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Database: UniProt
Entry: A0A0Q8LUC0_9MICO
LinkDB: A0A0Q8LUC0_9MICO
Original site: A0A0Q8LUC0_9MICO 
ID   A0A0Q8LUC0_9MICO        Unreviewed;       219 AA.
AC   A0A0Q8LUC0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=ASD93_02345 {ECO:0000313|EMBL:KRB38801.1};
OS   Microbacterium sp. Root180.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB38801.1, ECO:0000313|Proteomes:UP000050802};
RN   [1] {ECO:0000313|EMBL:KRB38801.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB38801.1,
RC   ECO:0000313|Proteomes:UP000050802};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB38801.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB38801.1,
RC   ECO:0000313|Proteomes:UP000050802};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRB38801.1}.
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DR   EMBL; LMHS01000001; KRB38801.1; -; Genomic_DNA.
DR   RefSeq; WP_056118171.1; NZ_LMHS01000001.1.
DR   AlphaFoldDB; A0A0Q8LUC0; -.
DR   STRING; 1736483.ASD93_02345; -.
DR   OrthoDB; 9781579at2; -.
DR   Proteomes; UP000050802; 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; 3.40.50.300; 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; 2.
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:UP000050802};
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   219 AA;  24233 MW;  D89EFC9C029170F2 CRC64;
     MAKLYFRYGA MNSGKSTSLL QAAYNYEERG QHVLLAKPEI DTKGADQISS RLGVERTVDF
     LIPPGADLRA LFAEHRAKVQ ERAEDALIPE SSATGAAPDV ACLMIDEAQF LTREQVDDLL
     RIVVLDRIPV LAYGIRTDFQ TQAFPGSRRL LELAHSLEEL KTICRCGRKA LFNARLVGGR
     FVFDGDQVAI DELSTARVTY ESMCAECYLR ESGGRIGAN
//
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