RANBP2-like and GRIP domain-containing protein 1 isoform X2 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| RanBD3_RanBP2-like | cd14685 | Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 8.49e-82 | ||||
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy. : Pssm-ID: 270204 Cd Length: 117 Bit Score: 263.75 E-value: 8.49e-82
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| RanBD2_RanBP2-like | cd13177 | Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 3.58e-77 | ||||
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy. : Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 250.73 E-value: 3.58e-77
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| Apc1_MidN super family | cl48671 | Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ... |
1-66 | 1.93e-19 | ||||
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich. The actual alignment was detected with superfamily member pfam20518: Pssm-ID: 466667 Cd Length: 371 Bit Score: 92.47 E-value: 1.93e-19
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
49-238 | 5.71e-14 | ||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; : Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 74.00 E-value: 5.71e-14
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| PRK08581 super family | cl35718 | amidase domain-containing protein; |
1514-1690 | 2.81e-03 | ||||
amidase domain-containing protein; The actual alignment was detected with superfamily member PRK08581: Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 42.47 E-value: 2.81e-03
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| Name | Accession | Description | Interval | E-value | ||||
| RanBD3_RanBP2-like | cd14685 | Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 8.49e-82 | ||||
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy. Pssm-ID: 270204 Cd Length: 117 Bit Score: 263.75 E-value: 8.49e-82
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| RanBD2_RanBP2-like | cd13177 | Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 3.58e-77 | ||||
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy. Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 250.73 E-value: 3.58e-77
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| RanBD | smart00160 | Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ... |
1344-1473 | 3.70e-64 | ||||
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase). Pssm-ID: 197549 Cd Length: 130 Bit Score: 213.79 E-value: 3.70e-64
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| Ran_BP1 | pfam00638 | RanBP1 domain; |
1355-1476 | 8.01e-64 | ||||
RanBP1 domain; Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 212.67 E-value: 8.01e-64
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| Ran_BP1 | pfam00638 | RanBP1 domain; |
1058-1179 | 6.65e-62 | ||||
RanBP1 domain; Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 206.90 E-value: 6.65e-62
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| RanBD | smart00160 | Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ... |
1047-1176 | 2.14e-48 | ||||
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase). Pssm-ID: 197549 Cd Length: 130 Bit Score: 168.72 E-value: 2.14e-48
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| YRB1 | COG5171 | Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; |
985-1177 | 2.54e-43 | ||||
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; Pssm-ID: 227499 Cd Length: 211 Bit Score: 157.49 E-value: 2.54e-43
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| YRB1 | COG5171 | Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; |
1317-1479 | 1.29e-38 | ||||
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; Pssm-ID: 227499 Cd Length: 211 Bit Score: 144.01 E-value: 1.29e-38
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| Apc1_MidN | pfam20518 | Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ... |
1-66 | 1.93e-19 | ||||
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich. Pssm-ID: 466667 Cd Length: 371 Bit Score: 92.47 E-value: 1.93e-19
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
49-238 | 5.71e-14 | ||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 74.00 E-value: 5.71e-14
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| TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
76-107 | 2.70e-05 | ||||
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism. Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 42.43 E-value: 2.70e-05
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| TPR_1 | pfam00515 | Tetratricopeptide repeat; |
76-107 | 3.91e-05 | ||||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 42.02 E-value: 3.91e-05
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| ACL4-like | cd24142 | Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
49-107 | 2.07e-03 | ||||
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present. Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 42.23 E-value: 2.07e-03
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| PRK08581 | PRK08581 | amidase domain-containing protein; |
1514-1690 | 2.81e-03 | ||||
amidase domain-containing protein; Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 42.47 E-value: 2.81e-03
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| Name | Accession | Description | Interval | E-value | |||||
| RanBD3_RanBP2-like | cd14685 | Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 8.49e-82 | |||||
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy. Pssm-ID: 270204 Cd Length: 117 Bit Score: 263.75 E-value: 8.49e-82
