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 1907111685 195 TGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNDtaGRECGTLQSRLIMRNQGSLRLVLNSRLWAQMKIQRASQKN 274
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLND--SKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907111685 275 LRITATDlEDDGIKIFLIQASAKDTGFLYAAIHHRL 310
Cdd:cd13180    79 LRITAMD-DEGQVKVFLLQASPEDAKQLYNAIQDRI 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 1907111685 195 TGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNDtaGRECGTLQSRLIMRNQGSLRLVLNSRLWAQMKIQRASQKN 274
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLND--SKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907111685 275 LRITATDlEDDGIKIFLIQASAKDTGFLYAAIHHRL 310
Cdd:cd13180    79 LRITAMD-DEGQVKVFLLQASPEDAKQLYNAIQDRI 113

RanBP1 domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111685 192 DVITGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNDTAGREcgtlQSRLIMRNQGSLRLVLNSRLWAQMKIQ--R 269
Cdd:pfam00638   1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDG----KVRILMRRDQVLKVCANHYITPDMTLKplA 76

                          90       100
                  ....*....|....*....|.
gi 1907111685 270 ASQKNLRITATDLEDDGIKIF 290
Cdd:pfam00638  77 GSDRSWVWTAADFADGEGKPE 97

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 1907111685 195 TGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNDtaGRECGTLQSRLIMRNQGSLRLVLNSRLWAQMKIQRASQKN 274
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLND--SKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907111685 275 LRITATDlEDDGIKIFLIQASAKDTGFLYAAIHHRL 310
Cdd:cd13180    79 LRITAMD-DEGQVKVFLLQASPEDAKQLYNAIQDRI 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 1907111685 195 TGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNdtagRECGTLQSRLIMRNQGSLRLVLNSRLWAQMKIQR--ASQ 272
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKIL----KNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKmgNND 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907111685 273 KNLRITATDLEDDG---IKIFLIQ-ASAKDTGFLYAAIHH 308
Cdd:cd00835    77 RAWVWTAMDDSEDGegkPETFAVRfKTAEDAEEFKKAFEE 116

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111685 195 TGEETEHNVLKINCKIFVFnkATESWSERGQGILRLNDTAGREcgtlQSRLIMRNQGSLRLVLNSRLWAQMKIQRASQKN 274
Cdd:cd13169     1 TGEENEKAVFSGDGALFEF--IDGGWKERGKGELRVNLSTTTG----QARLVMRARGNYRLILNANLYPDMKLTKMGGKG 74

                          90
                  ....*....|....*....
gi 1907111685 275 LR---ITATDLEDDGIKIF 290
Cdd:cd13169    75 VTfacVNSAADAKDKLSTF 93

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 1907111685 181 KPSQKclLEKIDVITGEETEHNVLKINCKIFVFNKATES--WSERGQGILRL--NDTAGREcgtlqsRLIMRNQGSLRLV 256
Cdd:cd13179     5 EPIVK--LPEVEVKTGEEDEEVLFKMRAKLYRFDTENDPpeWKERGTGDVKLlkHKETKKI------RLLMRRDKTLKIC 76

                          90
                  ....*....|..
gi 1907111685 257 LNSRLWAQMKIQ 268
Cdd:cd13179    77 ANHYITPEMKLK 88

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111685 188 LEKIDVITGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNdtagRECGTLQSRLIMRNQGSLRLVLNSRLWAQMKI 267
Cdd:COG5171    77 LQRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIIL----KHKKTNKARITMRRDKTLKLCANHFINPEFKL 152

                  .
gi 1907111685 268 Q 268
Cdd:COG5171   153 Q 153

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 1907111685 195 TGEETEHNVLKINCKIFVFNKatESWSERGQG---ILRLNDTAgrecgtlQSRLIMRNQGSLRLVLNSRLWAQMKIQRAS 271
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGdvkILRHKETG-------KLRLLMRRDQVLKICLNHALTEELEFRKKD 71

                          90
                  ....*....|...
gi 1907111685 272 QKNLRITATDLED 284
Cdd:cd13173    72 EKSWMWAAHDFSE 84

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 1907111685 195 TGEETEHNVLKINCKIFVFNKATESWSERGQGILRL------NDTAgrecgtlqsRLIMRNQGSLRLVLNSRLWAQMKIQ 268
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLlrnkedNNKV---------RLLMRREQVLKVCCNQRLTKDMEFK 71

                          90
                  ....*....|....*...
gi 1907111685 269 RA--SQKNLRITATDLED 284
Cdd:cd13172    72 YLtnNPKALTWCAQDYSE 89

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 1907111685 195 TGEETEHNVLKINCKIFVFNKA-TES-WSERGQG---ILRLNDTAgrecgtlQSRLIMRNQGSLRLVLNSRLWAQMKIQR 269
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDPSnTESpYTSKGVGelkLLKNKDTG-------KSRILVRAEGSLRVLLNTLVLKDVKYEK 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907111685 270 ASQKNL-RITATDlEDDGIKIFLIQASAKDTG 300
Cdd:cd13181    74 MGNGSLvRVPTIN-SDGKIETYVIKVKTAADG 104

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907111685 195 TGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNDTAGREcgtlQSRLIMRNQGSLRLVLNSRLWAQMKIQ--RASQ 272
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKH----YYRILMRRDQVLKVCANHVITQDMDLQplSASN 76

                          90
                  ....*....|..
gi 1907111685 273 KNLRITATDLED 284
Cdd:cd13178    77 NTLVWTATDYAD 88