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Database: UniProt
Entry: A0A1E7FW30_9STRA
LinkDB: A0A1E7FW30_9STRA
Original site: A0A1E7FW30_9STRA 
ID   A0A1E7FW30_9STRA        Unreviewed;       467 AA.
AC   A0A1E7FW30;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=FolC bifunctional protein {ECO:0000313|EMBL:OEU22324.1};
GN   ORFNames=FRACYDRAFT_267244 {ECO:0000313|EMBL:OEU22324.1};
OS   Fragilariopsis cylindrus CCMP1102.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC   Fragilariopsis.
OX   NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU22324.1, ECO:0000313|Proteomes:UP000095751};
RN   [1] {ECO:0000313|EMBL:OEU22324.1, ECO:0000313|Proteomes:UP000095751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU22324.1,
RC   ECO:0000313|Proteomes:UP000095751};
RG   DOE Joint Genome Institute;
RA   Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA   Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA   Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA   Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA   Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA   Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA   Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT   "Extensive genetic diversity and differential bi-allelic expression allows
RT   diatom success in the polar Southern Ocean.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276}.
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DR   EMBL; KV784353; OEU22324.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E7FW30; -.
DR   EnsemblProtists; OEU22324; OEU22324; FRACYDRAFT_267244.
DR   KEGG; fcy:FRACYDRAFT_267244; -.
DR   InParanoid; A0A1E7FW30; -.
DR   OrthoDB; 7073at2759; -.
DR   Proteomes; UP000095751; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR001645; Folylpolyglutamate_synth.
DR   InterPro; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   NCBIfam; TIGR01499; folC; 1.
DR   PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR   PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   PIRSF; PIRSF001563; Folylpolyglu_synth; 2.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095751}.
FT   DOMAIN          291..342
FT                   /note="Mur ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02875"
FT   REGION          44..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  51786 MW;  31211C03ACE530C1 CRC64;
     MRLLHKLIGN PMDDPNRVVV HVAGTNGKGS VCLKIANALR NQQRKSSFSF PGQEEKDNSK
     DNRNLNVGIF CSPHVSSFRE RMQVNGEMIT EEEVVELLPQ IYDLCLPENN DIPATFFEIT
     TALAFLFFAK RGVDVVVLET GLGGRLDATN VVNNPALSII TSIGLEHTRI LGDTIELIAR
     EKGGIIKKDC PVLVGPHCPH DVLMGVAREK GAGRYYVPSL VHGNLQDFAH MTKTDKNAEE
     EESFAITDYD IENQEIAKAA LLLLEQRHPE IFGVHLKPDE VDNFVSIRPP CRFEYFQKEN
     ATVILDVAHN PLAIEYLVHK LKTTFPEGTF RFVAGMSSDK DLGQCARSLL SVTVGSDDCR
     NKPRIHLVQA AHPRAASLED ILDAESILKT AAYYDFEDRS ITAQVVQALE MTKENDNEIL
     VVCGSVFLMA EAREALGIDE PRDSDCITEM AGAGIRHTQE NFGNTKM
//
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