ID A0A1L9PZC6_ASPVE Unreviewed; 681 AA.
AC A0A1L9PZC6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=thymidylate synthase {ECO:0000256|ARBA:ARBA00011947};
DE EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
GN ORFNames=ASPVEDRAFT_56358 {ECO:0000313|EMBL:OJJ06825.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ06825.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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}.
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DR EMBL; KV878135; OJJ06825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9PZC6; -.
DR STRING; 1036611.A0A1L9PZC6; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_56358; -.
DR OrthoDB; 1118873at2759; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000184073; Unassembled WGS sequence.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IEA:InterPro.
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 GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
DR CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1.
DR Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 1.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR004803; TGT.
DR InterPro; IPR036511; TGT-like_sf.
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 InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00430; Q_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR NCBIfam; TIGR03284; thym_sym; 1.
DR PANTHER; PTHR11548:SF2; THYMIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR Pfam; PF01702; TGT; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Reference proteome {ECO:0000313|Proteomes:UP000184073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 54..318
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT DOMAIN 372..681
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT REGION 15..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
SQ SEQUENCE 681 AA; 75105 MW; 5DE3D1DF7826BD74 CRC64;
MQNIRASRIV LHPFYPAPKA TSPSPPRSMS TTPPRKAMPS ALTFDLHRKC STTKARASTL
HLPHGSVPLP IFMPVATQAS LKGLTYDQLK QTGCMLCLNN TYHLGLKPGQ AVLDEVGGAH
KFQGWDRNIL TDSGGFQMVS LLKLAKVTEE GVRFLSPHDG TPMLLTPEHS ISLQNSIGSD
IIMQLDDVIA TTSPDHARIN EAMERSVRWL DRCIEAHKNP ETQNLFCIIQ GGLDLELRKQ
CCAEMVARDT PGIAIGGLSG GEAKEEFCKV VDTCTGLLPD HKPRYVMGVG YQEDLVIGVA
LGADMFDCVW PTRTARRDEG GLGITRAYIH HLASKETAGA HLKMTLSNDI QQGNGAAATP
PQIPQNPSHE EHQYLNLIRQ ILTEGEHRPD RTGTGTRSIF APLPMHFSLS KPDPANVGSK
IPVLPLLTTK RVFLRAVLAE LLWFISGSTS SIPLSEAGIK IWDGNGSREF LDNVGLSHRE
VGDLGPVYGF QWRHFGAEYV DAHTDYTGQG VDQLADVVRK IKETPFDRRI IMSAWNPADL
KKMALPPCHM FAQFYVSYPE GIEEGKGKGK GELSCLLYQR SCDMGLGVPF NIASYALLTH
IIAHATDLNP GKLIHTMGDA HVYLDHVEAL QEQLTREPTE FPELKIKRED RGSGVIDGWE
EEEFEVIGYQ PHKAIKMKMS V
//
