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Database: UniProt
Entry: E0CUK0_VITVI
LinkDB: E0CUK0_VITVI
Original site: E0CUK0_VITVI 
ID   E0CUK0_VITVI            Unreviewed;       536 AA.
AC   E0CUK0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Mur ligase central domain-containing protein {ECO:0000259|Pfam:PF08245};
GN   OrderedLocusNames=VIT_16s0050g02490 {ECO:0000313|EMBL:CBI22549.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI22549.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- SIMILARITY: Belongs to the folylpolyglutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008276}.
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DR   EMBL; FN595243; CBI22549.3; -; Genomic_DNA.
DR   RefSeq; XP_002267695.2; XM_002267659.4.
DR   AlphaFoldDB; E0CUK0; -.
DR   STRING; 29760.E0CUK0; -.
DR   PaxDb; 29760-VIT_16s0050g02490-t01; -.
DR   EnsemblPlants; Vitvi16g01211_t001; Vitvi16g01211_P001; Vitvi16g01211.
DR   GeneID; 100267405; -.
DR   Gramene; Vitvi16g01211_t001; Vitvi16g01211_P001; Vitvi16g01211.
DR   eggNOG; KOG2525; Eukaryota.
DR   HOGENOM; CLU_015869_4_1_1; -.
DR   InParanoid; E0CUK0; -.
DR   OMA; NLGWRIS; -.
DR   OrthoDB; 7073at2759; -.
DR   Proteomes; UP000009183; Chromosome 16.
DR   ExpressionAtlas; E0CUK0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblPlants.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008841; F:dihydrofolate synthase activity; IEA:EnsemblPlants.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IBA:GO_Central.
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; PS01011; FOLYLPOLYGLU_SYNT_1; 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:UP000009183}.
FT   DOMAIN          80..325
FT                   /note="Mur ligase central"
FT                   /evidence="ECO:0000259|Pfam:PF08245"
SQ   SEQUENCE   536 AA;  57800 MW;  CC2E67264A6F41E1 CRC64;
     MKIFRVVSHK RTLLGFKRSF STEPELKDFL NYLDNLKNYE KCGVPKDAGT DSSHGFDLGR
     MNRLMDRLGN PETGFKAVHI AGTKGKGSTA AFLANILRTE GYAVGCYTSP HVRTIRERIS
     LGKLGEPVSA KALNCLFHRI KPILDEAVAL ENGRLSHFEI LTAMAFKLFA QENVDVAVIE
     AGLGGARDAT NIISSSGLAA AVITTIGEEH LAALGGSLES IAMAKSGIIK QGCPLVLGGP
     FLPHIEHIFL DKASSMCSPV VSASGPGNRS AVKGVSKSNG KPFQSCDIVI EVERDFKLFI
     ELFDVKLQML GIHQLQNAAT ATCVALCLRD KGWRISDESI HAGLEHAYLL GRSQFLTSTE
     AETLGLPGAT IMLDGAHTKE SAKALVDTIQ MTFPEARLAL IVAMASDKDH MAFAREFLSG
     GQLEAVFLTE VNIAGAKSRT TSASMLRDCW IQASKELGIN TLHDGMEEYQ KLFENQSFCS
     AGESKHKTIL AAENSLLVSL RVGNQILRAR TRDQTSIIVI TGSLHIVSTV LSSLLG
//
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