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Protein

Bifunctional dihydrofolate reductase-thymidylate synthase

Gene

DHFR-TS

Organism
Cryptosporidium parvum
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism.UniRule annotation

Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional dihydrofolate reductase-thymidylate synthase (DHFR-TS)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei402 – 4021UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

MethyltransferaseUniRule annotation, OxidoreductaseUniRule annotation, Transferase

Keywords - Biological processi

Nucleotide biosynthesisUniRule annotation, One-carbon metabolismUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional dihydrofolate reductase-thymidylate synthaseUniRule annotation
Gene namesi
Name:DHFR-TSImported
OrganismiCryptosporidium parvumImported
Taxonomic identifieri5807 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaCryptosporidiidaeCryptosporidium

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366489.

Interactioni

Protein-protein interaction databases

STRINGi353152.XP_625460.1.

Chemistry

BindingDBiQ27552.

Structurei

3D structure databases

ProteinModelPortaliQ27552.
SMRiQ27552. Positions 3-521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27552.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 177173DHFR (dihydrofolate reductase)InterPro annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the thymidylate synthase family.UniRule annotation
In the N-terminal section; belongs to the dihydrofolate reductase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG410K5TU. Eukaryota.
KOG0673. Eukaryota.
KOG1324. Eukaryota.
COG0207. LUCA.
COG0262. LUCA.

Family and domain databases

Gene3Di3.30.572.10. 2 hits.
3.40.430.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact.
InterProiIPR024072. DHFR-like_dom.
IPR012262. DHFR-TS.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF000389. DHFR-TS. 1 hit.
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27552-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKNVSIVV AASVLSSGIG INGQLPWSIS EDLKFFSKIT NNKCDSNKKN
60 70 80 90 100
ALIMGRKTWD SIGRRPLKNR IIVVISSSLP QDEADPNVVV FRNLEDSIEN
110 120 130 140 150
LMNDDSIENI FVCGGESIYR DALKDNFVDR IYLTRVALED IEFDTYFPEI
160 170 180 190 200
PETFLPVYMS QTFCTKNISY DFMIFEKQEK KTLQNCDPAR GQLKSIDDTV
210 220 230 240 250
DLLGEIFGIR KMGNRHKFPK EEIYNTPSIR FGREHYEFQY LDLLSRVLEN
260 270 280 290 300
GAYRENRTGI STYSIFGQMM RFDMRESFPL LTTKKVAIRS IFEELIWFIK
310 320 330 340 350
GDTNGNHLIE KKVYIWSGNG SKEYLERIGL GHREENDLGP IYGFQWRHYN
360 370 380 390 400
GEYKTMHDDY TGVGVDQLAK LIETLKNNPK DRRHILTAWN PSALSQMALP
410 420 430 440 450
PCHVLSQYYV TNDNCLSCNL YQRSCDLGLG SPFNIASYAI LTMMLAQVCG
460 470 480 490 500
YEPGELAIFI GDAHIYENHL TQLKEQLSRT PRPFPQLKFK RKVENIEDFK
510 520
WEDIELIGYY PYPTIKMDMA V
Length:521
Mass (Da):60,192
Last modified:November 1, 1996 - v1
Checksum:i4AFFEEA5C2A9B8E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41366 Genomic DNA. Translation: AAC47230.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41366 Genomic DNA. Translation: AAC47230.1.

3D structure databases

ProteinModelPortaliQ27552.
SMRiQ27552. Positions 3-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi353152.XP_625460.1.

Chemistry

BindingDBiQ27552.
ChEMBLiCHEMBL2366489.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410K5TU. Eukaryota.
KOG0673. Eukaryota.
KOG1324. Eukaryota.
COG0207. LUCA.
COG0262. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Miscellaneous databases

EvolutionaryTraceiQ27552.

Family and domain databases

Gene3Di3.30.572.10. 2 hits.
3.40.430.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact.
InterProiIPR024072. DHFR-like_dom.
IPR012262. DHFR-TS.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF000389. DHFR-TS. 1 hit.
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Potential antifolate resistance determinants and genotypic variation in the bifunctional dihydrofolate reductase-thymidylate synthase gene from human and bovine isolates of Cryptosporidium parvum."
    Vasquez J.R., Gooze L., Kim K., Gut J., Petersen C., Nelson R.G.
    Mol. Biochem. Parasitol. 79:153-165(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ27552_CRYPV
AccessioniPrimary (citable) accession number: Q27552
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: March 16, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.