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| RanBD2_RanBP2-like | cd13177 | Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 3.58e-77 | |||||
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy. Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 250.73 E-value: 3.58e-77
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| RanBD_RanBP2-like | cd13176 | Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ... |
1358-1474 | 1.74e-71 | |||||
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy. Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 234.09 E-value: 1.74e-71
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| RanBD_RanBP2-like | cd13176 | Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ... |
1061-1177 | 6.43e-68 | |||||
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy. Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 224.08 E-value: 6.43e-68
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| RanBD | smart00160 | Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ... |
1344-1473 | 3.70e-64 | |||||
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase). Pssm-ID: 197549 Cd Length: 130 Bit Score: 213.79 E-value: 3.70e-64
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| Ran_BP1 | pfam00638 | RanBP1 domain; |
1355-1476 | 8.01e-64 | |||||
RanBP1 domain; Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 212.67 E-value: 8.01e-64
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| Ran_BP1 | pfam00638 | RanBP1 domain; |
1058-1179 | 6.65e-62 | |||||
RanBP1 domain; Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 206.90 E-value: 6.65e-62
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| RanBD_RanBP1 | cd13179 | Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ... |
1044-1177 | 5.38e-57 | |||||
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 193.55 E-value: 5.38e-57
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| RanBD_RanBP1 | cd13179 | Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ... |
1343-1474 | 8.24e-57 | |||||
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 193.17 E-value: 8.24e-57
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| RanBD_family | cd00835 | Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ... |
1358-1474 | 1.14e-53 | |||||
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins. Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 183.18 E-value: 1.14e-53
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| RanBD_family | cd00835 | Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ... |
1061-1177 | 3.58e-51 | |||||
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins. Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 176.25 E-value: 3.58e-51
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| RanBD3_RanBP2-like | cd14685 | Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 6.14e-51 | |||||
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy. Pssm-ID: 270204 Cd Length: 117 Bit Score: 175.54 E-value: 6.14e-51
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| RanBD4_RanBP2-like | cd13178 | Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 1.83e-50 | |||||
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy. Pssm-ID: 269999 Cd Length: 117 Bit Score: 173.99 E-value: 1.83e-50
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| RanBD4_RanBP2-like | cd13178 | Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 1.75e-48 | |||||
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy. Pssm-ID: 269999 Cd Length: 117 Bit Score: 168.59 E-value: 1.75e-48
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| RanBD | smart00160 | Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ... |
1047-1176 | 2.14e-48 | |||||
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase). Pssm-ID: 197549 Cd Length: 130 Bit Score: 168.72 E-value: 2.14e-48
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| RanBD1_RanBP2-like | cd14684 | Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 2.64e-46 | |||||
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy. Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 162.12 E-value: 2.64e-46
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| RanBD2_RanBP2-like | cd13177 | Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 4.45e-44 | |||||
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy. Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 155.98 E-value: 4.45e-44
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| YRB1 | COG5171 | Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; |
985-1177 | 2.54e-43 | |||||
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; Pssm-ID: 227499 Cd Length: 211 Bit Score: 157.49 E-value: 2.54e-43
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| RanBD2_RanBP2_insect-like | cd13172 | Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 3.95e-43 | |||||
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 2 is present in this hierarchy. Pssm-ID: 269993 Cd Length: 118 Bit Score: 153.38 E-value: 3.95e-43
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| RanBD2_RanBP2_insect-like | cd13172 | Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 5.26e-42 | |||||
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 2 is present in this hierarchy. Pssm-ID: 269993 Cd Length: 118 Bit Score: 149.91 E-value: 5.26e-42
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| RanBD1_RanBP2-like | cd14684 | Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 1.62e-40 | |||||
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy. Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 145.56 E-value: 1.62e-40
