NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19068577|emb|CAD25045|]
View 

RAN SPECIFIC GTPASE ACTIVATING PROTEIN [Encephalitozoon cuniculi GB-M1]

Protein Classification

Ran-binding domain-containing protein( domain architecture ID 11474075)

Ran-binding domain-containing protein similar to Homo sapiens Ran-specific GTPase-activating protein (RanBP1) that plays a role in RAN-dependent nucleocytoplasmic transport

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
2-215 1.57e-100

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


:

Pssm-ID: 227499  Cd Length: 211  Bit Score: 290.00  E-value: 1.57e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577   2 AEVERKEEQAKIESGSNEQKERGLDGVNKGDAVGDGKEGGEAKKVQQSPFLTNAVPRKDEGKGgEERDNIDAAEVVEKQR 81
Cdd:COG5171   1 MSVERKKKQAKIEKEENEQKERSLDVVSKGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKG-PESPNIHFEPVVELQR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  82 KHLEENQSDE-ILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVS 160
Cdd:COG5171  80 VHLKTNEEDEtVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19068577 161 NGWMWMSTEDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYDLGRAHNEKALKTK 215
Cdd:COG5171 160 RSWVWMSTADTVEGEA---KAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALKTK 211
 
Name Accession Description Interval E-value
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
2-215 1.57e-100

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 290.00  E-value: 1.57e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577   2 AEVERKEEQAKIESGSNEQKERGLDGVNKGDAVGDGKEGGEAKKVQQSPFLTNAVPRKDEGKGgEERDNIDAAEVVEKQR 81
Cdd:COG5171   1 MSVERKKKQAKIEKEENEQKERSLDVVSKGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKG-PESPNIHFEPVVELQR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  82 KHLEENQSDE-ILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVS 160
Cdd:COG5171  80 VHLKTNEEDEtVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19068577 161 NGWMWMSTEDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYDLGRAHNEKALKTK 215
Cdd:COG5171 160 RSWVWMSTADTVEGEA---KAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALKTK 211
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 85-205 1.72e-39

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: 131.95  E-value: 1.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENqsDEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWM 164
Cdd:cd00835   3 EEN--EEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19068577 165 WMSTEDTVETDalrKKIQLFVVKFYSEEDFKRFGEEYDLGR 205
Cdd:cd00835  81 WTAMDDSEDGE---GKPETFAVRFKTAEDAEEFKKAFEEAQ 118
Ran_BP1 pfam00638
RanBP1 domain;
82-202 7.12e-13

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 62.83  E-value: 7.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577    82 KHLEENQsdEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSN 161
Cdd:pfam00638   3 KTGEEDE--EVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 19068577   162 GWMWmSTEDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYD 202
Cdd:pfam00638  81 SWVW-TAADFADGEG---KPEQLAIRFKTKEEADSFKKKFE 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 82-197 1.92e-10

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: 56.63  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577     82 KHLEENqsDEILFKARCKLYYFSEETKALEERAEGTMIIEMHS-KSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVS 160
Cdd:smart00160  13 KTGEED--EEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKdNGGKVRIVMRRDGVLKVCANHPIFKSMTLKPLAGSN 90

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 19068577    161 NGWMWMSTEDTVETdalrKKIQLFVVKFYSEEDFKRF 197
Cdd:smart00160  91 RALKWTPEDFADDI----PKLVLYAVRFKTKEEADSF 123
 
Name Accession Description Interval E-value
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
2-215 1.57e-100

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 290.00  E-value: 1.57e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577   2 AEVERKEEQAKIESGSNEQKERGLDGVNKGDAVGDGKEGGEAKKVQQSPFLTNAVPRKDEGKGgEERDNIDAAEVVEKQR 81
Cdd:COG5171   1 MSVERKKKQAKIEKEENEQKERSLDVVSKGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKG-PESPNIHFEPVVELQR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  82 KHLEENQSDE-ILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVS 160
Cdd:COG5171  80 VHLKTNEEDEtVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19068577 161 NGWMWMSTEDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYDLGRAHNEKALKTK 215
Cdd:COG5171 160 RSWVWMSTADTVEGEA---KAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALKTK 211
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 85-205 1.72e-39

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: 131.95  E-value: 1.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENqsDEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWM 164
Cdd:cd00835   3 EEN--EEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19068577 165 WMSTEDTVETDalrKKIQLFVVKFYSEEDFKRFGEEYDLGR 205
Cdd:cd00835  81 WTAMDDSEDGE---GKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 82-202 1.12e-14

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: 67.98  E-value: 1.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  82 KHLEENqsDEILFKARCKLYYFSEETKALE--ERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKV 159
Cdd:cd13179  16 KTGEED--EEVLFKMRAKLYRFDTENDPPEwkERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYITPEMKLKPNAGS 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19068577 160 SNGWMWmSTEDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYD 202
Cdd:cd13179  94 DRAWVW-TCADFADEEP---KPELFAIRFANAENAQKFKEAFE 132
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 85-202 1.41e-13

