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Conserved domains on  [gi|1812588793|sp|Q9UKX7|]
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RecName: Full=Nuclear pore complex protein Nup50; AltName: Full=50 kDa nucleoporin; AltName: Full=Nuclear pore-associated protein 60 kDa-like; AltName: Full=Nucleoporin Nup50

Protein Classification

NUP50 and RanBD_NUP50 domain-containing protein( domain architecture ID 10556312)

NUP50 and RanBD_NUP50 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 350-466 9.90e-43

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: 146.59  E-value: 9.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 350 TEVKEEDAFYSKKCKLFYKKDN-EFKEKGIGTLHLKPTA-NQKTQLLVRADTNlGNILLNVLIPPNMPCTRTGKNNVLIV 427
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKKDDgEWKDKGVGTLRLKKHKtTGKARILVRADTL-GKILLNFLLYKGMPYSVAGKNNVFVG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1812588793 428 CVPNPPideknatMPVTMLIRVKTSEDADELHKILLEKK 466
Cdd:cd13170    80 CVPNPG-------KPVTYLLRVKTAEDADELAKALEEEK 111
NUP50 pfam08911
NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the ...
 2-67 1.34e-18

NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the importin-alpha:importin-beta heterodimer, which in turn allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. The C terminus of NUP50 binds importin-beta through RAN-GTP, the N terminus binds the C terminus of importin-alpha, while a central domain binds importin-beta. NUP50:importin-alpha:importin-beta then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to actively displace nuclear localization signals from importin-alpha.


:

Pssm-ID: 462629 [Multi-domain]  Cd Length: 71  Bit Score: 79.68  E-value: 1.34e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812588793   2 AKRNAEKELTDRNWDQEDE--AEEVGTFSMASEEVLKNRAIKKAKRRNVG---FESDTGGAFKGFKGLVVP 67
Cdd:pfam08911   1 AKRGADKQLTRDNWDEDEDedEEEAGTFKKASEEVLAKRKIKKAKRRMGSstpSSAASSSAFSGFSGFGKP 71
 
Name Accession Description Interval E-value
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 350-466 9.90e-43

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: 146.59  E-value: 9.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 350 TEVKEEDAFYSKKCKLFYKKDN-EFKEKGIGTLHLKPTA-NQKTQLLVRADTNlGNILLNVLIPPNMPCTRTGKNNVLIV 427
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKKDDgEWKDKGVGTLRLKKHKtTGKARILVRADTL-GKILLNFLLYKGMPYSVAGKNNVFVG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1812588793 428 CVPNPPideknatMPVTMLIRVKTSEDADELHKILLEKK 466
Cdd:cd13170    80 CVPNPG-------KPVTYLLRVKTAEDADELAKALEEEK 111
NUP50 pfam08911
NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the ...
 2-67 1.34e-18

NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the importin-alpha:importin-beta heterodimer, which in turn allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. The C terminus of NUP50 binds importin-beta through RAN-GTP, the N terminus binds the C terminus of importin-alpha, while a central domain binds importin-beta. NUP50:importin-alpha:importin-beta then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to actively displace nuclear localization signals from importin-alpha.


Pssm-ID: 462629 [Multi-domain]  Cd Length: 71  Bit Score: 79.68  E-value: 1.34e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812588793   2 AKRNAEKELTDRNWDQEDE--AEEVGTFSMASEEVLKNRAIKKAKRRNVG---FESDTGGAFKGFKGLVVP 67
Cdd:pfam08911   1 AKRGADKQLTRDNWDEDEDedEEEAGTFKKASEEVLAKRKIKKAKRRMGSstpSSAASSSAFSGFSGFGKP 71
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 344-464 1.84e-08

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: 52.78  E-value: 1.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793  344 PPKVVVTEVKEEDAFYSKKCKL--FYKKDNEFKEKGIGTLH-LKPTAN-QKTQLLVRADtNLGNILLNVLIPPNMPCTR- 418
Cdd:smart00160   8 PDVEVKTGEEDEEVIFSARAKLyrFANDKKEWKERGVGDLKiLKSKDNgGKVRIVMRRD-GVLKVCANHPIFKSMTLKPl 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1812588793  419 TGKNNVLIVcvpNPPIDEKNATMPVTMLIRVKTSEDADELHKILLE 464
Cdd:smart00160  87 AGSNRALKW---TPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEE 129
Ran_BP1 pfam00638
RanBP1 domain;
351-466 6.46e-08

