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Database: UniProt
Entry: A0A1R1SJX1_9ACTN
LinkDB: A0A1R1SJX1_9ACTN
Original site: A0A1R1SJX1_9ACTN 
ID   A0A1R1SJX1_9ACTN        Unreviewed;       543 AA.
AC   A0A1R1SJX1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00012980};
DE            EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980};
DE   Flags: Fragment;
GN   ORFNames=SPAR_15595 {ECO:0000313|EMBL:OMI38527.1};
OS   Streptomyces sparsogenes DSM 40356.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI38527.1, ECO:0000313|Proteomes:UP000186168};
RN   [1] {ECO:0000313|EMBL:OMI38527.1, ECO:0000313|Proteomes:UP000186168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI38527.1,
RC   ECO:0000313|Proteomes:UP000186168};
RA   Coyne S., Seebeck F.P.;
RT   "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL   Submitted (MAY-2013) 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:OMI38527.1}.
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DR   EMBL; ASQP01000224; OMI38527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1SJX1; -.
DR   Proteomes; UP000186168; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01672; TMPK; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
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; SSF103473; MFS general substrate transporter; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:OMI38527.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186168};
KW   Transferase {ECO:0000313|EMBL:OMI38527.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          237..422
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   REGION          461..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OMI38527.1"
FT   NON_TER         543
FT                   /evidence="ECO:0000313|EMBL:OMI38527.1"
SQ   SEQUENCE   543 AA;  58470 MW;  3C820DCA5C10978F CRC64;
     PRRAPAPTRA APAPSRCWSW ACGAVAAAIA AAVGVAALQA ADLGGGPVGF SLLVLALTGG
     PAVGIRWAPK VLPGLSRRRL LALAIALTGL ALLVAGLVHD TTTVMLIAVV AGVSAGVAAN
     IGHTLLDQES EDSRRTRTTE HLHAVVRVLV GLGAVVAPLL AAVIGPHRLG SGDFVFAHGG
     AAFTLMLVGA LLLPVAALVL GKTDDRQGVP LRHDLREALR GADPVEAPAP TGFFIVVEGG
     DGAGKTTQVE ALAEWIRAKG HEVVVTREPG ATAIGKRLRS ILLDVSSAGI SHRAEALLYA
     ADRAEHVDTV VRPALERGAV VISDRYIDSS VAYQGAGRDL APTEIARISR WATGGLVPHL
     TVLLDVSPET ARERFTEAPD RLESEPAEFH QRVRAGFLTL AAADPARYLV VDAGQLPEAV
     TAAVRHRLDR MLPLSEAEVK AQEEARRKAE EEARRKAEEE ARRKAEEERL ERERQEALAK
     ARAEEEERKR RELEEARQRE AERQAEEARK RAEDARRRAE EERKRIEAED RARAAEEERR
     RRQ
//
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