Value | Algorithm | Source | Identity | Coverage | Bit score | Evalue | Cross references |
---|---|---|---|---|---|---|---|
UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase | similarity |
KEGG
DB: KEGG |
28.6 | 447.0 | 162 | 3.10e-37 | sbe:RAAC3_TM7C01G0943 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase n=1 Tax=Clostridium botulinum D str. 1873 RepID=C5VT27_CLOBO (db=UNIREF evalue=5.0e-27 bit_score=126.0 identity=28.54 coverage=78.0542986425339) | similarity |
UNIREF
DB: UNIREF |
28.54 | 78.05 | 126 | 5.00e-27 | sbe:RAAC3_TM7C01G0943 |
seg (db=Seg db_id=seg from=417 to=427) | iprscan |
interpro
DB: Seg |
null | null | null | null | sbe:RAAC3_TM7C01G0943 |
seg (db=Seg db_id=seg from=185 to=201) | iprscan |
interpro
DB: Seg |
null | null | null | null | sbe:RAAC3_TM7C01G0943 |
MUR LIGASE FAMILY MEMBER (db=HMMPanther db_id=PTHR23135 from=31 to=423 evalue=1.1e-40) | iprscan |
interpro
DB: HMMPanther |
null | null | null | 1.10e-40 | sbe:RAAC3_TM7C01G0943 |
UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE--D-ALANYL-D- ALANYL LIGASE (db=HMMPanther db_id=PTHR23135:SF3 from=31 to=423 evalue=1.1e-40 interpro_id=IPR005863 interpro_description=UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase GO=Molecular Function: ATP binding (GO:0005524), Cellular Component: cytoplasm (GO:0005737), Biological Process: regulation of cell shape (GO:0008360), Molecular Function: UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activ | iprscan |
interpro
DB: HMMPanther |
null | null | null | 1.10e-40 | sbe:RAAC3_TM7C01G0943 |
MurD-like peptide ligases, peptide-binding domain (db=superfamily db_id=SSF53244 from=279 to=418 evalue=1.8e-24 interpro_id=IPR004101 interpro_description=Mur ligase, C-terminal GO=Molecular Function: ATP binding (GO:0005524), Biological Process: biosynthetic process (GO:0009058), Molecular Function: ligase activity (GO:0016874)) | iprscan |
interpro
DB: superfamily |
null | null | null | 1.80e-24 | sbe:RAAC3_TM7C01G0943 |
no description (db=Gene3D db_id=G3DSA:3.90.190.20 from=278 to=423 evalue=9.4e-20 interpro_id=IPR004101 interpro_description=Mur ligase, C-terminal GO=Molecular Function: ATP binding (GO:0005524), Biological Process: biosynthetic process (GO:0009058), Molecular Function: ligase activity (GO:0016874)) | iprscan |
interpro
DB: Gene3D |
null | null | null | 9.40e-20 | sbe:RAAC3_TM7C01G0943 |
no description (db=Gene3D db_id=G3DSA:3.40.1190.10 from=7 to=277 evalue=1.2e-19 interpro_id=IPR013221 interpro_description=Mur ligase, central GO=Molecular Function: ATP binding (GO:0005524), Biological Process: biosynthetic process (GO:0009058)) | iprscan |
interpro
DB: Gene3D |
null | null | null | 1.20e-19 | sbe:RAAC3_TM7C01G0943 |
MurD-like peptide ligases, catalytic domain (db=superfamily db_id=SSF53623 from=25 to=274 evalue=3.5e-19 interpro_id=IPR013221 interpro_description=Mur ligase, central GO=Molecular Function: ATP binding (GO:0005524), Biological Process: biosynthetic process (GO:0009058)) | iprscan |
interpro
DB: superfamily |
null | null | null | 3.50e-19 | sbe:RAAC3_TM7C01G0943 |
Mur_ligase_M (db=HMMPfam db_id=PF08245 from=31 to=239 evalue=4.3e-13 interpro_id=IPR013221 interpro_description=Mur ligase, central GO=Molecular Function: ATP binding (GO:0005524), Biological Process: biosynthetic process (GO:0009058)) | iprscan |
interpro
DB: HMMPfam |
null | null | null | 4.30e-13 | sbe:RAAC3_TM7C01G0943 |
Mur_ligase_C (db=HMMPfam db_id=PF02875 from=280 to=357 evalue=9.9e-08 interpro_id=IPR004101 interpro_description=Mur ligase, C-terminal GO=Molecular Function: ATP binding (GO:0005524), Biological Process: biosynthetic process (GO:0009058), Molecular Function: ligase activity (GO:0016874)) | iprscan |
interpro
DB: HMMPfam |
null | null | null | 9.90e-08 | sbe:RAAC3_TM7C01G0943 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase {ECO:0000256|RuleBase:RU004136}; EC=6.3.2.10 {ECO:0000256|RuleBase:RU004136};; TaxID=77133 species="Bacteria; environmental samples.;" source |
UNIPROT
DB: UniProtKB |
100.0 | 441.0 | 856 | 1.30e-245 | K2BZR0_9BACT |