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Protein
Submitted name:

Strain CBS138 chromosome J complete sequence

Gene

CAGL0J03894g

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111NADP; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei19 – 191NADP; via carbonyl oxygenCombined sources
Binding sitei98 – 981NADP; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 252NADPCombined sources
Nucleotide bindingi56 – 583NADPCombined sources
Nucleotide bindingi78 – 792NADPCombined sources
Nucleotide bindingi123 – 1297NADPCombined sources

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: InterPro
  2. NADP binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

NADPCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Strain CBS138 chromosome J complete sequenceImported
Gene namesi
Ordered Locus Names:CAGL0J03894gImported
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)Imported
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428: Chromosome J

Interactioni

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ6FPH0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6FPH0.

Family & Domainsi

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000040235.
InParanoidiQ6FPH0.
KOiK00287.
OMAiEMKYFRQ.
OrthoDBiEOG7Q8D07.

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]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 2 hits.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6FPH0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKVPVVGIV AALLPEMGIG FQGNLPWRLA KEMKYFREVT TLTNDNSKQN
60 70 80 90 100
VVIMGRKTWE SIPQKFRPLP KRINVVVSRS FDGELRKVED GIYHSNSLRN
110 120 130 140 150
CLTALQSSLA NENKIERIYI IGGGEIYRQS MDLADHWLIT KIMPLPETTI
160 170 180 190 200
PQMDTFLQKQ ELEQRFYDNS DKLVDFLPSS IQLEGRLTSQ EWNGELVKGL
210
PVQEKGYQFY FTLYTKK
Length:217
Mass (Da):25,050
Last modified:July 19, 2004 - v1
Checksum:iAF1E7DC86BB5BE80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380956 Genomic DNA. Translation: CAG60823.1.
RefSeqiXP_447874.1. XM_447874.1.

Genome annotation databases

GeneIDi2889661.
KEGGicgr:CAGL0J03894g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380956 Genomic DNA. Translation: CAG60823.1.
RefSeqiXP_447874.1. XM_447874.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ6FPH0.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ6FPH0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2889661.
KEGGicgr:CAGL0J03894g.

Phylogenomic databases

HOGENOMiHOG000040235.
InParanoidiQ6FPH0.
KOiK00287.
OMAiEMKYFRQ.
OrthoDBiEOG7Q8D07.

Miscellaneous databases

EvolutionaryTraceiQ6FPH0.

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]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 2 hits.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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-65Imported.
  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 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 NADP.

Entry informationi

Entry nameiQ6FPH0_CANGA
AccessioniPrimary (citable) accession number: Q6FPH0
Entry historyi
Integrated into UniProtKB/TrEMBL: July 19, 2004
Last sequence update: July 19, 2004
Last modified: January 7, 2015
This is version 73 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.