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 21355293 243 TGEEDEINIIDVSCKLFAFLN--SNWEERGRGSLRLNDAK-DLRGDSRVVFRTSGNLRLLLNTKVWAAMVAERASQKSLR 319
Cdd:cd13180   1 TGEEGETNVFQVNCKLYAFDKskQSWKERGRGTLRLNDSKsDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKSLR 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 21355293 320 LTAIDNSGVVKIFLAMGRPADIAQLHKALSERI 352
Cdd:cd13180  81 ITAMDDEGQVKVFLLQASPEDAKQLYNAIQDRI 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 21355293 243 TGEEDEINIIDVSCKLFAFLN--SNWEERGRGSLRLNDAK-DLRGDSRVVFRTSGNLRLLLNTKVWAAMVAERASQKSLR 319
Cdd:cd13180   1 TGEEGETNVFQVNCKLYAFDKskQSWKERGRGTLRLNDSKsDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKSLR 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 21355293 320 LTAIDNSGVVKIFLAMGRPADIAQLHKALSERI 352
Cdd:cd13180  81 ITAMDDEGQVKVFLLQASPEDAKQLYNAIQDRI 113

RanBP1 domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355293   240 ETFTGEEDEINIIDVSCKLFAF--LNSNWEERGRGSLRLNDAKDlRGDSRVVFRTSGNLRLLLN 301
Cdd:pfam00638   1 EVKTGEEDEEVLFSQRAKLFRFdaEVKQWKERGVGDIKILKNKD-DGKVRILMRRDQVLKVCAN 63

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 21355293 243 TGEEDEINIIDVSCKLFAFLN--SNWEERGRGSLRLNDAK-DLRGDSRVVFRTSGNLRLLLNTKVWAAMVAERASQKSLR 319
Cdd:cd13180   1 TGEEGETNVFQVNCKLYAFDKskQSWKERGRGTLRLNDSKsDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKSLR 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 21355293 320 LTAIDNSGVVKIFLAMGRPADIAQLHKALSERI 352
Cdd:cd13180  81 ITAMDDEGQVKVFLLQASPEDAKQLYNAIQDRI 113

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355293 243 TGEEDEINIIDVSCKLFAFLNSN--WEERGRGSLRLNDAKDlRGDSRVVFRTSGNLRLLLNTKVWAAMVAER--ASQKSL 318
Cdd:cd00835   1 TGEENEEVLFEKRAKLFRFDKETkeWKERGVGDLKILKNKD-TGKYRIVMRRDQVLKLCCNHYILPDMKLTKmgNNDRAW 79

                ....*...
gi 21355293 319 RLTAIDNS 326
Cdd:cd00835  80 VWTAMDDS 87

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 21355293 243 TGEEDEINIIDVSCKLFAFL-NSNWEERGRGSLRLNDAKDlRGDSRVVFRTSGNLRLLLNTKVWAAMVAERASQKSLRLT 321
Cdd:cd13170   1 AGEEEEDTVFEVRAKLFKKKdDGEWKDKGVGTLRLKKHKT-TGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVG 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 21355293 322 AIDNSGVVKIFLA-MGRPADIAQLHKALSERI 352
Cdd:cd13170  80 CVPNPGKPVTYLLrVKTAEDADELAKALEEEK 111

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355293 243 TGEEDEINIIDVSCKLFAFLNSNWEERGRGSLRLNDAKDlRGDSRVVFRTSGNLRLLLNTKVWAAMVAERASQKSLRLTA 322
Cdd:cd13173   1 TGEEDEEVLYSHRAKLFRFVDKEWKERGLGDVKILRHKE-TGKLRLLMRRDQVLKICLNHALTEELEFRKKDEKSWMWAA 79

                        90       100
                ....*....|....*....|....
gi 21355293 323 IDNS-GVVKI--FLAMGRPADIAQ 343
Cdd:cd13173  80 HDFSeGESELerFAIRFKNAEIAQ 103

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
                ....*....|....*....|....*....|....*....|....
gi 21355293 237 EEVETFTGEEDEINIIDVSCKLFAFLNSN----WEERGRGSLRL 276
Cdd:cd13179  11 PEVEVKTGEEDEEVLFKMRAKLYRFDTENdppeWKERGTGDVKL 54

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355293 211 KESAEAKSLTDVAREYEESRAQKR---------KYEEVETFTGEEDEINIIDVSCKLFAF--LNSNWEERGRGSLRLNDA 279
Cdd:COG5171  43 KKVQQSPFLENAVPEGDEGKGPESpnihfepvvELQRVHLKTNEEDETVLFKARAKLFRFdeEAKEWKERGTGDMIILKH 122

                        90       100
                ....*....|....*....|..
gi 21355293 280 KDlRGDSRVVFRTSGNLRLLLN 301
Cdd:COG5171 123 KK-TNKARITMRRDKTLKLCAN 143

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355293 243 TGEEDEINIIDVSCKLFAF--LNSNWEERGRGSLRLNDAKDlRGDSRVVFRTSGNLRLLLNTKVWA--AMVAERASQKSL 318
Cdd:cd13174   1 TGEEDETKLFGERAKLYRFdaDTKEWKERGVGEMKILYHPE-LNTYRLLMRREQVHKVVLNMLITSdlQLRPMNTSDKSF 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 21355293 319 ----RLTAIDNSGVVKIFLAMGRPADIAQLHK 346
Cdd:cd13174  80 twggMNYAEDAEPEVETLAVRFKNEEIASQFK 111