ID A0A0D1WM79_EXOME Unreviewed; 378 AA.
AC A0A0D1WM79;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=thymidylate synthase {ECO:0000256|ARBA:ARBA00011947};
DE EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
GN ORFNames=PV10_07432 {ECO:0000313|EMBL:KIV90090.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV90090.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV90090.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV90090.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-
CC dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422;
CC EC=2.1.1.45; Evidence={ECO:0000256|ARBA:ARBA00001707};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004992}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847524; KIV90090.1; -; Genomic_DNA.
DR RefSeq; XP_016221664.1; XM_016372332.1.
DR AlphaFoldDB; A0A0D1WM79; -.
DR STRING; 212818.A0A0D1WM79; -.
DR GeneID; 27325277; -.
DR VEuPathDB; FungiDB:PV10_07432; -.
DR HOGENOM; CLU_021669_0_2_1; -.
DR OMA; IVYELLW; -.
DR OrthoDB; 1118873at2759; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000054302; Unassembled WGS sequence.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 1.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR InterPro; IPR000398; Thymidylate_synthase.
DR InterPro; IPR020940; Thymidylate_synthase_AS.
DR NCBIfam; TIGR03284; thym_sym; 2.
DR PANTHER; PTHR11548:SF2; THYMIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 52..378
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
SQ SEQUENCE 378 AA; 42150 MW; 4A1218D37DB58C47 CRC64;
MAPSAVESEI LSPPGNSLNF LKENAKMLQS AMPTTEPSTK ATQPPSQPHE EHQYLDLIND
ILKRGEHRPD RTGTGTLSLF APPQLRFSLS KPDPSNPSGD RIPVLPLLTT KRVFLRAVTT
ELLWFVSGCT TSKPLSEAGI HIWDGNGSRE FLDKLGFTER EEGDLGPVYG FQWRHFGAEY
LDPNADYTNK GVDQIKEIVR KLKHSPYDRR IILSAWNVAD LSKMALPPCH MFAQFYVSFP
DAARGEAALQ SLSENGNNDD NTDKKSRGHL SCVLYQRSCD MGLGVPFNIA SYALLTHMLA
HACDLVPGEL IHTMGDAHVY LDHVDALKEQ LVREPRDFPT LNIKRDDRGS GEMDGWKLDE
LEVIGYKPHG GIKMKMSV
//
