ID A0A0D2E6T7_9EURO Unreviewed; 522 AA.
AC A0A0D2E6T7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Unplaced genomic scaffold supercont1.1, whole genome shotgun sequence {ECO:0000313|EMBL:KIW85826.1};
GN ORFNames=Z517_01218 {ECO:0000313|EMBL:KIW85826.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW85826.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW85826.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW85826.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-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; KN846969; KIW85826.1; -; Genomic_DNA.
DR RefSeq; XP_013289634.1; XM_013434180.1.
DR AlphaFoldDB; A0A0D2E6T7; -.
DR STRING; 1442368.A0A0D2E6T7; -.
DR GeneID; 25300708; -.
DR VEuPathDB; FungiDB:Z517_01218; -.
DR HOGENOM; CLU_015869_2_0_1; -.
DR OrthoDB; 7073at2759; -.
DR UniPathway; UPA00850; -.
DR Proteomes; UP000053029; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT DOMAIN 30..175
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 522 AA; 57393 MW; 6D1338014CE0226D CRC64;
MINLGLQRIT QLLNPLFSTH PTLPWRAVHI AGTNGKGSVA ALVSTFLGHL GYKVGRFTSP
HLIDRWDCIS LNRRVVERDK FLQVEQHFRD RSVREDIHAS EFEILTAAAF QLFTDAKVDV
AVIECGLGGR LDATNVLRPE DVLVSVLTKV GLDHTAFLGE TLEAIATEKV GIFKPGVPVV
LDQSNQRNVI DVAESRLRDL GWEDGGRAGV YISIEERRRE FDKAIARMRL AKHQAQNLYL
AFSCFQTAEE RLSGRSARRE DLTGDRSPGP LNFPQDFLVA TDQLRVDTVK KSLDILVPLA
QSSLPGRLQW IVLPSRLLPQ NLEDRAAQLN AGQTRQSLNA KVLLDGAHNW QSAAALADYI
KAQWRPPSKE PVPPVTWLLS VKNDKKVDEI LQLLLGPNDN VLTCSFGPVD GMPWVKSMGA
IELAEIATKY TSGIVEALGD EYIGGVTGKE DKTTPDEKMR IIIRQAVSVA SRDSKFSPLE
LKLCITGSLY LVGDVLRCIR NAGGPVVDGS SAPALAGSSY RV
//
