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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMAStdDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKS 191
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKS--DGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462568338 192 IRITAMDTEDQgVKVFLISASSKDTGQLYAALHHRI 227
Cdd:cd13180    79 LRITAMDDEGQ-VKVFLLQASPEDAKQLYNAIQDRI 113

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMAStdDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKS 191
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKS--DGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462568338 192 IRITAMDTEDQgVKVFLISASSKDTGQLYAALHHRI 227
Cdd:cd13180    79 LRITAMDDEGQ-VKVFLLQASPEDAKQLYNAIQDRI 113

RanBP1 domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 109 EVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNdmASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQID--K 186
Cdd:pfam00638   1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKIL--KNKDDG--KVRILMRRDQVLKVCANHYITPDMTLKplA 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462568338 187 ASEKSIRITAMDTEDQGVKVFL--ISASSKDTGQLY 220
Cdd:pfam00638  77 GSDRSWVWTAADFADGEGKPEQlaIRFKTKEEADSF 112

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMAStdDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKS 191
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKS--DGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462568338 192 IRITAMDTEDQgVKVFLISASSKDTGQLYAALHHRI 227
Cdd:cd13180    79 LRITAMDDEGQ-VKVFLLQASPEDAKQLYNAIQDRI 113

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338  105 LEKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNdmASTDDGTlQSRLVMRTQGSLRLILNTKLWAQMQI 184
Cdd:smart00160   7 LPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKIL--KSKDNGG-KVRIVMRRDGVLKVCANHPIFKSMTL 83

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462568338  185 D--KASEKSIRITAMDTEDQGVKVFLISASSKD 215
Cdd:smart00160  84 KplAGSNRALKWTPEDFADDIPKLVLYAVRFKT 116

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFDKTSqSWVERGRGLLRLNdmasTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIdKASEKS 191
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKKDDG-EWKDKGVGTLRLK----KHKTTGKARILVRADTLGKILLNFLLYKGMPY-SVAGKN 74

                          90
                  ....*....|....*...
gi 2462568338 192 IRITAMDTEDQGVKVFLI 209
Cdd:cd13170    75 NVFVGCVPNPGKPVTYLL 92

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 105 LEKVEVITGEEAESNVLQMQCKLFVFDKTSQS--WVERGRGLLRLndMASTDDGTLqsRLVMRTQGSLRLILNTKL--WA 180
Cdd:cd13179    10 LPEVEVKTGEEDEEVLFKMRAKLYRFDTENDPpeWKERGTGDVKL--LKHKETKKI--RLLMRRDKTLKICANHYItpEM 85

                          90       100
                  ....*....|....*....|....*...
gi 2462568338 181 QMQIDKASEKSIRITAMDTEDQGVKVFL 208
Cdd:cd13179    86 KLKPNAGSDRAWVWTCADFADEEPKPEL 113

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFD--KTSQSWVERGRGLLRLndMASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQIDK-AS 188
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKL--LKNKDTG--KSRILVRAEGSLRVLLNTLVLKDVKYEKmGN 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462568338 189 EKSIRITAMDtEDQGVKVFLISASSKDTGQ 218
Cdd:cd13181    77 GSLVRVPTIN-SDGKIETYVIKVKTAADGE 105

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNdMASTDDGTLqsRLVMRTQGSLRLILNTKLWAQMQIDKA--SE 189
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLL-RNKEDNNKV--RLLMRREQVLKVCCNQRLTKDMEFKYLtnNP 77

                          90
                  ....*....|....*..
gi 2462568338 190 KSIRITAMDTEDQGVKV 206
Cdd:cd13172    78 KALTWCAQDYSEGELKP 94

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLndMASTDDGTLqsRLVMRTQGSLRLILNTKLWAQMQI--DKASE 189
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKI--LRHKTSGKI--RLLMRREQVLKICANHYISADMKLkpNAGSD 76

                          90
                  ....*....|...
gi 2462568338 190 KSIRITAMDTEDQ 202
Cdd:cd14684    77 KSFVWNALDYADE 89

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLndMASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQI--DKASE 189
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKI--LQHKTTG--RIRILMRRDQVLKVCANHYITPDMKLkpNAGSD 76

                          90
                  ....*....|....*..
gi 2462568338 190 KSIRITAMDTEDQGVKV 206
Cdd:cd13176    77 RSWVWTALDFSEEEPKV 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568338 112 TGEEAESNVLQMQCKLFVFdkTSQSWVERGRGLLRLndMASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQID--KASE 189
Cdd:cd13171     1 TGEENEEVLFCARAKLFRY--VDKEWKERGIGNLKI--LKNPATG--KVRLLMRREQVHKVCANHFITKDMELTpmKKED 74

                          90
                  ....*....|....*
gi 2462568338 190 KSIRITAMDTEDQGV 204
Cdd:cd13171    75 KAYIWAANDFADEVV 89