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Entry: A0A367FE24_9ACTN
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ID   A0A367FE24_9ACTN        Unreviewed;       222 AA.
AC   A0A367FE24;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165,
GN   ECO:0000313|EMBL:RCG28169.1};
GN   ORFNames=DQ384_23730 {ECO:0000313|EMBL:RCG28169.1};
OS   Sphaerisporangium album.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Sphaerisporangium.
OX   NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG28169.1, ECO:0000313|Proteomes:UP000253094};
RN   [1] {ECO:0000313|EMBL:RCG28169.1, ECO:0000313|Proteomes:UP000253094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG28169.1,
RC   ECO:0000313|Proteomes:UP000253094};
RA   Li L.;
RT   "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT   the South China Sea.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-Rule:MF_00165}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00165}.
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:RCG28169.1}.
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DR   EMBL; QOIL01000014; RCG28169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367FE24; -.
DR   OrthoDB; 4549048at2; -.
DR   Proteomes; UP000253094; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF4; THYMIDYLATE KINASE; 1.
DR   Pfam; PF02223; Thymidylate_kin; 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|HAMAP-
KW   Rule:MF_00165};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:RCG28169.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000253094};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:RCG28169.1}.
FT   DOMAIN          18..164
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
SQ   SEQUENCE   222 AA;  24390 MW;  D8681515129FBF2E CRC64;
     MTRLRPSSDH QRGLFISIDG PSSAGKSTIL AHLSQLLIAD GEQVHTTAEP STGPIGTLAR
     NLTETVSGPA LACLYSADRY HHLESEIRPR LEAGETVLCD RYVPSGLVMQ RFDGVDPAFL
     WSLNAHADRP DLAVVLEADP QTIAARLESR GAHNRFQLAP GSSHAESRFY RQACARLVQA
     GYDVLRIDCT TMAPDQLAQI IRDRLQAFFA VPELETTDAR TW
//
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