ID C6LNR8_GIAIB Unreviewed; 390 AA.
AC C6LNR8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 22-FEB-2023, entry version 44.
DE RecName: Full=thymidine kinase {ECO:0000256|ARBA:ARBA00012118};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118};
GN ORFNames=GL50581_373 {ECO:0000313|EMBL:EET02334.1};
OS Giardia intestinalis (strain ATCC 50581 / GS clone H7) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=598745 {ECO:0000313|EMBL:EET02334.1, ECO:0000313|Proteomes:UP000002488};
RN [1] {ECO:0000313|EMBL:EET02334.1, ECO:0000313|Proteomes:UP000002488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50581 / GS clone H7 {ECO:0000313|Proteomes:UP000002488};
RX PubMed=19696920; DOI=10.1371/journal.ppat.1000560;
RA Franzen O., Jerlstrom-Hultqvist J., Castro E., Sherwood E., Ankarklev J.,
RA Reiner D.S., Palm D., Andersson J.O., Andersson B., Svard S.G.;
RT "Draft genome sequencing of giardia intestinalis assemblage B isolate GS:
RT is human giardiasis caused by two different species?";
RL PLoS Pathog. 5:E1000560-E1000560(2009).
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:EET02334.1}.
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DR EMBL; ACGJ01000532; EET02334.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LNR8; -.
DR EnsemblProtists; EET02334; EET02334; GL50581_373.
DR VEuPathDB; GiardiaDB:GL50581_373; -.
DR OMA; LTTHDNT; -.
DR OrthoDB; 674053at2759; -.
DR Proteomes; UP000002488; 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 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 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EET02334.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 390 AA; 42526 MW; 5E114293211AA10A CRC64;
MNSLTLILGP MFAGKSTELV GIHSRLIAAH KRVLVVKHTF DTRYNDNFLT THDNTKISAK
QATLLGEFTG EFDNYDALIV DEGQFFADIV TAVQCALSKG LYVYISALSG NFKREPFEVI
PQLFPLASAI YLRSAICAIC HAPAPFSARF SAQTEEIVIG GAEMYAPTCR TCWKSIAHQR
AIKQAKQLTD SEVKSFISDA AAILEGSALL GSKLLLIPAI ASPLDTELQC VYASASSAGQ
NLLVIAQQES QELNEAAETF GFTLRYFDSL AQSETEHVIS DSVRQVVDTH AIVLVYCADF
YEHADVILDE CVFQGKVVIA ATSTKISLQL LGSFLSHADI VSFSSLTRNT DEDPEKLNNS
KASTGMPRFF KTCLAGLSLE KLMLGTHEDL
//
