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   24-JAN-2024, entry version 125.
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 (Social amoeba).
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.Q27564; -.
DR   PaxDb; 44689-DDB0191436; -.
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; EAYEPRC; -.
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; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR   PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//