., Sochia A.E., Alverson J.B., Priestley N.D., Wright D.L., Anderson A.C.
J. Med. Chem. 57:2643-2656(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CHLORIDE AND NADP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR380956 Genomic DNA. Translation: CAG60823.1.
RefSeqXP_447874.1. XM_447874.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CSEX-ray1.60A/B1-217[»]
3EEJX-ray2.11A/B1-217[»]
3EEKX-ray2.03A/B1-217[»]
3EELX-ray1.95A/B1-217[»]
3EEMX-ray2.11A/B1-217[»]
3QLXX-ray2.24A/B1-217[»]
3QLYX-ray2.52A/B1-217[»]
3QLZX-ray1.94A/B1-217[»]
3RO9X-ray2.60A/B3-217[»]
3ROAX-ray2.30A/B3-217[»]
4H98X-ray2.90A/B4-217[»]
4HOGX-ray2.00A/B1-217[»]
ProteinModelPortalQ6FPH0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2889661.
KEGGcgr:CAGL0J03894g.

Phylogenomic databases

HOGENOMHOG000040235.
KOK00287.
OMAKEMKYFR.
OrthoDBEOG7Q8D07.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 2 hits.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ6FPH0.

Entry information

Entry nameQ6FPH0_CANGA
AccessionPrimary (citable) accession number: Q6FPH0
Entry history
Integrated into UniProtKB/TrEMBL: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)