ID   A0A369GIH3_9HYPO        Unreviewed;       571 AA.
AC   A0A369GIH3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-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=CP532_2119 {ECO:0000313|EMBL:RDA84239.1};
OS   Ophiocordyceps camponoti-leonardi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA84239.1, ECO:0000313|Proteomes:UP000252748};
RN   [1] {ECO:0000313|EMBL:RDA84239.1, ECO:0000313|Proteomes:UP000252748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA84239.1,
RC   ECO:0000313|Proteomes:UP000252748};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RDA84239.1}.
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DR   EMBL; PDHP01000131; RDA84239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369GIH3; -.
DR   STRING; 2039875.A0A369GIH3; -.
DR   Proteomes; UP000252748; 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; 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; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000252748}.
FT   DOMAIN          362..546
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   REGION          24..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   571 AA;  62407 MW;  F6246A3A2A465EC7 CRC64;
     MAAVARQPFA PLDGSRLQSL TSLKNRQNGM SYTSTSLHRR KADFDDSENV DPTLSAKRSK
     ASGPVDVDAG KAPVFYLSRS ATAPRHDALP LSASTKVTSA AARPVLQRKS PGSGIAKSTP
     LSAPAGRSPT GRGKRSGLLS NRRRYTRLDP PAFRLGSSSA PFSLDAAVKG TISSYSARPS
     KPLLPETKSS WHFDIHEDTP EQEMTNLLQH GTCILDISSD EENERKARRD SDEGRNKENI
     APADDISQTS VRHSDDMPLD KERIALGEMN TADFYPKGCD ETSVVLIPAD EELPVDTGAG
     ADADADADAD AVRNVEQLMR SSADELSAKA AVLEPIDGTG ESFDLWESGS AKDESRGALI
     VLEGLDRSGK STQAQLLVQR FSEEGRPVKM MRFPDRSTPI GQLIDSYLRR ATDMDDHAIH
     LLFSANRWEA AKHMRELLAA GTSVVCDRFY HSGIVYSAAK DNPELSLEWA RGPDIGLPRP
     DAVIFLDLNE EQAKARGGWG CEAYEEEQMQ RRVRELFSTL SKGKGQDGED LIIVDAKETV
     DEVAEQVWER VLTRVKLVDK GELGRTVRTM A
//