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Database: UniProt
Entry: A0A292Z4K8_9PSEU
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ID   A0A292Z4K8_9PSEU        Unreviewed;       599 AA.
AC   A0A292Z4K8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-NOV-2019, entry version 11.
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=TOK_5392 {ECO:0000313|EMBL:GAY10908.1};
OS   Pseudonocardia sp. N23.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Pseudonocardia; unclassified Pseudonocardia.
OX   NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY10908.1, ECO:0000313|Proteomes:UP000222857};
RN   [1] {ECO:0000313|EMBL:GAY10908.1, ECO:0000313|Proteomes:UP000222857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N23 {ECO:0000313|EMBL:GAY10908.1,
RC   ECO:0000313|Proteomes:UP000222857};
RA   Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT   "Characterization of newly isolated Pseudonocardia sp. N23 with high
RT   1,4-dioxane-degrading ability.";
RL   Submitted (AUG-2017) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00165}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAY10908.1}.
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DR   EMBL; BEGX01000063; GAY10908.1; -; Genomic_DNA.
DR   Proteomes; UP000222857; Unassembled WGS sequence.
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; 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.
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:UP000222857};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:GAY10908.1};
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:UP000222857};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204, ECO:0000313|EMBL:GAY10908.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     20     41       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     62     86       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     98    120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    154    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    188    208       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    220    238       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    244    266       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    278    303       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    323    340       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      409    546       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   REGION      558    599       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    571    587       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   599 AA;  62720 MW;  C2BDF919BE6B0C0D CRC64;
     MVVCDILRFG LFISIPLVGS LWWLFAATFL IEICSLFWIP SKDASVPNLL RRPDQVETAN
     QLALVMTYGV AVLTAVGLFT VISSAGSLID TTSPLTTVYV ALVINGCGYL LTATTVWFRI
     KEISGRTAER QGDSPAGLLS LLRGGFAFVG STPLIRGLVI GIIGAFAAGG AVIASAKLYS
     ASLGGGDAAY SVLFGGIFVG LACGMGVAPR LSRRLPHNRL FGAAIVAAGV ALTLVALAPH
     LFVAIVAVGL VGGFAGIAFL TGLTIIGAQV ADDVRGRVVA FVQSLVRVVL LGSMSLVPVL
     VGLVSARRID LFGYPFVIDG TRTVMFAGGL VAAVVGMLAY RQMDDRRTEP LLPDLLAALR
     RGDRRTGSGV LIAVEGATPV ETAEQTERLV ATLRVDGYDV VEPGDDRLRV VEAETQHSSA
     RAKALAVAAV RADTVERVVR PALRSGAVVV MDRFLASPLA QYGVESDRDD AALDSSELEN
     IVAWATGRLR PDVSVLLDRA PDGSAPPAGV AGEEHVRVQK LLTRMAAAEP HHYVVVDADA
     PADVVAARVI DGLRPLMRPP AGAAHGPTVP LQKTSAEQPT EPVSTRTVVP SRDDDPAPT
//
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