ID R7QQM9_CHOCR Unreviewed; 426 AA.
AC R7QQM9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Mur ligase central domain-containing protein {ECO:0000259|Pfam:PF08245};
GN ORFNames=CHC_T00000400001 {ECO:0000313|EMBL:CDF39796.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF39796.1, ECO:0000313|Proteomes:UP000012073};
RN [1] {ECO:0000313|Proteomes:UP000012073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT "Genome structure and metabolic features in the red seaweed Chondrus
RT crispus shed light on evolution of the Archaeplastida.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
CC -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00008276}.
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DR EMBL; HG002073; CDF39796.1; -; Genomic_DNA.
DR RefSeq; XP_005710090.1; XM_005710033.1.
DR AlphaFoldDB; R7QQM9; -.
DR STRING; 2769.R7QQM9; -.
DR EnsemblPlants; CDF39796; CDF39796; CHC_T00000400001.
DR GeneID; 17317803; -.
DR Gramene; CDF39796; CDF39796; CHC_T00000400001.
DR KEGG; ccp:CHC_T00000400001; -.
DR OMA; EIIGPTR; -.
DR OrthoDB; 1569at2759; -.
DR PhylomeDB; R7QQM9; -.
DR Proteomes; UP000012073; 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 Reference proteome {ECO:0000313|Proteomes:UP000012073}.
FT DOMAIN 30..176
FT /note="Mur ligase central"
FT /evidence="ECO:0000259|Pfam:PF08245"
SQ SEQUENCE 426 AA; 45439 MW; 00CD27E9FB6F5AFD CRC64;
MRANRISSEP AAELLSRLSS PQKAFSAVHV TGSKGKGSVA TMVTAALLHA PLFVSTVGTY
GSPHVERFNE RIRINGRSIP DDDLANALGQ VLDVREQEPE VRAATVFDVV CASAMLEFKR
IQARWAVIEV GLGGRLDSTN VLDAPVAVIT NVHLEHKEII GPTRKDIAYE KAGIIAPGAH
VVCGMSRGHE LANIFVQEAA SKSPPATIQF CAPEAGHSLF EHNLMLSRAA VQAVARREGV
AGMADNDLLP KSLAEEAMSN LPARQEMFTV ASGAGETDTP VRVLLDGAHV PESVEMVLRE
SSSGRPRVIL YGSGVDKDVE AIGQLLHDAR PLHVVATAAG VSETYMPADD LAERIRKTGN
TPVTAVGDAD EALQAAIDLA NSLGADLAIL GSLHIAGRVR PSLRARQDHF RSNQQKPRFS
PDARQQ
//