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 194097489 325 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMAStdDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKS 404
Cdd:cd13180    1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKS--DGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194097489 405 IRITAMDTEDQgVKVFLISASSKDTGQLYAALHHRI 440
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 194097489 325 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMAStdDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKS 404
Cdd:cd13180    1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKS--DGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194097489 405 IRITAMDTEDQgVKVFLISASSKDTGQLYAALHHRI 440
Cdd:cd13180   79 LRITAMDDEGQ-VKVFLLQASPEDAKQLYNAIQDRI 113

RanBP1 domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194097489  322 EVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNdmASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQID--K 399
Cdd:pfam00638   1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKIL--KNKDDG--KVRILMRRDQVLKVCANHYITPDMTLKplA 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 194097489  400 ASEKSIRITAMDTEDQGVKVFL--ISASSKDTGQLY 433
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 194097489 325 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMAStdDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKS 404
Cdd:cd13180    1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKS--DGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194097489 405 IRITAMDTEDQgVKVFLISASSKDTGQLYAALHHRI 440
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 194097489   318 LEKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNdmASTDDGTlQSRLVMRTQGSLRLILNTKLWAQMQI 397
Cdd:smart00160   7 LPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKIL--KSKDNGG-KVRIVMRRDGVLKVCANHPIFKSMTL 83

                           90       100       110
                   ....*....|....*....|....*....|...
gi 194097489   398 D--KASEKSIRITAMDTEDQGVKVFLISASSKD 428
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 194097489 325 TGEEAESNVLQMQCKLFVFDKTSqSWVERGRGLLRLNdmasTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIdKASEKS 404
Cdd:cd13170    1 AGEEEEDTVFEVRAKLFKKKDDG-EWKDKGVGTLRLK----KHKTTGKARILVRADTLGKILLNFLLYKGMPY-SVAGKN 74

                         90
                 ....*....|....*...
gi 194097489 405 IRITAMDTEDQGVKVFLI 422
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 194097489 318 LEKVEVITGEEAESNVLQMQCKLFVFDKTSQS--WVERGRGLLRLndMASTDDGTLqsRLVMRTQGSLRLILNTKL--WA 393
Cdd:cd13179   10 LPEVEVKTGEEDEEVLFKMRAKLYRFDTENDPpeWKERGTGDVKL--LKHKETKKI--RLLMRRDKTLKICANHYItpEM 85

                         90       100
                 ....*....|....*....|....*...
gi 194097489 394 QMQIDKASEKSIRITAMDTEDQGVKVFL 421
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 194097489 325 TGEEAESNVLQMQCKLFVFD--KTSQSWVERGRGLLRLndMASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQIDK-AS 401
Cdd:cd13181    1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKL--LKNKDTG--KSRILVRAEGSLRVLLNTLVLKDVKYEKmGN 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 194097489 402 EKSIRITAMDtEDQGVKVFLISASSKDTGQ 431
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 194097489 325 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNdMASTDDGTLqsRLVMRTQGSLRLILNTKLWAQMQIDKA--SE 402
Cdd:cd13172    1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLL-RNKEDNNKV--RLLMRREQVLKVCCNQRLTKDMEFKYLtnNP 77

                         90
                 ....*....|....*..
gi 194097489 403 KSIRITAMDTEDQGVKV 419
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 194097489 325 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLndMASTDDGTLqsRLVMRTQGSLRLILNTKLWAQMQI--DKASE 402
Cdd:cd14684    1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKI--LRHKTSGKI--RLLMRREQVLKICANHYISADMKLkpNAGSD 76

                         90
                 ....*....|...
gi 194097489 403 KSIRITAMDTEDQ 415
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 194097489 325 TGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLndMASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQI--DKASE 402
Cdd:cd13176    1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKI--LQHKTTG--RIRILMRRDQVLKVCANHYITPDMKLkpNAGSD 76

                         90
                 ....*....|....*..
gi 194097489 403 KSIRITAMDTEDQGVKV 419
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 194097489 325 TGEEAESNVLQMQCKLFVFdkTSQSWVERGRGLLRLndMASTDDGtlQSRLVMRTQGSLRLILNTKLWAQMQID--KASE 402
Cdd:cd13171    1 TGEENEEVLFCARAKLFRY--VDKEWKERGIGNLKI--LKNPATG--KVRLLMRREQVHKVCANHFITKDMELTpmKKED 74

                         90
                 ....*....|....*
gi 194097489 403 KSIRITAMDTEDQGV 417
Cdd:cd13171   75 KAYIWAANDFADEVV 89