ID E7A295_SPORE Unreviewed; 1229 AA.
AC E7A295;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00012980};
DE EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980};
GN ORFNames=sr11108 {ECO:0000313|EMBL:CBQ73602.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ73602.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ73602.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311473; CBQ73602.1; -; Genomic_DNA.
DR AlphaFoldDB; E7A295; -.
DR EnsemblFungi; CBQ73602; CBQ73602; sr11108.
DR VEuPathDB; FungiDB:sr11108; -.
DR eggNOG; KOG3327; Eukaryota.
DR HOGENOM; CLU_008149_0_0_1; -.
DR OrthoDB; 5473102at2759; -.
DR Proteomes; UP000008867; Chromosome 8.
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; 3.40.50.300; 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 Kinase {ECO:0000313|EMBL:CBQ73602.1};
KW Transferase {ECO:0000313|EMBL:CBQ73602.1}.
FT DOMAIN 436..613
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 129177 MW; BE0F3A0B4EEC1682 CRC64;
MSGLKSSVVP QSNGVADTDR SPRRKLSSDL MRIKNFPSTL SLRKADQETL QPSSSTFSRF
KPFGSRNSLG ADQADTSSDS KSSKRTSWLL DAFKPSKKPP PSFQVVRKPP NRSTSFHSSS
HQPSPHLEIH RPDSHLSSSH DAAAPHALQP AAPRISLSAP TSDAPVQQQP HFDNARAAPS
QPTQNGLVAR SPYPPSTSKT RRSSGAIAAT NSRRTSDPYL NLGSASNSAA QSPSASPSMD
PTNGSFSLHS FRNVRSASDV STPDDLSARP HSRVQSMISV DEYLTPGEEL PEPQYPDSNA
SRSAGTTAAG PDRAQSTSPS PLPSNNAKPA SISAAKFRQA ARQRSESGSI PTVDAIQATT
GGSGFVRPPR SRTPSQDLAA MEAVLAQTHH KPTHRSSDAA NDPRKSTDPT SLPATALASN
TPEDSQRRKR GFFIVVEGLD RAGKSTQVER LAQHLHAKAI KFPERTTAIG QMINSYLAQT
SDLDDQAIHL LFSANRWECV ASIKKTLDAG ESIVCDRYAF SGIAYSVAKG LSYDWCRNPD
VGLPLPDLTM FLDLDAETAA ARGGYGEERY EKLDFQAKVR DAFTRVSQDV RAHGGRWVTI
DASKTLDQVT DDIQKAVQRV TSSIDRVGAR LGRLFVSEPR PPNPRAGSSN ELFPPAMVPA
AKRSSMSSDN SDGRGKSLDQ PRISVNTATT NGSFPAARPS GSPLTYTEQL AAVRAAAAGT
LSGFFGASST TVDQQQTSPA MGERQLAGAD GPSPVNAARG QGFDSARVLA KYPDGSGRRR
TLIDVIGEIE NQPQQAAWPD HRRSASAAAE STSPTLQSPV DGFPSTFAQA GRVRRSTDQG
RGSQLPTIAS GSVPPAAGAR STSLTVQSGE GGSGAAPPVA ASGEKPLPLS PNMRASSFTP
TGNAGGVENS LNPSAQNVRA STLSPTARTA SPAITTSSRS SLASPPPHVS SSTPPIPRPA
STSPADHAYV DALSSQHLSM LNVQQNHAEM QEQYMRNYMA MMANPMLAQQ AHYQMMLQRH
QQQYYGRAAS AIGFGGGHLG AGANGNGVQP GATQAGAGAG PPLAAFMQPA QAMAMQSSDA
IVGGKRERVR STHKRTQSSG SLYENGAGGA PPSSAQQPPP MLSMMMAPPP PATSAATSPT
VAAASSPAVG PQAFYGAAHP HAMYAQQPMF YPNGAQAFPA MMGGAAWAQQ AAGYGGGRPG
YVSSRSEVGV PLALRSQRSA DKGLRQPQQ
//
