ID A0A0H2SHE0_9AGAM Unreviewed; 531 AA.
AC A0A0H2SHE0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Mur ligase {ECO:0000313|EMBL:KLO16466.1};
GN ORFNames=SCHPADRAFT_208557 {ECO:0000313|EMBL:KLO16466.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO16466.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO16466.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO16466.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
RL Submitted (APR-2015) 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; KQ085915; KLO16466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2SHE0; -.
DR STRING; 27342.A0A0H2SHE0; -.
DR InParanoid; A0A0H2SHE0; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000053477; 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; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR11136:SF0; DIHYDROFOLATE SYNTHETASE-RELATED; 1.
DR PANTHER; PTHR11136; FOLYLPOLYGLUTAMATE SYNTHASE-RELATED; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KLO16466.1};
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:UP000053477}.
FT DOMAIN 56..211
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 531 AA; 57805 MW; EFEB082CA0BEC62B CRC64;
MVMVVRGQRA DELRDAHGTH STSSHLTTAM SIDLTLDRIR ILLSKFEKYT RPTIHVAGTN
GKGSVCALLS SVFQACHPTP SVGRFNSPHL VDVTDSITIN GKPISQSTFG AIYSEVKETN
DRQRIGASNF EVLTVTALLI FERQQVDVVV CEVGMGGRLD ATNVIPDEAI VASVITSIDL
DHQAFLGSTV AAIAREKAGI IRRNKPVVVG QQKHAEVVGV VEEIAHSQGA FLTIAPCAKT
RNWNEILDGA RPPSFSLNPF SPPPPNPVSV EVLDSDPYDL LLPLHGEHQR NNLGVVVAVL
KILSTISSVS RNPNNFLQAA DASTMRRGIR ECIWPGRLSF HTFKGLNANS PELPILADGA
HNEAASQLLA NYVSNLVQNP ASENTERTTN LTFILALSHS PPKTPSSVIQ PLLTVCDAFG
TWRSRTRLSV RVAALRFTPP SGMPWVKSVP PSEIQKVVED TAKASPDRKC TDYWTASDAE
VDDARNDLAK ALEWASQWSH DEDGRKLDHL VVIAGSLYLV ADLYRLLDNH A
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