(data stored in ACNUC7421 zone)

SWISSPROT: C6WFD0_ACTMD

ID   C6WFD0_ACTMD            Unreviewed;       710 AA.
AC   C6WFD0;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
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   OrderedLocusNames=Amir_0293 {ECO:0000313|EMBL:ACU34262.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34262.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34262.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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: ATP + dTMP = ADP + dTDP. {ECO:0000256|HAMAP-
CC       Rule:MF_00165}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP001630; ACU34262.1; -; Genomic_DNA.
DR   RefSeq; WP_012782925.1; NC_013093.1.
DR   STRING; 446462.Amir_0293; -.
DR   EnsemblBacteria; ACU34262; ACU34262; Amir_0293.
DR   KEGG; ami:Amir_0293; -.
DR   eggNOG; ENOG4108ZMD; Bacteria.
DR   eggNOG; COG0125; LUCA.
DR   HOGENOM; HOG000022435; -.
DR   KO; K00943; -.
DR   OMA; DRRWTMV; -.
DR   OrthoDB; POG091H02B9; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd06174; MFS; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   InterPro; IPR010290; TM_effector.
DR   Pfam; PF05977; MFS_3; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WFD0.
DR   SWISS-2DPAGE; C6WFD0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     41     63       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     75     95       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    169    192       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    204    227       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    266    288       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    300    320       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    332    350       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    356    378       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    390    416       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    436    455       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   710 AA;  74963 MW;  C580B64640D09A83 CRC64;
     MSTIQDSDTA GGPGRSGSNR TEASTGHRIR SVLAIRPFRR LWGVTYLCSV GDWLSLLALT
     GLVTKLAEGY RWEGFALSAV VITQLLPGML FAPLGGVLAD RFDRRKVMVA CDLARGALFL
     SIAFVGTAWW LFIANFLIGC CAMLWIPAKD SAVPNLLRRP DQVETANQLG LVMTYGITTI
     SGFGLYALIS GIPGYFHLQG GDLSFRIATI AVVVNGLLYV SSAVLVATRI PELSGRMATP
     RKRDDDAPGF LVMMRDGLSY AWHRPLLRGL VIGMTGAFAA AGAVIGSAKL YALSLLGGES
     AYGLLFIAVF AGLATGMITA PKLARRLTHG RLFGVTIVCA GLSLGVVSLA PHLWFALVAV
     ALVGGCAGIA FLTGLTIIGS KVEDEVRGRM VALVQSLMKV ILGLSTVASP LLVTTLQPRV
     ITVLDHPLKI DGTRPVLFGA GVLAAAVGLI AYRLMDDRRE TPILSDLLAA LRGRPRRERG
     LLITVEGDAS LDTSVQAREL AEVLRSAGHE VLLASEPDLD ERRVHELLNT ADLAGVRAHA
     LVAAAVRADV VERRVRPALE AGLIVVVDRF ADSPIAHFSA SGSVDTSELE RLSDWATGRL
     RPDLTVLLDR TPTTLPASAL GAPPGAVPAG TAPPGAASAG LEGARRTITH VEHHWQVQRL
     LTGMAAADPD RYLVVDADGT PDEVAARVKA AVARLVGGEI RAAAPLAETP
//

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