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Database: UniProt
Entry: R4LFE9_9ACTN
LinkDB: R4LFE9_9ACTN
Original site: R4LFE9_9ACTN 
ID   R4LFE9_9ACTN            Unreviewed;       832 AA.
AC   R4LFE9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-NOV-2019, entry version 36.
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=L083_0470 {ECO:0000313|EMBL:AGL13980.1};
OS   Actinoplanes sp. N902-109.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes; unclassified Actinoplanes.
OX   NCBI_TaxID=649831 {ECO:0000313|EMBL:AGL13980.1, ECO:0000313|Proteomes:UP000013541};
RN   [1] {ECO:0000313|EMBL:AGL13980.1, ECO:0000313|Proteomes:UP000013541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N902-109 {ECO:0000313|EMBL:AGL13980.1,
RC   ECO:0000313|Proteomes:UP000013541};
RA   Hu H., Huang H., Lu X., Zhu B.;
RT   "Comparative analysis of rapamycin biosynthesis clusters between
RT   Streptomyces hygroscopicus ATCC 29253 and Actinoplanes sp. N902-109.";
RL   Submitted (MAY-2013) 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-
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}.
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DR   EMBL; CP005929; AGL13980.1; -; Genomic_DNA.
DR   STRING; 649831.L083_0470; -.
DR   EnsemblBacteria; AGL13980; AGL13980; L083_0470.
DR   KEGG; actn:L083_0470; -.
DR   PATRIC; fig|649831.3.peg.464; -.
DR   KO; K00943; -.
DR   Proteomes; UP000013541; Chromosome.
DR   GO; GO:0016021; C:integral component of 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: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; 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   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 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:UP000013541};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:AGL13980.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
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:UP000013541};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     21     44       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     56     77       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     89    109       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    115    135       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    156    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    196    216       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    254    273       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    285    305       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    317    336       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    342    363       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    375    400       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    420    437       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      476    665       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND     478    485       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   REGION      732    832       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    738    767       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    780    802       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   832 AA;  86632 MW;  C632A2744A5F5A0D CRC64;
     MDLTGVAALR SVLRIRPFRR LWLVLSVASF GDWIGILATA LFASQQVSGS VAQGSAFSST
     IAIRLLPALI LGPIAGVMAD RFDRRYTMVI CDILRFFVYG SIPVVALISN SGGLTVTWTV
     IATFIGETIT LMWIPAKEAA VPNLIPKGRL EASNQLSLIT TYGVTPILAA LVLAALDGVV
     RGPVGGLPTW ASPVQIALYI NALSRAATAA VVFFGIKEIS AGRRERQEKN AEQSMFRQFV
     EGWRYIGGTP FVRGLVLGIF GAFAGAGIVV GTARFFTASL GAGDAAFYLL FATLFIGLAV
     GIGAGPAIVK ELSRRRWFGV SLVLASGAVA FLSVAFHLSM ALFGALFVGA GAGMAFLAGV
     TLLGGQVNDE VRGRVFAVVQ IGARLVLLLA ISLAGLLVGL GSSRTVHLGG LHFAISSTRV
     LLLVAGLGGI WSGVTAFRQM DDKHGVPVLA DLWGAIRGRP LSPAEPFSRT GIFVVFEGGE
     GAGKSTQVTR LSEALAATGA DVVVTREPGA TDVGARIRSL VLSHGSPTDA PSPRAEALLY
     AADRAHHVAT VVRPALARGA VVISDRYVDS SLAYQGAGRT LPVQEISWLS SWATGGLKPD
     LVVLLDVDPA VGLSRVDSRG AGPDRLESES RAFHERVRYA FLDLASADPK RYLVLDAARP
     AEEIAAVVST RVNALLADGD DLHGAPDSTD APPGVDLTAP DLMDRTVVVR PGATPDETSV
     IYPAGAPVAQ RTQVIPPSSP PGISPPGVSP PGASPPGASP PGASPPGASP VEAERTQVVP
     ESERTQILSE ADLTQTLPSA DPTQVIVPAP DPTQPLPRQA GEDGDDVVGE RR
//
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