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P0CS12 (TYSY_CRYNJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 17. 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 attributes

Sequence length317 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

Subunit structure

Homodimer By similarity. 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 – 317317Thymidylate synthase HAMAP-Rule MF_00008
PRO_0000140910

Sites

Active site1871 By similarity

Secondary structure

............................................. 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CS12 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: E6322588CE1B50B2

FASTA31735,866
        10         20         30         40         50         60 
MTATIDDQEK NQRSNPDHEE YQYLDLIRRI INVGEVRPDR TGTGTVALFA PPSFRFSLAD 

        70         80         90        100        110        120 
NTLPLLTTKR VFLRGVIAEL LWFVSGCTDA KMLSSQGVGI WDGNGSKEFL EKVGLGHRRE 

       130        140        150        160        170        180 
GDLGPVYGFQ WRHFGAEYTD ADGDYKGKGV DQLQRVIDTI KNNPTDRRII LSAWNPKDLP 

       190        200        210        220        230        240 
LMALPPCHMF CQFFVSLPPA DSPGSKPKLS CLMYQRSCDL GLGVPFNIAS YALLTHMIAL 

       250        260        270        280        290        300 
ITDTEPHEFI LQMGDAHVYR DHVEPLKTQL EREPRDFPKL KWARSKEEIG DIDGFKVEDF 

       310 
VVEGYKPWGK IDMKMSA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017350 Genomic DNA. Translation: AAW45984.1.
RefSeqXP_567501.1. XM_567501.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AAZX-ray2.08A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-317[»]
ProteinModelPortalP0CS12.
SMRP0CS12. Positions 19-316.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP0CS12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAW45984; AAW45984; CNJ01230.
GeneID3254191.
KEGGcne:CNJ01230.

Phylogenomic databases

KOK00560.
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

EvolutionaryTraceP0CS12.

Entry information

Entry nameTYSY_CRYNJ
AccessionPrimary (citable) accession number: P0CS12
Secondary accession number(s): P45351, Q55KW0, Q5KAL9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: February 19, 2014
This is version 17 of the entry and version 1 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