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| RanBD3_RanBP2_insect-like | cd13173 | Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 1.64e-40 | |||||
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy. Pssm-ID: 269994 Cd Length: 115 Bit Score: 145.70 E-value: 1.64e-40
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| RanBD1_RanBP2_insect-like | cd13171 | Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1175 | 2.07e-40 | |||||
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy. Pssm-ID: 269992 Cd Length: 117 Bit Score: 145.30 E-value: 2.07e-40
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| RanBD1_RanBP2_insect-like | cd13171 | Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ... |
1358-1474 | 2.10e-39 | |||||
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy. Pssm-ID: 269992 Cd Length: 117 Bit Score: 142.61 E-value: 2.10e-39
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| YRB1 | COG5171 | Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; |
1317-1479 | 1.29e-38 | |||||
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]; Pssm-ID: 227499 Cd Length: 211 Bit Score: 144.01 E-value: 1.29e-38
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| RanBD3_RanBP2_insect-like | cd13173 | Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1175 | 1.72e-36 | |||||
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy. Pssm-ID: 269994 Cd Length: 115 Bit Score: 134.15 E-value: 1.72e-36
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| RanBD4_RanBP2_insect-like | cd13174 | Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ... |
1061-1177 | 7.66e-36 | |||||
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy. Pssm-ID: 269995 Cd Length: 118 Bit Score: 132.53 E-value: 7.66e-36
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| RanBD4_RanBP2_insect-like | cd13174 | Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ... |
1359-1473 | 1.58e-34 | |||||
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy. Pssm-ID: 269995 Cd Length: 118 Bit Score: 128.68 E-value: 1.58e-34
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| Apc1_MidN | pfam20518 | Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ... |
1-66 | 1.93e-19 | |||||
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich. Pssm-ID: 466667 Cd Length: 371 Bit Score: 92.47 E-value: 1.93e-19
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| RanBD_NUP50_plant | cd13169 | Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ... |
1358-1474 | 9.26e-17 | |||||
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP#importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The first RanBD2 is present in this hierarchy. Pssm-ID: 269990 Cd Length: 117 Bit Score: 77.87 E-value: 9.26e-17
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| RanBD_NUP50 | cd13170 | Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ... |
1061-1177 | 1.30e-16 | |||||
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 269991 Cd Length: 111 Bit Score: 77.26 E-value: 1.30e-16
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| RanBD_NUP50 | cd13170 | Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ... |
1359-1474 | 4.14e-15 | |||||
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 269991 Cd Length: 111 Bit Score: 73.02 E-value: 4.14e-15
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| RanBD_RanBP3 | cd13180 | Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ... |
1061-1133 | 9.90e-15 | |||||
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 270001 Cd Length: 113 Bit Score: 71.88 E-value: 9.90e-15
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| RanBD_RanBP3 | cd13180 | Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ... |
1358-1469 | 1.17e-14 | |||||
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 270001 Cd Length: 113 Bit Score: 71.88 E-value: 1.17e-14
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
49-238 | 5.71e-14 | |||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 74.00 E-value: 5.71e-14
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| RanBD_NUP2 | cd13181 | Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ... |
1061-1177 | 1.34e-13 | |||||
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 270002 Cd Length: 115 Bit Score: 68.62 E-value: 1.34e-13
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| RanBD_NUP50_plant | cd13169 | Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ... |
1061-1175 | 3.07e-13 | |||||
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP#importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The first RanBD2 is present in this hierarchy. Pssm-ID: 269990 Cd Length: 117 Bit Score: 67.86 E-value: 3.07e-13
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| LapB | COG2956 | Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
45-277 | 1.50e-11 | |||||
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 67.06 E-value: 1.50e-11
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| RanBD_NUP2 | cd13181 | Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ... |
1358-1474 | 2.56e-11 | |||||
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. Pssm-ID: 270002 Cd Length: 115 Bit Score: 62.07 E-value: 2.56e-11
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
46-155 | 1.81e-10 | |||||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 60.59 E-value: 1.81e-10
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
46-276 | 7.69e-10 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 61.18 E-value: 7.69e-10
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
