ID A0A0V0S0M9_9BILA Unreviewed; 435 AA.
AC A0A0V0S0M9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=Thymidylate synthase {ECO:0000256|ARBA:ARBA00015931};
DE EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
DE Flags: Fragment;
GN Name=TYMS {ECO:0000313|EMBL:KRX20288.1};
GN ORFNames=T07_5895 {ECO:0000313|EMBL:KRX20288.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX20288.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX20288.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX20288.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004992}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits. {ECO:0000256|ARBA:ARBA00011695}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000256|ARBA:ARBA00008045}.
CC -!- SIMILARITY: Belongs to the thymidylate synthase family.
CC {ECO:0000256|ARBA:ARBA00009972}.
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:KRX20288.1}.
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DR EMBL; JYDL01000050; KRX20288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S0M9; -.
DR STRING; 6336.A0A0V0S0M9; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0051082; F:unfolded protein binding; 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:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00632; Prefoldin_beta; 1.
DR CDD; cd00351; TS_Pyrimidine_HMase; 1.
DR Gene3D; 1.10.287.370; -; 1.
DR Gene3D; 3.30.572.10; Thymidylate synthase/dCMP hydroxymethylase domain; 1.
DR HAMAP; MF_00008; Thymidy_synth_bact; 1.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
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; 1.
DR PANTHER; PTHR11548:SF2; THYMIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11548; THYMIDYLATE SYNTHASE 1; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR Pfam; PF00303; Thymidylat_synt; 1.
DR PRINTS; PR00108; THYMDSNTHASE.
DR SUPFAM; SSF46579; Prefoldin; 1.
DR SUPFAM; SSF55831; Thymidylate synthase/dCMP hydroxymethylase; 1.
DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..321
FT /note="Thymidylate synthase/dCMP hydroxymethylase"
FT /evidence="ECO:0000259|Pfam:PF00303"
FT COILED 394..428
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX20288.1"
SQ SEQUENCE 435 AA; 50429 MW; 0B710F89E72453D6 CRC64;
LSYSICILEF IDIYTMTETV HKLDTNSTSQ DDYVNQEELN YLNQLKDIID HGVRKNDRTG
IGTLSTFGTQ SRYCLRDDIF PLLTTKRVFW RGVVEELLWF ISGSTNAKQL SEKNVNIWDG
NSSREFLDSR GLYNYEEGDL GPVYGFQWRH FGCPYSSMTA DYTGKGYDQL QQCIKMIREE
PESRRIIMTA WNPCDLEKVA LPPCHCFVQF YVADGELSCQ MYQRSADMGL GVPFNIASYS
LLTRMIAHIT SLKPGFFIHT IGDAHVYLTH VDALKVQMER KPRPFPKLKI LRNVENIDDF
RAEDFELINY KPYPKISMPM ARLELEILKL QNIQNDIKKH ARIRQQVETQ YTENHFALEE
LNLLTDQTLI YKMIGPVLVK HSLAEAKGTI IKRLEFIEQE KKRLDDALEK AKNEVVAQKD
KINFLQNQLS STTAE
//
