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Database: UniProt
Entry: R7SML7_DICSQ
LinkDB: R7SML7_DICSQ
Original site: R7SML7_DICSQ 
ID   R7SML7_DICSQ            Unreviewed;       507 AA.
AC   R7SML7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Mur ligase {ECO:0000313|EMBL:EJF57133.1};
GN   ORFNames=DICSQDRAFT_112243 {ECO:0000313|EMBL:EJF57133.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF57133.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF57133.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF57133.1,
RC   ECO:0000313|Proteomes:UP000053319};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276}.
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DR   EMBL; JH719457; EJF57133.1; -; Genomic_DNA.
DR   RefSeq; XP_007370185.1; XM_007370123.1.
DR   AlphaFoldDB; R7SML7; -.
DR   GeneID; 18834026; -.
DR   KEGG; dsq:DICSQDRAFT_112243; -.
DR   HOGENOM; CLU_015869_2_0_1; -.
DR   OMA; SIHDRIC; -.
DR   OrthoDB; 7073at2759; -.
DR   UniPathway; UPA00850; -.
DR   Proteomes; UP000053319; 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   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
DR   PROSITE; PS01012; FOLYLPOLYGLU_SYNT_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:EJF57133.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053319}.
SQ   SEQUENCE   507 AA;  54511 MW;  75EC9D0235D121DB CRC64;
     MSIDLSLDRI RNLLDHLPIP YTRPTIHVAG TNGKGSVCAL VASILSAASP PLVVGRFNSP
     HLLSPLDGIF VRNEPVDRHI FMEAREEVQR RNEEHCCGAT SFEMYTCYAL LIFERLKVDV
     VVLEVGMGGR LDATNVLPDE SILISALTSV DLDHQAFLGD TVEAITREKA AIARRGKPFV
     VGPQAHQQVE AVARSIIHSS GGEIAVPCAV VAVDWDPDLD GAPVPTQTGI RVPQSQPVHI
     HRPCHADPIR ALLPLHGEHQ LGNLGTAMGI ISALQTHPAC ERPGLNFDQR LTPDAISRGI
     RATRWPGRLS YHAILLSPAS LGTSAIATHE HTDPESSQIL VLADGAHNPA SAAALAAYIT
     STLGKSGGGP VALTYILALS HSPPKTPEQT LKPLLAIREG LPHKRELRLG VALLPFTPPL
     GMPWIKFVPP SDIRAAVDSL VPPSSEAPIP VEPPRTDHVE EALRWAASRR RHGEDSLVVL
     AGSLYLVADF YRLLQELGQA GDIWGSS
//
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