ID C5L4J8_PERM5 Unreviewed; 375 AA.
AC C5L4J8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Folylpolyglutamate synthase, putative {ECO:0000313|EMBL:EER08329.1};
GN ORFNames=Pmar_PMAR002704 {ECO:0000313|EMBL:EER08329.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER08329.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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; GG679091; EER08329.1; -; Genomic_DNA.
DR RefSeq; XP_002776513.1; XM_002776467.1.
DR AlphaFoldDB; C5L4J8; -.
DR EnsemblProtists; EER08329; EER08329; Pmar_PMAR002704.
DR GeneID; 9064550; -.
DR InParanoid; C5L4J8; -.
DR OMA; ITHLEYD; -.
DR OrthoDB; 7073at2759; -.
DR Proteomes; UP000007800; 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; 3.40.1190.10; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT DOMAIN 52..200
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 375 AA; 40852 MW; A881542B88161438 CRC64;
MPPLTEALAA SNFCKGAIDQ STESLQRMRR VMEAVGNPLE TLAASGSRFV HVTGTNGKGT
VCSGLAARLQ SYRVGVFTSP CQRWPNDQIS ISGDIMPALE YEQQLKFIMR EAHQKGEVGL
TNFEATTIAA FSWFARMRPL DFVIIEVGVG GRDDATNVLP KTDVAVLTGV ALDHVKFLGP
TLEDICSAKC GIITPHTTTA VASGAYLNAS CLNIVKERCA STGTALRVVT GRGDSDDYKA
HYAALEDEVL SALGVSHQQN HPSDTGTYLH TLRGRQELTH HPLNPTIPII LDGAHNEEGL
RSLTHFIQRM LDQQRDITEV AAHPTIQSPH ELFPLFLKPF SVPIATVYPT TFRDVPEMPW
VEAVDPEEAV TAARQ
//
