ID A0A316TY03_9BASI Unreviewed; 375 AA.
AC A0A316TY03;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00012980};
DE EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980};
GN ORFNames=BCV69DRAFT_295629 {ECO:0000313|EMBL:PWN17980.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN17980.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN17980.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN17980.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004992}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000256|ARBA:ARBA00009776}.
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DR EMBL; KZ819339; PWN17980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TY03; -.
DR STRING; 1684307.A0A316TY03; -.
DR OrthoDB; 5473102at2759; -.
DR Proteomes; UP000245942; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR CDD; cd01672; TMPK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018094; Thymidylate_kinase.
DR NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF1; THYMIDYLATE KINASE; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245942}.
FT DOMAIN 126..284
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 68..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 40345 MW; BE1F4DE31EA2C648 CRC64;
MSLIFTPRQA RISSAQSGDL AADEGVLFTR DSLLSFLHSH GVTADASHVQ VDKLTSFATV
GRMASATSSQ SQAQASGSSS ASNLAASSST NPSIDPTPTT SAAPPAPAQS VTGSLAPKKR
GSFIVIEGLD RAGKSSQVEL LSQYLSDRKQ DGKVKVMKFP DRTTPIGRIL NSYLTDPSIS
LHPKAVHLLF SANRWELHDQ ILKDLNDGCD IIADRYAGSG VAYSRAKGLP LPWLLSPDTS
LPSPDLTLFL SLSAAAAAKR GGYGEERYEK EEMQRRVREA FAEIEEVTRQ GSRSLQDQGQ
GQGQGQGQGQ GQEQGGEVEG RMGTRWRTLD AEKSLEEVFE EVKREVESVR DEVHRSGRGI
GGLWNGHGEL DAQTH
//
