KITH_DICDI
ID KITH_DICDI Reviewed; 227 AA.
AC Q27564; Q54HT8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Thymidine kinase 1;
DE Short=TK1;
DE EC=2.7.1.21;
DE AltName: Full=Calmodulin-binding protein ThyB;
GN Name=thyB {ECO:0000312|EMBL:AAB03673.1}; ORFNames=DDB_G0289179;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM44288.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CALMODULIN.
RX PubMed=15883042; DOI=10.1016/j.bbrc.2005.04.074;
RA O'Day D.H., Chatterjee-Chakraborty M., Wagler S., Myre M.A.;
RT "Isolation and characterization of Dictyostelium thymidine kinase 1 as a
RT calmodulin-binding protein.";
RL Biochem. Biophys. Res. Commun. 331:1494-1502(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAO64434.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=AX4 {ECO:0000269|PubMed:17448496};
RX PubMed=17448496; DOI=10.1016/j.jmb.2007.03.053;
RA Sandrini M.P.B., Soederbom F., Mikkelsen N.E., Piskur J.;
RT "Dictyostelium discoideum salvages purine deoxyribonucleosides by highly
RT specific bacterial-like deoxyribonucleoside kinases.";
RL J. Mol. Biol. 369:653-664(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AX4;
RX PubMed=8643615; DOI=10.1073/pnas.93.11.5562;
RA Kuspa A., Loomis W.F.;
RT "Ordered yeast artificial chromosome clones representing the Dictyostelium
RT discoideum genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5562-5566(1996).
RN [4] {ECO:0000305, ECO:0000312|EMBL:EAL62823.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL62823.1};
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [5] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=11923193; DOI=10.1242/dev.129.7.1543;
RA Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M.,
RA Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H.,
RA Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G.;
RT "A transcriptional profile of multicellular development in Dictyostelium
RT discoideum.";
RL Development 129:1543-1552(2002).
RN [6] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=12912885; DOI=10.1128/ec.2.4.664-670.2003;
RA Iranfar N., Fuller D., Loomis W.F.;
RT "Genome-wide expression analyses of gene regulation during early
RT development of Dictyostelium discoideum.";
RL Eukaryot. Cell 2:664-670(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000269|PubMed:17448496};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.1 uM for thymidine {ECO:0000269|PubMed:17448496};
CC -!- SUBUNIT: Interacts with calmodulin in the presence of Ca(2+).
CC {ECO:0000269|PubMed:15883042}.
CC -!- DEVELOPMENTAL STAGE: Expression levels decrease throughout development.
CC {ECO:0000269|PubMed:11923193, ECO:0000269|PubMed:12912885}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000255}.
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DR EMBL; AY192984; AAO64434.1; -; mRNA.
DR EMBL; AF510846; AAM44288.1; -; mRNA.
DR EMBL; U61990; AAB03673.1; -; mRNA.
DR EMBL; AAFI02000131; EAL62823.1; -; Genomic_DNA.
DR RefSeq; XP_636351.1; XM_631259.1.
DR AlphaFoldDB; Q27564; -.
DR SMR; Q27564; -.
DR MINT; Q27564; -.
DR STRING; 44689.DDB0191436; -.
DR PaxDb; Q27564; -.
DR EnsemblProtists; EAL62823; EAL62823; DDB_G0289179.
DR GeneID; 8627024; -.
DR KEGG; ddi:DDB_G0289179; -.
DR dictyBase; DDB_G0289179; thyB.
DR eggNOG; KOG3125; Eukaryota.
DR HOGENOM; CLU_064400_3_1_1; -.
DR InParanoid; Q27564; -.
DR OMA; GWLELIC; -.
DR PhylomeDB; Q27564; -.
DR BRENDA; 2.7.1.21; 1939.
DR Reactome; R-DDI-73614; Pyrimidine salvage.
DR SABIO-RK; Q27564; -.
DR PRO; PR:Q27564; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0005516; F:calmodulin binding; IPI:dictyBase.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IDA:dictyBase.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; DNA synthesis; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..227
FT /note="Thymidine kinase 1"
FT /id="PRO_0000293627"
FT REGION 187..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255, ECO:0000305"
FT BINDING 47..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 91..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 25494 MW; CF96E644406C0772 CRC64;
MIVTQIAGKI QVIFGPMFSG KTTELIRRIK RFNFANKKCL LIKYSKDTRY NDNIDKSFLV
THDKQNYQAF PCSILEDVKE QAQNYDVIGI DEGQFFPDVV QFSEDLANQG KTVIIAALDG
TFQRKPFQSV IDLVSKAEYI TKLTAVCMVC YNEAAFSKRI VESDDIELIG GIDKYISVCR
GCYNSDQNEG NSTKPSKTAR HSHSQSAPSV APLAVNINPD DHLNNDY
