| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SPBC2D10.07c.1 | SPBC336.13c.1 | SPBC2D10.07c.1 | SPBC336.13c.1 | mitochondrial inner membrane peptidase complex catalytic subunit (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | mitochondrial inner membrane peptidase complex catalytic subunit 2 (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | 0.970 |
| SPBC2D10.07c.1 | sec11 | SPBC2D10.07c.1 | SPBC1685.03.1 | mitochondrial inner membrane peptidase complex catalytic subunit (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | 0.572 |
| SPBC2D10.07c.1 | spc2 | SPBC2D10.07c.1 | SPAC1071.04c.1 | mitochondrial inner membrane peptidase complex catalytic subunit (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | signal peptidase subunit Spc2 (predicted); Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. Spc2 enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity) | 0.479 |
| SPBC2D10.07c.1 | spc3 | SPBC2D10.07c.1 | SPAC56F8.11.1 | mitochondrial inner membrane peptidase complex catalytic subunit (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | signal peptidase subunit Spc3 (predicted); Microsomal signal peptidase is a membrane-bound endoproteinase that removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) | 0.574 |
| SPBC336.13c.1 | SPBC2D10.07c.1 | SPBC336.13c.1 | SPBC2D10.07c.1 | mitochondrial inner membrane peptidase complex catalytic subunit 2 (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | mitochondrial inner membrane peptidase complex catalytic subunit (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | 0.970 |
| SPBC336.13c.1 | spc2 | SPBC336.13c.1 | SPAC1071.04c.1 | mitochondrial inner membrane peptidase complex catalytic subunit 2 (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | signal peptidase subunit Spc2 (predicted); Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. Spc2 enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity) | 0.479 |
| SPBC336.13c.1 | spc3 | SPBC336.13c.1 | SPAC56F8.11.1 | mitochondrial inner membrane peptidase complex catalytic subunit 2 (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | signal peptidase subunit Spc3 (predicted); Microsomal signal peptidase is a membrane-bound endoproteinase that removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) | 0.574 |
| SPCC1281.06c.1 | sec11 | SPCC1281.06c.1 | SPBC1685.03.1 | acyl-coA desaturase (predicted); Utilizes O(2) and electrons from the reduced cytochrome b(5) domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates (By similarity) | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | 0.773 |
| SPCC1281.06c.1 | spc2 | SPCC1281.06c.1 | SPAC1071.04c.1 | acyl-coA desaturase (predicted); Utilizes O(2) and electrons from the reduced cytochrome b(5) domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates (By similarity) | signal peptidase subunit Spc2 (predicted); Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. Spc2 enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity) | 0.856 |
| SPCC1281.06c.1 | spc3 | SPCC1281.06c.1 | SPAC56F8.11.1 | acyl-coA desaturase (predicted); Utilizes O(2) and electrons from the reduced cytochrome b(5) domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates (By similarity) | signal peptidase subunit Spc3 (predicted); Microsomal signal peptidase is a membrane-bound endoproteinase that removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) | 0.886 |
| SPCC1281.06c.1 | ubi4 | SPCC1281.06c.1 | SPBC337.08c.1 | acyl-coA desaturase (predicted); Utilizes O(2) and electrons from the reduced cytochrome b(5) domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates (By similarity) | ubiquitin; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked- Lys-6-linked may be involved in DNA repair; Lys-11- [...] | 0.932 |
| arc5 | spc3 | SPAC17G8.04c.1 | SPAC56F8.11.1 | ARP2/3 actin-organizing complex subunit Arc5; Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks (By similarity) | signal peptidase subunit Spc3 (predicted); Microsomal signal peptidase is a membrane-bound endoproteinase that removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) | 0.606 |
| sbh1 | sec11 | SPBC2G2.03c.1 | SPBC1685.03.1 | translocon beta subunit Sbh1 (predicted); Necessary for protein translocation in the endoplasmic reticulum (By similarity) | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | 0.999 |
| sbh1 | spc3 | SPBC2G2.03c.1 | SPAC56F8.11.1 | translocon beta subunit Sbh1 (predicted); Necessary for protein translocation in the endoplasmic reticulum (By similarity) | signal peptidase subunit Spc3 (predicted); Microsomal signal peptidase is a membrane-bound endoproteinase that removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) | 0.606 |
| sec11 | SPBC2D10.07c.1 | SPBC1685.03.1 | SPBC2D10.07c.1 | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | mitochondrial inner membrane peptidase complex catalytic subunit (predicted); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space (By similarity) | 0.572 |
| sec11 | SPCC1281.06c.1 | SPBC1685.03.1 | SPCC1281.06c.1 | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | acyl-coA desaturase (predicted); Utilizes O(2) and electrons from the reduced cytochrome b(5) domain to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates (By similarity) | 0.773 |
| sec11 | sbh1 | SPBC1685.03.1 | SPBC2G2.03c.1 | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | translocon beta subunit Sbh1 (predicted); Necessary for protein translocation in the endoplasmic reticulum (By similarity) | 0.999 |
| sec11 | spc2 | SPBC1685.03.1 | SPAC1071.04c.1 | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | signal peptidase subunit Spc2 (predicted); Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. Spc2 enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity) | 0.848 |
| sec11 | spc3 | SPBC1685.03.1 | SPAC56F8.11.1 | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | signal peptidase subunit Spc3 (predicted); Microsomal signal peptidase is a membrane-bound endoproteinase that removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) | 0.993 |
| sec11 | ubi4 | SPBC1685.03.1 | SPBC337.08c.1 | signal peptidase subunit Sec11 (predicted); Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | ubiquitin; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked- Lys-6-linked may be involved in DNA repair; Lys-11- [...] | 0.882 |
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