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: 64.61  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENqsDEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWM 164
Cdd:cd13176   3 EED--EEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19068577 165 WMSTeDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYD 202
Cdd:cd13176  81 WTAL-DFSEEEP---KVEQLAVKFKTPEVADEFKKKFE 114
Ran_BP1 pfam00638
RanBP1 domain;
82-202 7.12e-13

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 62.83  E-value: 7.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577    82 KHLEENQsdEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSN 161
Cdd:pfam00638   3 KTGEEDE--EVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 19068577   162 GWMWmSTEDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYD 202
Cdd:pfam00638  81 SWVW-TAADFADGEG---KPEQLAIRFKTKEEADSFKKKFE 117
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 85-202 1.84e-11

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: 59.21  E-value: 1.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENQsdEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWM 164
Cdd:cd14685   3 EENE--QVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19068577 165 WmSTEDTVETDalrKKIQLFVVKFYSEEDFKRFGEEYD 202
Cdd:cd14685  81 W-TAMDFAEGE---GKIEQLAVRFKLQETADTFKQIFD 114
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 88-200 1.01e-10

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: 57.27  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  88 QSDEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWMWMS 167
Cdd:cd13178   4 EDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLVWTA 83

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19068577 168 TeDTVETDAlrkKIQLFVVKFYSEE---DFKRFGEE 200
Cdd:cd13178  84 T-DYADGEG---KVEQLAVRFKTKEiadSFKKVFEE 115
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 82-197 1.92e-10

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: 56.63  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577     82 KHLEENqsDEILFKARCKLYYFSEETKALEERAEGTMIIEMHS-KSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVS 160
Cdd:smart00160  13 KTGEED--EEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKdNGGKVRIVMRRDGVLKVCANHPIFKSMTLKPLAGSN 90

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 19068577    161 NGWMWMSTEDTVETdalrKKIQLFVVKFYSEEDFKRF 197
Cdd:smart00160  91 RALKWTPEDFADDI----PKLVLYAVRFKTKEEADSF 123
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 88-202 6.51e-10

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: 55.04  E-value: 6.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  88 QSDEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWMWMS 167
Cdd:cd14684   4 EDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFVWNA 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 19068577 168 TEdtvETDALRKKIQLfVVKFYSEEDFKRFGEEYD 202
Cdd:cd14684  84 LD---YADELPKPEQL-AIRFKTVEEAALFKCKFE 114
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 85-189 2.14e-09

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: 53.56  E-value: 2.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENQsdEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWM 164
Cdd:cd13174   3 EEDE--TKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 19068577 165 W------MSTEDTVETDALRKKIQLFVVKFY 189
Cdd:cd13174  81 WggmnyaEDAEPEVETLAVRFKNEEIASQFK 111
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 88-202 3.98e-09

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: 52.74  E-value: 3.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  88 QSDEILFKARCKLYYFSEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWMWMS 167
Cdd:cd13177   4 EDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWMWMA 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 19068577 168 TeDTVETDAlrkKIQLFVVKFYSEEDFKRFGEEYD 202
Cdd:cd13177  84 N-DFSDGDA---KLEQLAAKFKTPELAEEFKLKFE 114
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 85-205 2.61e-08

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: 50.54  E-value: 2.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENqsDEILFKARCKLYYFSeeTKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGWM 164
Cdd:cd13171   3 EEN--EEVLFCARAKLFRYV--DKEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19068577 165 WMSTEDTVETDALRKkiqlFVVKFYSEEDFKRFGEEYDLGR 205
Cdd:cd13171  79 WAANDFADEVVVLEK----LCVRFKTVELAKEFRDVFTKAK 115
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 85-197 1.76e-07

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: 48.22  E-value: 1.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENqsDEILFKARCKLYYFSEETKALEERAEGTM-IIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKVSNGW 163
Cdd:cd13172   3 EEN--EEVLFEHRAKLLRFDKATKEWKERGLGNIkLLRNKEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 19068577 164 MWMStEDTVETDAlrkKIQLFVVKFYSEEDFKRF 197
Cdd:cd13172  81 TWCA-QDYSEGEL---KPETFAIRFKTQEICKDF 110
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 85-165 6.83e-04

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: 38.23  E-value: 6.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19068577  85 EENQsdEILFKARCKLYYFSEetKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPhgKVSNGWM 164
Cdd:cd13173   3 EEDE--EVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76


                .
gi 19068577 165 W 165
Cdd:cd13173  77 W 77
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 85-159 2.93e-03

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: 36.04  E-value: 2.93e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19068577  85 EENQSDEILFKARCKLYYFsEETKALEERAEGTMIIEMHSKSNLAKITMFRDQIGRLGCNHFINPRFKAQPHGKV 159
Cdd:cd13170   1 AGEEEEDTVFEVRAKLFKK-KDDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKN 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH