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Database: UniProt
Entry: A0A088C316_9CAUD
LinkDB: A0A088C316_9CAUD
Original site: A0A088C316_9CAUD 
ID   A0A088C316_9CAUD        Unreviewed;       284 AA.
AC   A0A088C316;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-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=S14_38 {ECO:0000313|EMBL:AHK11150.1};
OS   Shewanella sp. phage 1/4.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX   NCBI_TaxID=1458859 {ECO:0000313|EMBL:AHK11150.1, ECO:0000313|Proteomes:UP000029368};
RN   [1] {ECO:0000313|EMBL:AHK11150.1, ECO:0000313|Proteomes:UP000029368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25156651;
RA   Sencilo A., Luhtanen A.M., Saarijarvi M., Bamford D.H., Roine E.;
RT   "Cold-active bacteriophages from the Baltic Sea ice have diverse genomes
RT   and virus-host interactions.";
RL   Environ. Microbiol. 0:0-0(2014).
RN   [2] {ECO:0000313|EMBL:AHK11150.1, ECO:0000313|Proteomes:UP000029368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24297705; DOI=10.1007/s00792-013-0604-y;
RA   Luhtanen A.M., Eronen-Rasimus E., Kaartokallio H., Rintala J.M., Autio R.,
RA   Roine E.;
RT   "Isolation and characterization of phage-host systems from the Baltic Sea
RT   ice.";
RL   Extremophiles 18:121-130(2014).
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009972}.
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DR   EMBL; KJ018209; AHK11150.1; -; Genomic_DNA.
DR   RefSeq; YP_009100345.1; NC_025436.1.
DR   GeneID; 22110425; -.
DR   KEGG; vg:22110425; -.
DR   OrthoDB; 13491at10239; -.
DR   Proteomes; UP000029368; Genome.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:InterPro.
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   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   PANTHER; PTHR11548:SF9; 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029368};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..282
FT                   /note="Thymidylate synthase/dCMP hydroxymethylase"
FT                   /evidence="ECO:0000259|Pfam:PF00303"
SQ   SEQUENCE   284 AA;  32483 MW;  061027CCEA2C2F05 CRC64;
     MTSLHYEQQY LDLCNKLLTK GVWINNSRTG KRCLSTETTI FQYDVGAGEF PLITTRKAFY
     KMAIAEVIGY WQGLTNANDF VKLGCATWLA NSNKNTSWLN NPNRKGDGDM GNVYGYFGHN
     FGGVNQFEKV YNNLSNGIDD RGEIITYWKP DQFSEGCLRP CLHSVQFNLL GGILSMTATQ
     RSCDVPLGLV SNIPQCWIML YLMARITGHK AGKVTHVINQ PHVYEDQVDL LRLQLNREPI
     DCKPEIEVCD SIQTWEDIMN LKNMDKFMLY GYQSHDRIDF PFSE
//
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