ID A0A1X2IUQ1_9FUNG Unreviewed; 430 AA.
AC A0A1X2IUQ1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Mur ligase {ECO:0000313|EMBL:ORZ22504.1};
DE Flags: Fragment;
GN ORFNames=BCR42DRAFT_406319 {ECO:0000313|EMBL:ORZ22504.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ22504.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ22504.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ22504.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORZ22504.1}.
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DR EMBL; MCGE01000004; ORZ22504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IUQ1; -.
DR STRING; 90262.A0A1X2IUQ1; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000193560; 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 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 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; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:ORZ22504.1};
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:UP000193560}.
FT DOMAIN 27..267
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
FT NON_TER 430
FT /evidence="ECO:0000313|EMBL:ORZ22504.1"
SQ SEQUENCE 430 AA; 46786 MW; ADB016A66F3098D0 CRC64;
MDFGLERIHR LLGYLGNPHQ RVPIIHVAGT NGKGSVCAYV SNVLLAAGYK VGRFNSPHLI
APHDSVQING QAVDAKVFED ISNMVAKIDN DNQLGATSFE LLVGTALWLF DHQQGALDFV
VVEVGLGGLL DATNVFTAPI MTVITSIGLD HMGLLGNTIE DIALAKAGIM KKGCPVVIAP
QAEPMAEKAL VDHARALDIS CVVMEPSTII TNNGNDSNGS TTGQRMQLQK KPIDVTKGTS
LSAIDVDYTV SLYGDYQREN SAAAVMALKW MASIGYIQLT KEALQDGMAS TKWPGRLDWV
DTERISLPEK KDRLAFSRIL VDGAHNPPAC RELRHYVDQV LDRQQRKRVI WIIGVTLGKS
LNDMLPTLIR PDDVIFTVPF SQPEGMPWIH CVDPVVLAQQ HADSAEHQKE ALPQKTLKDA
LVAASALYCA
//
