ID A0A101UR63_9ACTN Unreviewed; 1097 AA.
AC A0A101UR63;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AQJ91_41760 {ECO:0000313|EMBL:KUO15333.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO15333.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO15333.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO15333.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) 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: 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:KUO15333.1}.
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DR EMBL; LMXB01000116; KUO15333.1; -; Genomic_DNA.
DR RefSeq; WP_067033266.1; NZ_KQ949118.1.
DR AlphaFoldDB; A0A101UR63; -.
DR STRING; 909626.AQJ91_41760; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000053260; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
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; 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; IPR011701; MFS.
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; PF07690; MFS_1; 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, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:KUO15333.1};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000053260};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 514..697
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 742..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 516..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 1097 AA; 116390 MW; D3E963B378C7C79D CRC64;
MTRAEQPTAH HPAPDDALVA DSRERAVRAL LRRPQLRRLW SAQLVGGVGD ILALLVLVLL
ALQAAIAEGS FGGGYRGVAF AVATVFGARI LATLLFGAVL LGPLTSLTSQ EGPLDRRWTM
VGADGVRAAL LIVAPLWIDW TPDDALAVLL VTVFVSGVAE RFWTVCRESA APALLPGPPP
EGATVRPLPD HMDALRRLSL RTSFVAIPVA GAVLVAAALL NNLLGTGIDW FGQHQAAFGS
YVAAGLFAAS LSVLTFLELP DTRTPRARSP LEGLRRPKTG TGVDKGRTGA IPLLVLACAA
VAAAVAAAVA VAVLHAKDLG GGPVLYGLLV LALTGGVVVG IGTASSVLPT LSRRRLLSLA
IAFTGVALLA AGLVPDVTTV LLIVALAGIG AGVAANTGHT LLDQEAEEFR RARTTEHLHA
VVRVFVALGA VIAPLVAALI GPHRLENGKF VFAHGGAAFT LMLVGALLLP VAALVLAKVD
DRSGVPLRHD LRDALLGGDD PEQAPAVSGF FIALEGGDGA GKSTQAEALA EWIRAKGHEV
VVTREPGATP VGKRLRSILL DVSSAGLSHR AEALLYAADR AEHVDTVVRP ALERGAVVIS
DRYIDSSVAY QGAGRDLSPT EIARINRWAT NGLVPHLTVL LDVSPEIARE RFTEAPDRLE
SEPAEFHARV RSGFLTLAAA DPGRYLVVDG GQEPEGVTTV VRHRLDQMLP LSEAEIRAQE
EARRKAEEEA RRKAEEEAAR KAEEERLERE RQEQLERLRA EEEERKRREL EEAQRREAER
QAEEARQRAE EARRRAEEER QRLLAEEKAR AEEEARRKVE EDRRRKQAEE EARLRAEAET
RRLEKQRKAE EALLRAEEAR RLAEQAAAAA EAGPRPPAPG AAASAEAEAA TVATPVVSLG
KGAGESVSAS ASTSASASAS AEETTVLRPV RDASAREQAS GGGGERASSG GRSAGESDAE
VTTKLPQPPA PSGAADETAV LPPVVPGAAD ETAVLPPVAP GAADETAVLP PVRGEDPSDR
VPSGFFRDEE AVRPDGAEDR TREMPQVDDE GAPRRRPRSD WAEETPLDDL PSLADELLGP
HEDEYGDEGG RGRGRRR
//
