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Database: UniProt
Entry: E9SFM8_RUMAL
LinkDB: E9SFM8_RUMAL
Original site: E9SFM8_RUMAL 
ID   E9SFM8_RUMAL            Unreviewed;       217 AA.
AC   E9SFM8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=dTMP kinase {ECO:0000313|EMBL:EGC01851.1};
DE            EC=2.7.4.9 {ECO:0000313|EMBL:EGC01851.1};
GN   ORFNames=CUS_7826 {ECO:0000313|EMBL:EGC01851.1};
OS   Ruminococcus albus 8.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC01851.1, ECO:0000313|Proteomes:UP000004259};
RN   [1] {ECO:0000313|EMBL:EGC01851.1, ECO:0000313|Proteomes:UP000004259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:EGC01851.1,
RC   ECO:0000313|Proteomes:UP000004259};
RA   Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D., Montgomery R.,
RA   Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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:EGC01851.1}.
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DR   EMBL; ADKM02000122; EGC01851.1; -; Genomic_DNA.
DR   RefSeq; WP_002852204.1; NZ_JAJFOM010000003.1.
DR   AlphaFoldDB; E9SFM8; -.
DR   STRING; 246199.CUS_7826; -.
DR   eggNOG; COG0125; Bacteria.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000004259; Unassembled WGS sequence.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
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; 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:EGC01851.1};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW   Transferase {ECO:0000313|EMBL:EGC01851.1}.
FT   DOMAIN          7..195
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
SQ   SEQUENCE   217 AA;  24804 MW;  A5CB2E1DC0E00EAD CRC64;
     MSELIVLEGL DGSGKSTQFE KLTEYLKGKD VKLKAISFPD YNDPSSTLVQ MYLNGEIAGS
     AEAVNAYAAS SFYAADRYVS YKKYWEKDHA EGSLILAARY VTSNCIYQMT KLPEEQWESY
     LEWLEDYEYE KLGLPKPTKV IFLDMPIEIS QKLLSARYDG DESKKDIHEK NIEFLYKCRS
     AALFTAKRQG WHIIECGRDG EPLSIEEIFG KIIELIG
//
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