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UniProtKB/Swiss-Prot entry Q05763


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

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Entry information
Entry name DRTS2_ARATH
Primary accession number Q05763
Secondary accession number Q0WT35
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on June 26, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 67)
Name and origin of the protein
Protein name Bifunctional dihydrofolate reductase-thymidylate synthase 2
Synonym DHFR-TS 2
Includes Dihydrofolate reductase
     (EC 1.5.1.3)
Thymidylate synthase
     (EC 2.1.1.45)
Gene name
Name: THY-2
OrderedLocusNames: At4g34570
ORFNames: T4L20.150
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Landsberg erecta;
PubMed=8374616 [NCBI, ExPASy, EBI, Israel, Japan]
Lazar G., Zhang H., Goodman H.M.;
"The origin of the bifunctional dihydrofolate reductase-thymidylate synthase isogenes of Arabidopsis thaliana.";
Plant J. 3:657-668(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-565.
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
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
L08594; AAA32789.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL023094; CAA18836.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161585; CAB80174.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK227728; BAE99713.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT003159; AAO24591.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T05277; T05277.
RefSeq NP_195183.2; -.
UniGene At.31491
3D structure databases
HSSP P04818; 1HW4. [HSSP ENTRY / PDB]
ModBase Q05763.
Organism-specific databases
TAIR At4g34570; -.
Gene expression databases
ArrayExpress Q05763; -.
GermOnline AT4G34570; Arabidopsis thaliana.
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; 1.
PS51330; DHFR_2; 1.
PS00091; THYMIDYLATE_SYNTHASE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q05763.
Genome annotation databases
GeneID 829609; -.
GenomeReviews CT486007_GR; AT4G34570.
KEGG ath:AT4G34570; -.
NMPDR fig|3702.1.peg.21530; -.
Other
ProtoNet Q05763.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; 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   565  565     Bifunctional dihydrofolate reductase-thymidylate synthase 2. PRO_0000186356
DOMAIN   65   242  178     DHFR. 
REGION   245   280  36     Hinge. 
REGION   281   565  285     Thymidylate synthase. 
ACT_SITE   447   447        By similarity. 
Sequence information
Length: 565 AA [This is the length of the unprocessed precursor] Molecular weight: 63209 Da [This is the MW of the unprocessed precursor] CRC64: C442A1402A591DD9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRCLQNSAKT LPLAFKSALL PLSQRWFCKF SPKPSSLTNI FKVSISTMAN TLNGNVIMTS 

        70         80         90        100        110        120 
KPQSTYQVVV AATKEMGIGK DGKLPWNLPT DLKFFKDLTL STSDSAKKNA VVMGRKTWES 

       130        140        150        160        170        180 
IPKKYRPLSG RLNVVLSRSS GFDIANTENV VTCSSIDSAL DLLAAPPFSL SIEKVFVIGG 

       190        200        210        220        230        240 
GDILREALNK PSCEAIHITE IDTSIDCDTF IPTVDTSAYQ PWCSSFPICE NGLRFSFTTH 

       250        260        270        280        290        300 
VRVKSSSAGE ASDESDGSKV LQVDWKKFSS VLPKMIFDRH EEYLYLNLVK EIISNGNLKD 

       310        320        330        340        350        360 
DRTGTGTLSK FGCQMKFNLR RNFPLLTTKR VFWRGVVEEL LWFISGSTNA KVLQEKGIRI 

       370        380        390        400        410        420 
WDGNASRAYL DGIGLTEREE GDLGPVYGFQ WRHFGAKYTD MHADYTGQGF DQLLDVINKI 

       430        440        450        460        470        480 
KNNPDDRRII MSAWNPSDLK LMALPPCHMF AQFYVANGEL SCQMYQRSAD MGLGVPFNIA 

       490        500        510        520        530        540 
SYSLLTCILA HVCDLVPGDF IHVIGDAHVY KNHVRPLQEQ LENPPKPFPV LKINPEKKDI 

       550        560 
DSFVADDFEL IGYDPHKKID MKMAV 

Q05763 in FASTA format

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