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Database: UniProt
Entry: A0A1I2KZ41_9ACTN
LinkDB: A0A1I2KZ41_9ACTN
Original site: A0A1I2KZ41_9ACTN 
ID   A0A1I2KZ41_9ACTN        Unreviewed;      1093 AA.
AC   A0A1I2KZ41;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JUL-2019, entry version 10.
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=SAMN05216251_125101 {ECO:0000313|EMBL:SFF71589.1};
OS   Streptomyces alni.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF71589.1, ECO:0000313|Proteomes:UP000199323};
RN   [1] {ECO:0000313|EMBL:SFF71589.1, ECO:0000313|Proteomes:UP000199323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF71589.1,
RC   ECO:0000313|Proteomes:UP000199323};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FONG01000025; SFF71589.1; -; Genomic_DNA.
DR   Proteomes; UP000199323; 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; 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:UP000199323};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:SFF71589.1};
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:UP000199323};
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     52     70       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     82    105       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    125    144       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    208    233       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    295    316       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    328    346       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    358    377       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    383    404       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    425    447       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    459    479       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      515    698       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND     517    524       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   REGION      803   1093       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    803    856       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    937    955       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    973    987       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS   1051   1068       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1078   1093       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1093 AA;  115137 MW;  5C2E2B181A87A037 CRC64;
     MTPSQQQPAA DVTVTDAFAT DLAADSRERA VGALLKIPAL RKLWSAQLTG AVADRLGLLV
     LLWLAVQAAA ADGAYGGGYR GVSLAVAAVF AARLVATLLF GAVLLGPLSA LTAEGGKLDR
     RWTMIGADAV RLGLFIVAPL WITWSQHNAL TWLLVTAFVT GIAERLWAVA KDGAAPLLLP
     PPGDTSVRPA PDHLATLHRL DLRTSFSALP LAAAAMVVVT LVNTLIAVGV TWFDQHQVAL
     SSYVAAGLFS SSMSVLYLLE LPSGTVARPR SPLEGLRLPK GPAGAERGRT GALPLLVLAT
     AAVVGAIGTA VAVSVLHALD LGFGPTGFGL LVLALTAGTV CGIRLAPRTL PALSRRRLLA
     LSIGITGLGL LLTGIVADQT TVLLLALLTG AAAGVTANTG HVLIEQEAEA GRRGRTTEHL
     HAVSRAVLAV AVIAGPAVAG AIGPHRIQKG HFTFDHGGAA YTLMLVGALL LPVAALVLGK
     TDDRSGVPLR RDLREALTGA EPAVAPAATG FFIAIEGGDG AGKSTQVEAL AEWIRAKGHE
     VVVTREPGAT AIGKRLRSIL LDVASGGISH RAEALLYAAD RAEHIDTVVR PALERGAVVI
     SDRYIDSSVA YQGAGRDLAP TEIARISRWA TDGLVPHLTV LLDVSPEAAR ERFTEAPDRL
     ESEPAAFHQR VRAGFLTLAA ADPGRYLVVD GGQDPADVTT VVRHRLDQLL PLSEQEIEAR
     AEAERQAAAE AARLAAEEAA RKAEEERLER ERQEQLERLR REEEERRLAA EEEARREIAE
     RAAAREAEAA RLRAEEEARV AAEETARREA EEAARAAEQE RLRRLAEEQA RLRAEAEERR
     LEKQRKAEEA LLRAERARTE AAAAAAAAAA AAESGGTEET TEVTALPVEP VEPAEPGASS
     SDTTLVNVVP AVPDAEKTAV LRAVPAEEAD SEETTVLPAV TEDSSETTVL PAVTEDSSET
     XXXXXXXXXX AVTEDSSETT VLPAVTEDSS ETAVLPAVPA EEAAEAEEEP GDGSETTTVM
     PPVVPPTGSP AADDPTDRVP PWLFRPEDQP GASPDRPRRP RPDWAEETPL DDLPTLADEL
     LGPHDDDPPP ARR
//
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