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Database: UniProt
Entry: W7J6M7_9PSEU
LinkDB: W7J6M7_9PSEU
Original site: W7J6M7_9PSEU 
ID   W7J6M7_9PSEU            Unreviewed;       214 AA.
AC   W7J6M7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Thymidylate kinase {ECO:0000313|EMBL:EWC64637.1};
DE            EC=2.7.4.9 {ECO:0000313|EMBL:EWC64637.1};
GN   ORFNames=UO65_0043 {ECO:0000313|EMBL:EWC64637.1};
OS   Actinokineospora spheciospongiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC64637.1, ECO:0000313|Proteomes:UP000019277};
RN   [1] {ECO:0000313|EMBL:EWC64637.1, ECO:0000313|Proteomes:UP000019277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EG49 {ECO:0000313|EMBL:EWC64637.1,
RC   ECO:0000313|Proteomes:UP000019277};
RX   PubMed=24604655;
RA   Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA   Hentschel U.;
RT   "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT   Bacterium Actinokineospora sp. Strain EG49.";
RL   Genome Announc. 2:e00160-14(2014).
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};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776}.
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:EWC64637.1}.
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DR   EMBL; AYXG01000003; EWC64637.1; -; Genomic_DNA.
DR   RefSeq; WP_035277575.1; NZ_AYXG01000003.1.
DR   AlphaFoldDB; W7J6M7; -.
DR   STRING; 909613.UO65_0043; -.
DR   PATRIC; fig|909613.9.peg.43; -.
DR   eggNOG; COG0125; Bacteria.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000019277; Unassembled WGS sequence.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
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   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
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};
KW   Kinase {ECO:0000313|EMBL:EWC64637.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW   Transferase {ECO:0000313|EMBL:EWC64637.1}.
FT   DOMAIN          7..201
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   REGION          148..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   214 AA;  23558 MW;  6991310E4BAAA882 CRC64;
     MGRLIVIEGL DGAGKRTLAD GLTTAFTRAG ATVTGMAFPR YETSTEAKLI RDALYGELGG
     LGEEAYGMGI LYALDRHHAR EDLITALTTH DVLLLDRYVA SNAAYGAARK HEGAHGPFVE
     WVRATEIKRF GLPVPHAQLL LRVPPQLAAQ RSADRERTES TRPRDTWETD DNLQTRVGKV
     YDELAETHWL SPWHIIDGTT PTDLDTLATT LLAP
//
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