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UniProtKB/Swiss-Prot entry Q23695

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DRTS_CRIFA
Primary accession number Q23695
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
Name and origin of the protein
Protein name Bifunctional dihydrofolate reductase-thymidylate synthase
Synonym DHFR-TS
Includes Dihydrofolate reductase
     (EC 1.5.1.3)
Thymidylate synthase
     (EC 2.1.1.45)
Gene name None
From
Crithidia fasciculata [TaxID: 5656] 
Taxonomy Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Crithidia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0166-6851(89)90007-8; PubMed=2540436 [NCBI, ExPASy, EBI, Israel, Japan]
Hughes D.E., Shonekan O.A., Simpson L.;
"Structure, genomic organization and transcription of the bifunctional dihydrofolate reductase-thymidylate synthase gene from Crithidia fasciculata.";
Mol. Biochem. Parasitol. 34:155-166(1989).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M22852; AAA30318.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P04818; 1HW4. [HSSP ENTRY / PDB]
ModBase Q23695.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0004799; Molecular function: thymidylate synthase activity (inferred from electronic annotation from InterPro).
GO:0006231; Biological process: dTMP biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006545; Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012262; DHFR-TS.
IPR001796; DHFR_reg.
IPR000398; Thymidylat_synth_C.
Graphical view of domain structure.
Gene3D G3DSA:3.30.572.10; Thymidylat_synth_C; 1.
PANTHER PTHR11549:SF2; Thymidylat_synth_C; 1.
Pfam PF00186; DHFR_1; 1.
PF00303; Thymidylat_synt; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000389; DHFR-TS; 1.
PRINTS PR00070; DHFR.
PR00108; THYMDSNTHASE.
ProDom PD001180; Thymidylat_synth; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR03284; thym_sym; 1.
PROSITE PS00075; DHFR_1; FALSE_NEG.
PS51330; DHFR_2; 1.
PS00091; THYMIDYLATE_SYNTHASE; 1.
PROSITE graphical view of domain structure (profiles).
Other
ProtoNet Q23695.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Methyltransferase; Multifunctional enzyme; NADP; Nucleotide biosynthesis; One-carbon metabolism; Oxidoreductase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   515  515     Bifunctional dihydrofolate reductase-thymidylate synthase. PRO_0000186343
DOMAIN   26   228  203     DHFR. 
REGION   233   515  283     Thymidylate synthase. 
ACT_SITE   385   385        By similarity. 
Sequence information
Length: 515 AA [This is the length of the unprocessed precursor] Molecular weight: 58294 Da [This is the MW of the unprocessed precursor] CRC64: 8327DAB231535921 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSRAAAKFKI PMPVTKADFA FPSLRAFSIV VAADQQHGIG DGETIPWTVP ETLAFFKDQT 

        70         80         90        100        110        120 
TLLRNKKPPT EKKRNAVVMG RKTWEVPLKF RPLKGRLNVV LSCRRPVDDL LAQLPEEKRA 

       130        140        150        160        170        180 
AAAADVVING GLKEALHLLA RPPYCSSIET AYCIGGARVY TEAMQSPCVE KLKEVYLTRV 

       190        200        210        220        230        240 
HTAPTCNRFY EFVRRRRARA AVDLESTSGV KVSDAAAHLS YEIMKYVPHN AEERQYLELI 

       250        260        270        280        290        300 
DRIMKTGLVK EDRTGVGTIS LFGAQMFSLR DNQLPLLTTK RVFWRGVCEE LIWFLRGETN 

       310        320        330        340        350        360 
AHVLADKDIH IWDGNGSREF LDSRGLTENK EMDLGPVYGF QWRHFGADYK GFDANYDEGV 

       370        380        390        400        410        420 
DQIKTIVETL KTNDRRLLVT AWNPCALHKM AVRPCHLLGQ FYVNTQTKEL SCMLYQRCCD 

       430        440        450        460        470        480 
MGLGVPFNIA SYALLTILIA KATGLRPGEL VHTLGTAHVY SNHVEALKEQ LQRVPVAFPV 

       490        500        510 
LVFKKEREFL EDYESTDMEV VDYVPYPPIK MEMAV
Q23695 in FASTA format

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