75-148 | 1.18e-07 | |||||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 52.32 E-value: 1.18e-07
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
69-315 | 1.60e-07 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 54.24 E-value: 1.60e-07
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
51-142 | 3.99e-07 | |||||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 51.50 E-value: 3.99e-07
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| TPR | COG0457 | Tetratricopeptide (TPR) repeat [General function prediction only]; |
49-210 | 8.75e-07 | |||||
Tetratricopeptide (TPR) repeat [General function prediction only]; Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 51.93 E-value: 8.75e-07
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
51-142 | 1.03e-06 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 48.63 E-value: 1.03e-06
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
47-142 | 1.60e-06 | |||||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 49.42 E-value: 1.60e-06
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
46-107 | 4.40e-06 | |||||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 47.88 E-value: 4.40e-06
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| NrfG | COG4235 | Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
46-114 | 6.04e-06 | |||||
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 47.31 E-value: 6.04e-06
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
49-107 | 1.50e-05 | |||||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 46.88 E-value: 1.50e-05
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| TPR | smart00028 | Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
76-107 | 2.70e-05 | |||||
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism. Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 42.43 E-value: 2.70e-05
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| TPR_1 | pfam00515 | Tetratricopeptide repeat; |
76-107 | 3.91e-05 | |||||
Tetratricopeptide repeat; Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 42.02 E-value: 3.91e-05
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| Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
48-148 | 5.44e-05 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 48.07 E-value: 5.44e-05
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| Spy | COG3914 | Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
46-191 | 6.62e-05 | |||||
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 47.68 E-value: 6.62e-05
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
49-107 | 7.29e-05 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 43.24 E-value: 7.29e-05
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| HemYx | COG3071 | Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ... |
49-105 | 1.01e-04 | |||||
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown]; Pssm-ID: 442305 [Multi-domain] Cd Length: 323 Bit Score: 46.44 E-value: 1.01e-04
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| TPR_2 | pfam07719 | Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ... |
76-107 | 1.59e-04 | |||||
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515. Pssm-ID: 429619 [Multi-domain] Cd Length: 33 Bit Score: 40.20 E-value: 1.59e-04
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| BepA | COG4783 | Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
73-207 | 2.52e-04 | |||||
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 42.87 E-value: 2.52e-04
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| CpoB | COG1729 | Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
50-154 | 3.17e-04 | |||||
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 41.90 E-value: 3.17e-04
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| RanBD5_RanBP2_insect-like | cd13175 | Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase ... |
1360-1474 | 7.98e-04 | |||||
Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 5 is present in this hierarchy. Pssm-ID: 269996 Cd Length: 114 Bit Score: 40.98 E-value: 7.98e-04
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| PilF | COG3063 | Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
85-160 | 1.32e-03 | |||||
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 39.77 E-value: 1.32e-03
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| NlpI | COG4785 | Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
51-107 | 1.76e-03 | |||||
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 41.82 E-value: 1.76e-03
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| TadD | COG5010 | Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
40-148 | 1.90e-03 | |||||
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 40.71 E-value: 1.90e-03
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| ACL4-like | cd24142 | Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ... |
49-107 | 2.07e-03 | |||||
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present. Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 42.23 E-value: 2.07e-03
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| PRK08581 | PRK08581 | amidase domain-containing protein; |
1514-1690 | 2.81e-03 | |||||
amidase domain-containing protein; Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 42.47 E-value: 2.81e-03
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| TPR_8 | pfam13181 | Tetratricopeptide repeat; |
82-107 | 9.97e-03 | |||||
Tetratricopeptide repeat; Pssm-ID: 404131 [Multi-domain] Cd Length: 33 Bit Score: 35.45 E-value: 9.97e-03
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