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
//
