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Database: UniProt
Entry: A0A1Q4ZMW9_9ACTN
LinkDB: A0A1Q4ZMW9_9ACTN
Original site: A0A1Q4ZMW9_9ACTN 
ID   A0A1Q4ZMW9_9ACTN        Unreviewed;       218 AA.
AC   A0A1Q4ZMW9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   31-JUL-2019, entry version 11.
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   ORFNames=A6A29_03960 {ECO:0000313|EMBL:OKI48201.1};
OS   Streptomyces sp. TSRI0281.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI48201.1, ECO:0000313|Proteomes:UP000186952};
RN   [1] {ECO:0000313|EMBL:OKI48201.1, ECO:0000313|Proteomes:UP000186952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI48201.1,
RC   ECO:0000313|Proteomes:UP000186952};
RX   PubMed=27999165;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural
RT   Products.";
RL   MBio 7:e02104-16(2016).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-
CC       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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00165}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OKI48201.1}.
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DR   EMBL; LWLE01000001; OKI48201.1; -; Genomic_DNA.
DR   RefSeq; WP_073718478.1; NZ_LWLE01000001.1.
DR   Proteomes; UP000186952; 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   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   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186952};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:OKI48201.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186952};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN       11    165       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   REGION      196    218       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    200    218       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   218 AA;  23787 MW;  95782082801B3CBE CRC64;
     MTTPGTFVTL DGPGAVGKST TLEELDRLLR QEGRLVYRTC EPTHSALGQF TRASAAFLDG
     HALACLVAAN RYEHIENELR PMRDAGFTVI SDRYLASSLV LQRLDGVAEQ FVLDLNRRIM
     LPTLAVILTA EPSVIAARLA DRGVRHRFHH DPDAPRREVE LYAEAAETLM TLGIQVLVID
     STTTAPTDVA RRIADALPTG GSSVHSNPSR PDDHTVNP
//
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