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Database: UniProt
Entry: Q8I4S1_PLAF7
LinkDB: Q8I4S1_PLAF7
Original site: Q8I4S1_PLAF7 
ID   Q8I4S1_PLAF7            Unreviewed;       210 AA.
AC   Q8I4S1;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   16-OCT-2019, entry version 119.
DE   SubName: Full=Thymidylate kinase {ECO:0000313|EMBL:CZT99668.1};
DE            EC=2.7.4.9 {ECO:0000313|EMBL:CZT99668.1};
GN   ORFNames=PF3D7_1251300 {ECO:0000313|EMBL:CZT99668.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT99668.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|EMBL:CZT99668.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S.,
RA   Chan M.S., Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S.,
RA   Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B.,
RA   Martin D.M., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A.,
RA   McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C.,
RA   Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W.,
RA   Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium
RT   falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0000213|PDB:2WWF, ECO:0000213|PDB:2WWG, ECO:0000213|PDB:2WWH}
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH ADP.
RX   PubMed=20353400; DOI=10.1042/BJ20091880;
RA   Whittingham J.L., Carrero-Lerida J., Brannigan J.A., Ruiz-Perez L.M.,
RA   Silva A.P., Fogg M.J., Wilkinson A.J., Gilbert I.H., Wilson K.S.,
RA   Gonzalez-Pacanowska D.;
RT   "Structural basis for the efficient phosphorylation of AZT-MP (3'-
RT   azido-3'-deoxythymidine monophosphate) and dGMP by Plasmodium
RT   falciparum type I thymidylate kinase.";
RL   Biochem. J. 428:499-509(2010).
RN   [3] {ECO:0000213|PDB:2YOF, ECO:0000213|PDB:2YOG, ECO:0000213|PDB:2YOH}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RX   PubMed=23240776; DOI=10.1021/JM301328H;
RA   Cui H., Carrero-Lerida J., Silva A.P., Whittingham J.L.,
RA   Brannigan J.A., Ruiz-Perez L.M., Read K.D., Wilson K.S.,
RA   Gonzalez-Pacanowska D., Gilbert I.H.;
RT   "Synthesis and evaluation of alpha-thymidine analogues as novel
RT   antimalarials.";
RL   J. Med. Chem. 55:10948-10957(2012).
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DR   EMBL; LN999947; CZT99668.1; -; Genomic_DNA.
DR   RefSeq; XP_001350897.1; XM_001350861.1.
DR   PDB; 2WWF; X-ray; 1.89 A; A/B/C=1-210.
DR   PDB; 2WWG; X-ray; 2.40 A; A/B/C=1-210.
DR   PDB; 2WWH; X-ray; 2.70 A; A/B/C=1-210.
DR   PDB; 2WWI; X-ray; 2.99 A; A/B/C=1-210.
DR   PDB; 2YOF; X-ray; 1.82 A; A/B/C=1-210.
DR   PDB; 2YOG; X-ray; 1.50 A; A/B=1-210.
DR   PDB; 2YOH; X-ray; 1.60 A; A/B=1-210.
DR   PDBsum; 2WWF; -.
DR   PDBsum; 2WWG; -.
DR   PDBsum; 2WWH; -.
DR   PDBsum; 2WWI; -.
DR   PDBsum; 2YOF; -.
DR   PDBsum; 2YOG; -.
DR   PDBsum; 2YOH; -.
DR   SMR; Q8I4S1; -.
DR   ChEMBL; CHEMBL2176852; -.
DR   SwissPalm; Q8I4S1; -.
DR   PRIDE; Q8I4S1; -.
DR   EnsemblProtists; CZT99668; CZT99668; PF3D7_1251300.
DR   GeneDB; PF3D7_1251300.1:pep; -.
DR   GeneID; 811545; -.
DR   KEGG; pfa:PF3D7_1251300; -.
DR   EuPathDB; PlasmoDB:PF3D7_1251300; -.
DR   KO; K00943; -.
DR   OMA; RPAEMMR; -.
DR   Reactome; R-PFA-499943; Interconversion of nucleotide di- and triphosphates.
DR   Proteomes; UP000001450; Chromosome 12.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0004798; F:thymidylate kinase activity; IDA:GeneDB.
DR   GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IDA:GeneDB.
DR   GO; GO:0006227; P:dUDP biosynthetic process; IDA:GeneDB.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:2WWF, ECO:0000213|PDB:2WWG,
KW   ECO:0000213|PDB:2WWH, ECO:0000213|PDB:2WWI};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001450};
KW   Kinase {ECO:0000313|EMBL:CZT99668.1};
KW   Nucleotide-binding {ECO:0000213|PDB:2WWF, ECO:0000213|PDB:2WWG,
KW   ECO:0000213|PDB:2WWI};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Transferase {ECO:0000313|EMBL:CZT99668.1}.
FT   DOMAIN       13    191       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      18     23       ADP. {ECO:0000213|PDB:2WWF,
FT                                ECO:0000213|PDB:2WWG, ECO:0000213|PDB:
FT                                2WWI}.
FT   BINDING     145    145       ADP. {ECO:0000213|PDB:2WWF,
FT                                ECO:0000213|PDB:2WWG, ECO:0000213|PDB:
FT                                2WWI}.
FT   BINDING     182    182       ADP; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:2WWF, ECO:0000213|PDB:
FT                                2WWG, ECO:0000213|PDB:2WWI}.
SQ   SEQUENCE   210 AA;  24691 MW;  E9329D393B685FB3 CRC64;
     MTDDKKKGKF IVFEGLDRSG KSTQSKLLVE YLKNNNVEVK HLYFPNRETG IGQIISKYLK
     MENSMSNETI HLLFSANRWE HMNEIKSLLL KGIWVVCDRY AYSGVAYSSG ALNLNKTWCM
     NPDQGLIKPD VVFYLNVPPN YAQNRSDYGE EIYEKVETQK KIYETYKHFA HEDYWINIDA
     TRKIEDIHND IVKEVTKIKV EPEEFNFLWS
//
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