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Database: UniProt
Entry: A0A249KMJ8_9ACTN
LinkDB: A0A249KMJ8_9ACTN
Original site: A0A249KMJ8_9ACTN 
ID   A0A249KMJ8_9ACTN        Unreviewed;       697 AA.
AC   A0A249KMJ8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   31-JUL-2019, entry version 9.
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=A1sIA105_00115 {ECO:0000313|EMBL:ASY18011.1};
OS   Candidatus Planktophila versatilis.
OC   Bacteria; Actinobacteria; Candidatus Nanopelagicales;
OC   Candidatus Nanopelagicaceae; Candidatus Planktophila.
OX   NCBI_TaxID=1884905 {ECO:0000313|EMBL:ASY18011.1, ECO:0000313|Proteomes:UP000217175};
RN   [1] {ECO:0000313|EMBL:ASY18011.1, ECO:0000313|Proteomes:UP000217175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-IA-105 {ECO:0000313|EMBL:ASY18011.1};
RA   Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT   "High microdiversification within the ubiquitous acI lineage of
RT   Actinobacteria.";
RL   Submitted (JUL-2016) 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; CP016775; ASY18011.1; -; Genomic_DNA.
DR   Proteomes; UP000217175; 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   InterPro; IPR010290; TM_effector.
DR   Pfam; PF05977; MFS_3; 1.
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:UP000217175};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:ASY18011.1};
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   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     31     51       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     63     87       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    156    184       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    248    270       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    282    302       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    314    333       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    339    360       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    372    395       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    415    434       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      472    658       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND     474    481       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
SQ   SEQUENCE   697 AA;  75096 MW;  E7B79011C09CBE17 CRC64;
     MPASLPTPAA PKQDATRSVL AIPAFRKLWK AMVFSSLGDW LGLLATTALA AQLSGGSYTT
     ANFAIAGVFI ARLLPAVFLG PIAGVFADRF DRRRLMVVID ILRAALYISI PIVHTYFWLY
     AAMILVECLT LFWSPAKEAS VPNLVPRDKL ENANQVSLLA AYGTAPIAAI LFTLLTLLSG
     ALATISPLLP TNSVDIALYF NALSFLFAAY TIRGLKEIPK GAASKKDAEQ NIGQSLLQGW
     KAVSQSKIIR GLIIGMIGAF SAAGAVIGLA RTFVGDLGGG DAAYGVLFGA VFTGLAIGIA
     FGPKIFAQFS RRRLFGASLS TAGFFLVLLA LISNLTLSVI IVIFLGAFSG ITWVTGFTML
     GMEVHDDVRG RTFAFVQSLI RITLVAVLAT APIIAATIGE HRYEFQNTTL DYNGAQITML
     LAGLIAALIG VISYRQMKDR PQVSLWSDIV AALQGELGAI TGAQTQSIFI AFEGGEGTGK
     STQSKLLAKW LEQEAETVLL TREPGGTTLG KDLRTILLGH ETGAISPRAE ALLYAADRAH
     HVYSVIRPAL DRGEVVISDR YFDSSAAYQG AGRVLIPGEV ARISRWATES LYPTLTILID
     LPAEVGLARL QSLDRLEAEP KEFHERVRQE FLQIAMMDPE RYFVVDGTQS VADIHKQIIG
     RVAELPALKR NAAGPQPNRL LRPIRFATNA VTHRIKK
//
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