ID   A0A446BHL6_9PEZI        Unreviewed;       404 AA.
AC   A0A446BHL6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=1045b5d7-1731-47ca-a065-dce5c83e0aac {ECO:0000313|EMBL:SPQ21985.1};
GN   ORFNames=TT172_LOCUS4404 {ECO:0000313|EMBL:SPQ21985.1};
OS   Thermothielavioides terrestris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX   NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ21985.1, ECO:0000313|Proteomes:UP000289323};
RN   [1] {ECO:0000313|EMBL:SPQ21985.1, ECO:0000313|Proteomes:UP000289323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Huttner S., Dainat J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276}.
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DR   EMBL; OUUZ01000008; SPQ21985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A446BHL6; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000289323; 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; 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   PIRSF; PIRSF001563; Folylpolyglu_synth; 1.
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   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
SQ   SEQUENCE   404 AA;  43738 MW;  B6C85968FF28800E CRC64;
     MIDLGLARVS RLVQHVPQTW KAIHVAGTNG KGSICAYLSA MLTASGLSWA RFTSPHLIDR
     WDCIAVNGKP VSESVFRDAE NLVKQRDQEG RVGATEFELL TATAFEIFHR QNVEYGVVEV
     GLGGRLDATN VLKQKAVTVI AKIGLDHQAF LGNTIEEIAL QKAGIIRAGV PCVVDGSNQP
     SVLRVIEEHA REIGAELHYP AIASVSEALS GEEFEPHQVQ NLACAHAAFR LACPGDDRPL
     AHFLPMIKQM QWPGRLQRLD LQKITGRPQE ALLDGAHNPQ SAEVLAHYVS RHLRSGDQPV
     TWVVAATQGK DMNGIFSLLL KPDDRAAAVR FGPVDGMPWV KPADPVGLLE LAAQYGVQEP
     AMYDAGDDIR AALTWASQAA GDGPLVIAGS LYLVSSVLRL LRES
//