node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CPE0450 | CPE0451 | gene:10489706 | gene:10489707 | Hypothetical protein; 107 aa, no significant homology. | Conserved hypothetical protein; 130 aa, similar to sp:YWKD_BACSU HYPOTHETICAL 14.8 KDA PROTEIN IN TDK-PRFA INTERGENIC REGION from Bacillus subtilis (128 aa); 64.3% identity in 126 aa overlap. | 0.510 |
CPE0450 | CPE1218 | gene:10489706 | gene:10490481 | Hypothetical protein; 107 aa, no significant homology. | Probable ABC transporter; 333 aa, similar to pir:G70046 iron-binding protein homolog yvrC from Bacillus subtilis (314 aa); 25.8% identity in 229 aa overlap; binding protein. | 0.459 |
CPE0450 | CPE2107 | gene:10489706 | gene:10491377 | Hypothetical protein; 107 aa, no significant homology. | Hypothetical protein; 1081 aa, partially similar to pir:T28317 ORF MSV156 hypothetical protein from Melanoplus sanguinipes entomopoxvirus (1127 aa); 21% identity in 675 aa overlap. | 0.541 |
CPE0450 | colA | gene:10489706 | gene:10489417 | Hypothetical protein; 107 aa, no significant homology. | Collagenase; Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity). | 0.488 |
CPE0450 | dchS | gene:10489706 | gene:10489646 | Hypothetical protein; 107 aa, no significant homology. | 320 aa, similar to pir:DCCLHP histidine decarboxylase (EC 4.1.1.22) precursor from Clostridium perfringens (320 aa); 99.7% identity in 320 aa overlap; CPE0390. | 0.448 |
CPE0451 | CPE0450 | gene:10489707 | gene:10489706 | Conserved hypothetical protein; 130 aa, similar to sp:YWKD_BACSU HYPOTHETICAL 14.8 KDA PROTEIN IN TDK-PRFA INTERGENIC REGION from Bacillus subtilis (128 aa); 64.3% identity in 126 aa overlap. | Hypothetical protein; 107 aa, no significant homology. | 0.510 |
CPE1218 | CPE0450 | gene:10490481 | gene:10489706 | Probable ABC transporter; 333 aa, similar to pir:G70046 iron-binding protein homolog yvrC from Bacillus subtilis (314 aa); 25.8% identity in 229 aa overlap; binding protein. | Hypothetical protein; 107 aa, no significant homology. | 0.459 |
CPE2107 | CPE0450 | gene:10491377 | gene:10489706 | Hypothetical protein; 1081 aa, partially similar to pir:T28317 ORF MSV156 hypothetical protein from Melanoplus sanguinipes entomopoxvirus (1127 aa); 21% identity in 675 aa overlap. | Hypothetical protein; 107 aa, no significant homology. | 0.541 |
CPE2107 | colA | gene:10491377 | gene:10489417 | Hypothetical protein; 1081 aa, partially similar to pir:T28317 ORF MSV156 hypothetical protein from Melanoplus sanguinipes entomopoxvirus (1127 aa); 21% identity in 675 aa overlap. | Collagenase; Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity). | 0.673 |
CPE2107 | dchS | gene:10491377 | gene:10489646 | Hypothetical protein; 1081 aa, partially similar to pir:T28317 ORF MSV156 hypothetical protein from Melanoplus sanguinipes entomopoxvirus (1127 aa); 21% identity in 675 aa overlap. | 320 aa, similar to pir:DCCLHP histidine decarboxylase (EC 4.1.1.22) precursor from Clostridium perfringens (320 aa); 99.7% identity in 320 aa overlap; CPE0390. | 0.736 |
colA | CPE0450 | gene:10489417 | gene:10489706 | Collagenase; Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity). | Hypothetical protein; 107 aa, no significant homology. | 0.488 |
colA | CPE2107 | gene:10489417 | gene:10491377 | Collagenase; Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity). | Hypothetical protein; 1081 aa, partially similar to pir:T28317 ORF MSV156 hypothetical protein from Melanoplus sanguinipes entomopoxvirus (1127 aa); 21% identity in 675 aa overlap. | 0.673 |
colA | dchS | gene:10489417 | gene:10489646 | Collagenase; Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity). | 320 aa, similar to pir:DCCLHP histidine decarboxylase (EC 4.1.1.22) precursor from Clostridium perfringens (320 aa); 99.7% identity in 320 aa overlap; CPE0390. | 0.462 |
dchS | CPE0450 | gene:10489646 | gene:10489706 | 320 aa, similar to pir:DCCLHP histidine decarboxylase (EC 4.1.1.22) precursor from Clostridium perfringens (320 aa); 99.7% identity in 320 aa overlap; CPE0390. | Hypothetical protein; 107 aa, no significant homology. | 0.448 |
dchS | CPE2107 | gene:10489646 | gene:10491377 | 320 aa, similar to pir:DCCLHP histidine decarboxylase (EC 4.1.1.22) precursor from Clostridium perfringens (320 aa); 99.7% identity in 320 aa overlap; CPE0390. | Hypothetical protein; 1081 aa, partially similar to pir:T28317 ORF MSV156 hypothetical protein from Melanoplus sanguinipes entomopoxvirus (1127 aa); 21% identity in 675 aa overlap. | 0.736 |
dchS | colA | gene:10489646 | gene:10489417 | 320 aa, similar to pir:DCCLHP histidine decarboxylase (EC 4.1.1.22) precursor from Clostridium perfringens (320 aa); 99.7% identity in 320 aa overlap; CPE0390. | Collagenase; Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity). | 0.462 |