node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
D7SWB0_VITVI | D7TF34_VITVI | D7SWB0 | D7TF34 | SH3 domain-containing protein. | CS domain-containing protein. | 0.766 |
D7SWB0_VITVI | D7TFR8_VITVI | D7SWB0 | D7TFR8 | SH3 domain-containing protein. | CS domain-containing protein. | 0.766 |
D7SWB0_VITVI | D7TFR9_VITVI | D7SWB0 | D7TFR9 | SH3 domain-containing protein. | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | 0.499 |
D7SWB0_VITVI | D7THE7_VITVI | D7SWB0 | D7THE7 | SH3 domain-containing protein. | Peptidylprolyl isomerase. | 0.530 |
D7SWB0_VITVI | F6HZ37_VITVI | D7SWB0 | F6HZ37 | SH3 domain-containing protein. | CS domain-containing protein. | 0.766 |
D7TF34_VITVI | D7SWB0_VITVI | D7TF34 | D7SWB0 | CS domain-containing protein. | SH3 domain-containing protein. | 0.766 |
D7TF34_VITVI | D7THE7_VITVI | D7TF34 | D7THE7 | CS domain-containing protein. | Peptidylprolyl isomerase. | 0.610 |
D7TFR8_VITVI | D7SWB0_VITVI | D7TFR8 | D7SWB0 | CS domain-containing protein. | SH3 domain-containing protein. | 0.766 |
D7TFR8_VITVI | D7THE7_VITVI | D7TFR8 | D7THE7 | CS domain-containing protein. | Peptidylprolyl isomerase. | 0.610 |
D7TFR9_VITVI | D7SWB0_VITVI | D7TFR9 | D7SWB0 | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | SH3 domain-containing protein. | 0.499 |
D7TFR9_VITVI | D7THE7_VITVI | D7TFR9 | D7THE7 | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Peptidylprolyl isomerase. | 0.505 |
D7THE7_VITVI | D7SWB0_VITVI | D7THE7 | D7SWB0 | Peptidylprolyl isomerase. | SH3 domain-containing protein. | 0.530 |
D7THE7_VITVI | D7TF34_VITVI | D7THE7 | D7TF34 | Peptidylprolyl isomerase. | CS domain-containing protein. | 0.610 |
D7THE7_VITVI | D7TFR8_VITVI | D7THE7 | D7TFR8 | Peptidylprolyl isomerase. | CS domain-containing protein. | 0.610 |
D7THE7_VITVI | D7TFR9_VITVI | D7THE7 | D7TFR9 | Peptidylprolyl isomerase. | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | 0.505 |
D7THE7_VITVI | D7U6A1_VITVI | D7THE7 | D7U6A1 | Peptidylprolyl isomerase. | Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors [...] | 0.947 |
D7THE7_VITVI | E0CRP9_VITVI | D7THE7 | E0CRP9 | Peptidylprolyl isomerase. | Queuine tRNA-ribosyltransferase catalytic subunit 1; Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, formi [...] | 0.500 |
D7THE7_VITVI | F6GTR9_VITVI | D7THE7 | F6GTR9 | Peptidylprolyl isomerase. | Uncharacterized protein. | 0.593 |
D7THE7_VITVI | F6GVK2_VITVI | D7THE7 | F6GVK2 | Peptidylprolyl isomerase. | Uncharacterized protein; Belongs to the short-chain dehydrogenases/reductases (SDR) family. | 0.889 |
D7THE7_VITVI | F6HZ37_VITVI | D7THE7 | F6HZ37 | Peptidylprolyl isomerase. | CS domain-containing protein. | 0.610 |