node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CAZ95732.1 | CAZ95733.1 | ZOBELLIA_1678 | ZOBELLIA_1679 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.854 |
CAZ95732.1 | CAZ95735.1 | ZOBELLIA_1678 | ZOBELLIA_1681 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | 0.458 |
CAZ95732.1 | CAZ95736.1 | ZOBELLIA_1678 | ZOBELLIA_1682 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Glyoxalase superfamily protein; Family membership. | 0.404 |
CAZ95732.1 | rnpA | ZOBELLIA_1678 | ZOBELLIA_1680 | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.564 |
CAZ95733.1 | CAZ95732.1 | ZOBELLIA_1679 | ZOBELLIA_1678 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | 0.854 |
CAZ95733.1 | CAZ95735.1 | ZOBELLIA_1679 | ZOBELLIA_1681 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | 0.484 |
CAZ95733.1 | CAZ95736.1 | ZOBELLIA_1679 | ZOBELLIA_1682 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Glyoxalase superfamily protein; Family membership. | 0.417 |
CAZ95733.1 | rnpA | ZOBELLIA_1679 | ZOBELLIA_1680 | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.599 |
CAZ95735.1 | CAZ95732.1 | ZOBELLIA_1681 | ZOBELLIA_1678 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | 0.458 |
CAZ95735.1 | CAZ95733.1 | ZOBELLIA_1681 | ZOBELLIA_1679 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.484 |
CAZ95735.1 | CAZ95736.1 | ZOBELLIA_1681 | ZOBELLIA_1682 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Glyoxalase superfamily protein; Family membership. | 0.701 |
CAZ95735.1 | CAZ95768.1 | ZOBELLIA_1681 | ZOBELLIA_1715 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Conserved hypothetical membrane protein; Contains three transmembrane helices in the N-terminal region; Localized in the cytoplasmic membrane; Conserved hypothetical protein. | 0.502 |
CAZ95735.1 | CAZ95778.1 | ZOBELLIA_1681 | ZOBELLIA_1725 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Lytic murein transglycosylase, family GH23; Lytic murein transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N- acetylmuramic acid and N-acetylglucosamine residues, thereby conserving the energy in a newly synthesized 1,6- anhydrobond in the muramic acid residue. May play a role in recycling of muropeptides during cell elongation and/or cell division; Contains a N-terminal catalytic module belonging to the family 23 of the glycoside hydrolases (GH23) and two C-terminal LysM domains, predicted to bind peptidoglycans and belonging to the family 50 of the carbo [...] | 0.473 |
CAZ95735.1 | CAZ96289.1 | ZOBELLIA_1681 | ZOBELLIA_2131 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | TPR repeats protein; Protein containing six tetratrico peptide repeats (TPR). TPR repeats mediate proteinprotein interactions and the assembly of multiprotein complexes; Signal peptide cleaved between the residues 18 and 19; Localized in the periplasmic space; Function unclear. | 0.562 |
CAZ95735.1 | CAZ97869.1 | ZOBELLIA_1681 | ZOBELLIA_3731 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 21 and 22; Localized in the periplasmic space; Conserved hypothetical protein. | 0.438 |
CAZ95735.1 | CAZ98217.1 | ZOBELLIA_1681 | ZOBELLIA_4081 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Membrane protein displaying a domain of unknown function DUF1550; Contains two N-terminal transmembrane helices; Localized in the cytoplasmic membrane; Family membership. | 0.479 |
CAZ95735.1 | furA1 | ZOBELLIA_1681 | ZOBELLIA_3675 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Ferric uptake regulation protein is a transcriptional regulator that acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed metal ion-responsive genes. It regulates the expression of several outer- membrane proteins including the iron transport operon; Contains a N-terminal Fur-type HTH DNA-binding domain; Belongs to the Fur family; Localized in the cytoplasm; High confidence in function and specificity. | 0.424 |
CAZ95735.1 | rnpA | ZOBELLIA_1681 | ZOBELLIA_1680 | Carboxy-terminal processing peptidase, family S41; This enzyme is a modular protein with a N-terminal PDZ domain, a central carboxy-terminal processing peptidase and a C-terminal domain of unknown function. The catalytic module belongs to the family S41 of the peptidase. It shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C- terminus. PDZ domains are multifunctional protein-protein interaction modules. In many cases, PDZ dom [...] | Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. | 0.672 |
CAZ95736.1 | CAZ95732.1 | ZOBELLIA_1682 | ZOBELLIA_1678 | Glyoxalase superfamily protein; Family membership. | Serine endopeptidase, family S8; The Serine endopeptidases use a catalytic serine residue as a nucleophile and form an acyl intermediate. These peptidases can also readily act as transferases; Belongs to the families S8 of peptidases, clan SB; Contains a prokaryotic lipoprotein signal peptide cleaved between the residues 20 and 21; Localized in the cytoplasmic and/or outer membrane; Family membership. | 0.404 |
CAZ95736.1 | CAZ95733.1 | ZOBELLIA_1682 | ZOBELLIA_1679 | Glyoxalase superfamily protein; Family membership. | Aminopeptidase, family M1; Aminopeptidase catalyzes the hydrolysis of N-terminal amino-acid residues from oligopeptides or polypeptides. This enzyme belongs to the family M1 of the peptidases. A catalytic zinc ion is bound by two histidines and a glutamate. The histidines are within an 'HEXXH' motif on one long helix with the glutamate on another antiparallel helix. The catalytic mechanism is believed to involve activation of a water molecule by the zinc ion. The glutamate of the HEXXH motif is known to be important for catalysis and a tyrosine may also be involved. Features a signal p [...] | 0.417 |