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 50.89  E-value: 6.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 351 EVK--EED--AFYSKKCKLF-YKKDN-EFKEKGIGTLH-LKPTANQKTQLLVRADtNLGNILLNVLIPPNMPCT-RTGKN 422
Cdd:pfam00638   1 EVKtgEEDeeVLFSQRAKLFrFDAEVkQWKERGVGDIKiLKNKDDGKVRILMRRD-QVLKVCANHYITPDMTLKpLAGSD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1812588793 423 NVLI-VCVPNPPIDEKnatmPVTMLIRVKTSEDADELHKILLEKK 466
Cdd:pfam00638  80 RSWVwTAADFADGEGK----PEQLAIRFKTKEEADSFKKKFEEAQ 120
 
Name Accession Description Interval E-value
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 350-466 9.90e-43

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: 146.59  E-value: 9.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 350 TEVKEEDAFYSKKCKLFYKKDN-EFKEKGIGTLHLKPTA-NQKTQLLVRADTNlGNILLNVLIPPNMPCTRTGKNNVLIV 427
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKKDDgEWKDKGVGTLRLKKHKtTGKARILVRADTL-GKILLNFLLYKGMPYSVAGKNNVFVG 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1812588793 428 CVPNPPideknatMPVTMLIRVKTSEDADELHKILLEKK 466
Cdd:cd13170    80 CVPNPG-------KPVTYLLRVKTAEDADELAKALEEEK 111
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 350-466 4.61e-24

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: 96.51  E-value: 4.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 350 TEVKEEDAFYSKKCKLFY--KKDNEFKEKGIGTLH-LKPTANQKTQLLVRADTnLGNILLNVLIPPNMPCTRTGKN-NVL 425
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRfdKETKEWKERGVGDLKiLKNKDTGKYRIVMRRDQ-VLKLCCNHYILPDMKLTKMGNNdRAW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1812588793 426 IVCVPNPpiDEKNATMPVTMLIRVKTSEDADELHKILLEKK 466
Cdd:cd00835    80 VWTAMDD--SEDGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
NUP50 pfam08911
NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the ...
 2-67 1.34e-18

NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the importin-alpha:importin-beta heterodimer, which in turn allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. The C terminus of NUP50 binds importin-beta through RAN-GTP, the N terminus binds the C terminus of importin-alpha, while a central domain binds importin-beta. NUP50:importin-alpha:importin-beta then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to actively displace nuclear localization signals from importin-alpha.


Pssm-ID: 462629 [Multi-domain]  Cd Length: 71  Bit Score: 79.68  E-value: 1.34e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1812588793   2 AKRNAEKELTDRNWDQEDE--AEEVGTFSMASEEVLKNRAIKKAKRRNVG---FESDTGGAFKGFKGLVVP 67
Cdd:pfam08911   1 AKRGADKQLTRDNWDEDEDedEEEAGTFKKASEEVLAKRKIKKAKRRMGSstpSSAASSSAFSGFSGFGKP 71
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 354-464 4.53e-09

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.


Pssm-ID: 270001  Cd Length: 113  Bit Score: 54.16  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 354 EEDAFYSKKCKL--FYKKDNEFKEKGIGTLHL---KPTANQKTQLLVRADTNLGNIlLNVLIPPNMPCTRTGKNNVLIVC 428
Cdd:cd13180     5 GETNVFQVNCKLyaFDKSKQSWKERGRGTLRLndsKSDGSGQSRIVMRTQGSLRVI-LNTKIWPGMTVEKVSEKSLRITA 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1812588793 429 VPnppiDEKNatmPVTMLIRVKtSEDADELHKILLE 464
Cdd:cd13180    84 MD----DEGQ---VKVFLLQAS-PEDAKQLYNAIQD 111
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 355-466 4.62e-09

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.


Pssm-ID: 270002  Cd Length: 115  Bit Score: 53.98  E-value: 4.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 355 EDAFYSKKCKLFY----KKDNEFKEKGIGTLH-LKPTANQKTQLLVRADtNLGNILLNVLIPPNMPCTRTGKNNVLIVcv 429
Cdd:cd13181     6 EEVLYTKRAKLMLfdpsNTESPYTSKGVGELKlLKNKDTGKSRILVRAE-GSLRVLLNTLVLKDVKYEKMGNGSLVRV-- 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1812588793 430 pnPPIDEKNATmpVTMLIRVKTSEDADELHKILLEKK 466
Cdd:cd13181    83 --PTINSDGKI--ETYVIKVKTAADGEELLKALNDAK 115
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 344-464 1.84e-08

