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O62584 (TYS1_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidylate synthase 1/2

Short name=TS 1/2
Short name=TSase 1/2
EC=2.1.1.45
Gene names
Name:TS-1
Ordered Locus Names:ECU01_0180
AND
Name:TS-2
Ordered Locus Names:ECU01_1430
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00008

Sequence similarities

Belongs to the thymidylate synthase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdTMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

dTTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionthymidylate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Thymidylate synthase 1/2 HAMAP-Rule MF_00008
PRO_0000140906

Sites

Active site1741 By similarity

Experimental info

Sequence conflict341T → A in CAA06648. Ref.2

Secondary structure

........................................... 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O62584 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 5FF3C707E86C0C56

FASTA29433,112
        10         20         30         40         50         60 
MPQDPRHPEH QYLDLVKHIL ENGARRMDRT GTGTLSVFGA TMRFSLEDNT FPLLTTRRVF 

        70         80         90        100        110        120 
YRGVVEELLF FLRGETDSKV LEKKGVRIWE KNGAKQFLQS VGIDREEGDL GPIYGFQWRH 

       130        140        150        160        170        180 
FGARYETSAS SYEGKGVDQI ASAIAAIRAN PASRRIVVSA WNPTDLGSMA LPPCHVLFQF 

       190        200        210        220        230        240 
NVTDGKLSCA MYQRSGDMGL GVPFNIASYS LLTILVAHLT GLQPGEFVHF LGDAHVYLDH 

       250        260        270        280        290 
VDSLRQQIQR PPRAFPKLFV SPKGPRTEPE HFQYEDFELV GYDPHPAIKM NMSA 

« Hide

References

« Hide 'large scale' references
[1]"First report on the systematic sequencing of the small genome of Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3 kbp region on chromosome I."
Duffieux F., Peyret P., Roe B.A., Vivares C.P.
Microb. Comp. Genomics 3:1-11(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence and analysis of chromosome I of the amitochondriate intracellular parasite Encephalitozoon cuniculi (Microspora)."
Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M., Weissenbach J., Saurin W., Vivares C.P.
Genome Res. 11:198-207(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.
[3]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005644 Genomic DNA. Translation: CAA06648.1.
AL391737 Genomic DNA. Translation: CAD24888.1.
AL391737 Genomic DNA. Translation: CAD25016.1.
RefSeqXP_965853.1. XM_960760.1.
XP_965981.1. XM_960888.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KGBX-ray2.20A1-294[»]
ProteinModelPortalO62584.
SMRO62584. Positions 6-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6035.ECU01_1430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID860190.
860191.
KEGGecu:ECU01_0180.
ecu:ECU01_1430.

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHOG000257899.
KOK00560.
OMAKWARSKE.
OrthoDBEOG7X6M9G.

Enzyme and pathway databases

UniPathwayUPA00575.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF55831. SSF55831. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO62584.

Entry information

Entry nameTYS1_ENCCU
AccessionPrimary (citable) accession number: O62584
Secondary accession number(s): Q8SQI4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 31, 2004
Last modified: June 11, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways