ID A0A1R2ALP6_9CILI Unreviewed; 194 AA.
AC A0A1R2ALP6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN ORFNames=SteCoe_38173 {ECO:0000313|EMBL:OMJ65458.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ65458.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ65458.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ65458.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU000544};
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMJ65458.1}.
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DR EMBL; MPUH01002125; OMJ65458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2ALP6; -.
DR OrthoDB; 674053at2759; -.
DR Proteomes; UP000187209; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000544};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU000544};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000544};
KW Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ SEQUENCE 194 AA; 22262 MW; A68E6D6A37E0BDD8 CRC64;
MAETLYLRDY SIQSKNFKST TISKGEIQVI FGPMFSGKST ELLRRIRRYK IRNDSCLLLK
TKDTRYVNDD DKVVTHDEYN FLDAHSCDFL YEKLDLAMNY DVIGIDEGQF FTDIIGFSET
LANNGKTVII ACLDSDYRRE PFGNICQIIA KAEKITKLTS ICHYCKEDAA FSARITKETS
IKVIGGKDKY RPID
//