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: 52.78  E-value: 1.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793  344 PPKVVVTEVKEEDAFYSKKCKL--FYKKDNEFKEKGIGTLH-LKPTAN-QKTQLLVRADtNLGNILLNVLIPPNMPCTR- 418
Cdd:smart00160   8 PDVEVKTGEEDEEVIFSARAKLyrFANDKKEWKERGVGDLKiLKSKDNgGKVRIVMRRD-GVLKVCANHPIFKSMTLKPl 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1812588793  419 TGKNNVLIVcvpNPPIDEKNATMPVTMLIRVKTSEDADELHKILLE 464
Cdd:smart00160  87 AGSNRALKW---TPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEE 129
Ran_BP1 pfam00638
RanBP1 domain;
351-466 6.46e-08

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 50.89  E-value: 6.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 351 EVK--EED--AFYSKKCKLF-YKKDN-EFKEKGIGTLH-LKPTANQKTQLLVRADtNLGNILLNVLIPPNMPCT-RTGKN 422
Cdd:pfam00638   1 EVKtgEEDeeVLFSQRAKLFrFDAEVkQWKERGVGDIKiLKNKDDGKVRILMRRD-QVLKVCANHYITPDMTLKpLAGSD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1812588793 423 NVLI-VCVPNPPIDEKnatmPVTMLIRVKTSEDADELHKILLEKK 466
Cdd:pfam00638  80 RSWVwTAADFADGEGK----PEQLAIRFKTKEEADSFKKKFEEAQ 120
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 355-468 2.73e-07

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: 49.00  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 355 EDAFYSKKCKLFYKKDNEFKEKGIGTLH-LKPTANQKTQLLVRADTNLgNILLNVLIPPNMPCTRTGKNNVLIVCVPNPP 433
Cdd:cd13171     6 EEVLFCARAKLFRYVDKEWKERGIGNLKiLKNPATGKVRLLMRREQVH-KVCANHFITKDMELTPMKKEDKAYIWAANDF 84

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1812588793 434 IDEKnaTMPVTMLIRVKTSEDADELHKILLEKKDA 468
Cdd:cd13171    85 ADEV--VVLEKLCVRFKTVELAKEFRDVFTKAKKE 117
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 355-466 3.07e-06

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: 46.29  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 355 EDAFYSKKCKL--FYKKDNEFKEKGIGTLHL--KPTANQKTQLLVRADTNLgNILLNVLIPPNMPCTRTGKN-NVLIVCV 429
Cdd:cd13172     6 EEVLFEHRAKLlrFDKATKEWKERGLGNIKLlrNKEDNNKVRLLMRREQVL-KVCCNQRLTKDMEFKYLTNNpKALTWCA 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1812588793 430 PNPpidEKNATMPVTMLIRVKTSEDADELHKILLEKK 466
Cdd:cd13172    85 QDY---SEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 353-414 4.95e-05

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: 42.47  E-value: 4.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812588793 353 KEEDAFYSKKCKLFYKKDNEFKEKGIGTLH-LKPTANQKTQLLVRADTNLgNILLNVLIPPNM 414
Cdd:cd13173     4 EDEEVLYSHRAKLFRFVDKEWKERGLGDVKiLRHKETGKLRLLMRRDQVL-KICLNHALTEEL 65
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 342-414 7.64e-04

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: 39.47  E-value: 7.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812588793 342 DEPPKVVVTEVKEEDAFYSKKCKLF-YKKD---NEFKEKGIGTLH-LKPTANQKTQLLVRADTNLgNILLNVLIPPNM 414
Cdd:cd13179     9 KLPEVEVKTGEEDEEVLFKMRAKLYrFDTEndpPEWKERGTGDVKlLKHKETKKIRLLMRRDKTL-KICANHYITPEM 85
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 354-464 1.12e-03

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: 38.80  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812588793 354 EEDAFYSKKCKLF-YKKD-NEFKEKGIGTLH-LKPTANQKTQLLVRADTNLgNILLNVLIPPNMPCT-RTGKNNVLIVCV 429
Cdd:cd13176     5 DEEVLFSHRAKLYrFDKDvKQWKERGVGDIKiLQHKTTGRIRILMRRDQVL-KVCANHYITPDMKLKpNAGSDRSWVWTA 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1812588793 430 PN----PPIDEKNAtmpvtmlIRVKTSEDADELHKILLE 464
Cdd:cd13176    84 LDfseeEPKVEQLA-------VKFKTPEVADEFKKKFEE 115
 
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.
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