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Database: UniProt
Entry: A0A0M8MNH6_9BASI
LinkDB: A0A0M8MNH6_9BASI
Original site: A0A0M8MNH6_9BASI 
ID   A0A0M8MNH6_9BASI        Unreviewed;       533 AA.
AC   A0A0M8MNH6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00012980};
DE            EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980};
GN   ORFNames=Malapachy_3205 {ECO:0000313|EMBL:KOS16056.1};
OS   Malassezia pachydermatis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS16056.1, ECO:0000313|Proteomes:UP000037751};
RN   [1] {ECO:0000313|EMBL:KOS16056.1, ECO:0000313|Proteomes:UP000037751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS16056.1,
RC   ECO:0000313|Proteomes:UP000037751};
RA   Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT   "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT   pachydermatis CBS1879.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC         H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043665};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC         Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC         Evidence={ECO:0000256|ARBA:ARBA00043831};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004992}.
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOS16056.1}.
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DR   EMBL; LGAV01000001; KOS16056.1; -; Genomic_DNA.
DR   RefSeq; XP_017993688.1; XM_018137682.1.
DR   AlphaFoldDB; A0A0M8MNH6; -.
DR   STRING; 77020.A0A0M8MNH6; -.
DR   GeneID; 28729558; -.
DR   VEuPathDB; FungiDB:Malapachy_3205; -.
DR   OrthoDB; 5473102at2759; -.
DR   Proteomes; UP000037751; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005645; FSH-like_dom.
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   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF1; THYMIDYLATE KINASE; 1.
DR   Pfam; PF03959; FSH1; 1.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:KOS16056.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW   Transferase {ECO:0000313|EMBL:KOS16056.1}.
FT   DOMAIN          95..247
FT                   /note="Serine hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF03959"
FT   DOMAIN          317..494
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
SQ   SEQUENCE   533 AA;  59750 MW;  6DC8614A7D033C80 CRC64;
     MHEYKIVIPV PGSTEEAAAQ GHGIHGVLRV YGQPEEASLP ANGSCEGKPL AIFTHGLLSH
     KNALFFRPMT GMVGMDSFRW DMVGEGESPG DWKAGDYPRS IEMLRHVVDY ITKRFGYHID
     LMVGHSKGCV VTSAYVSQYC SLGAKHRGHR PPRRMILCSG RIRMENLRRK DAVFNPQFER
     HGHAVINVKV RGVMKEYRIY PDDHESQCSF PTRQYVQQIP PHIRIFIAHG TLDEVVPVVD
     AGDMVSVLTS HPYRQPGTVH LELIEGADHN YRGEYNDILL KKAQQWLESS ALALETSKPT
     TAVPTPVGVR RGALIVVEGL DRSGKSTQVE RLVQRLQAQL VKFPDRTTSI GTMINSYLTQ
     QSDVNDQSIH LLFSANRWEV ITSILNALRR GQNVVCDRYA FSGIAYSRAK GLDLEWCISP
     DVGLPIPDLT LFLDVDEATA TKRAAYGEER YEKRAFQRLV REAFYNVETL VRYAGATWVR
     IDAGASIDQV SEQIMSHVTR TSEHLPTNLM TLSLDVMRPA LTFVPDANEK ASL
//
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