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Conserved domains on  [gi|1063711796|ref|NP_001326913|]
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NUP50 (Nucleoporin 50 kDa) protein [Arabidopsis thaliana]

Protein Classification

PH domain-containing protein; Tec family PH domain-containing protein( domain architecture ID 10556310)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner| Tec family PH (pleckstrin homology) domain-containing protein similar to the PH domain of tyrosine-protein kinase BTK, a non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 326-443 2.09e-68

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.


:

Pssm-ID: 269990  Cd Length: 117  Bit Score: 213.85  E-value: 2.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGGWKERGKGELKVNISTTeNRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGITFAC 405
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFIDGGWKERGKGELRVNLSTT-TGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFAC 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063711796 406 VNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDSK 443
Cdd:cd13169    80 VNSAADAKDKLSTFALKFKDPQVVEEFRAAVEAHKDSA 117
NUP50 pfam08911
NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the ...
 13-77 8.05e-13

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: 63.51  E-value: 8.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796  13 KRTALKELSRDNPgldDDDEDTSALESGTFNTASKEVLASRRIIRVRR-----TDRSATAPPASNPFTGI 77
Cdd:pfam08911   2 KRGADKQLTRDNW---DEDEDEDEEEAGTFKKASEEVLAKRKIKKAKRrmgssTPSSAASSSAFSGFSGF 68
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 93-237 8.37e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796   93 ETTKPLSAGKQETLADGRSDATKETDGDSKEKSDA-IDAVGKQETQGD-EISAKTKDIidGGEKEMSEAVNSVEGGGAVN 170
Cdd:TIGR00927  649 GERPTEAEGENGEESGGEAEQEGETETKGENESEGeIPAERKGEQEGEgEIEAKEADH--KGETEAEEVEHEGETEAEGT 726

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063711796  171 KNEDEIKTTMVTEVAAGEETVKDDNNNSNTVEGSDCVVKDTGGNQTEKEGKEGDG----NEDTEKNGDSGA 237
Cdd:TIGR00927  727 EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGeiqaGEDGEMKGDEGA 797
 
Name Accession Description Interval E-value
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 326-443 2.09e-68

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.


Pssm-ID: 269990  Cd Length: 117  Bit Score: 213.85  E-value: 2.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGGWKERGKGELKVNISTTeNRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGITFAC 405
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFIDGGWKERGKGELRVNLSTT-TGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFAC 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063711796 406 VNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDSK 443
Cdd:cd13169    80 VNSAADAKDKLSTFALKFKDPQVVEEFRAAVEAHKDSA 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 320-438 1.37e-20

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: 87.44  E-value: 1.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796  320 QDVSVETGEENEKAAFTADSVMFEY--LEGGWKERGKGELKVNISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMD 397
Cdd:smart00160   8 PDVEVKTGEEDEEVIFSARAKLYRFanDKKEWKERGVGDLKILKSKDNGGKVRIVMRRDGVLKVCANHPIFKSMTLKPLA 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1063711796  398 K--KGITFACVNSVSDAKDgLSTLALKFKDPTVVEEFRAVIEE 438
Cdd:smart00160  88 GsnRALKWTPEDFADDIPK-LVLYAVRFKTKEEADSFKNIFEE 129
Ran_BP1 pfam00638
RanBP1 domain;
324-440 3.65e-15

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 71.69  E-value: 3.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 324 VETGEENEKAAFTADSVMFEY--LEGGWKERGKGELKVNISTtENRKARLVMRSKGNYRLTLNASLYPEMKLAKMdkKGI 401
Cdd:pfam00638   2 VKTGEEDEEVLFSQRAKLFRFdaEVKQWKERGVGDIKILKNK-DDGKVRILMRRDQVLKVCANHYITPDMTLKPL--AGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063711796 402 TFACVNSVSDAKDG---LSTLALKFKDPTVVEEFRAVIEEHK 440
Cdd:pfam00638  79 DRSWVWTAADFADGegkPEQLAIRFKTKEEADSFKKKFEEAQ 120
NUP50 pfam08911
NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the ...
 13-77 8.05e-13

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: 63.51  E-value: 8.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796  13 KRTALKELSRDNPgldDDDEDTSALESGTFNTASKEVLASRRIIRVRR-----TDRSATAPPASNPFTGI 77
Cdd:pfam08911   2 KRGADKQLTRDNW---DEDEDEDEEEAGTFKKASEEVLAKRKIKKAKRrmgssTPSSAASSSAFSGFSGF 68
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
319-423 3.40e-05

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 45.01  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 319 KQDVSVETGEENEKAAFTADSVMFEYLEGG--WKERGKGELKVNISTTENrKARLVMRSKGNYRLTLNASLYPEMKLAKM 396
Cdd:COG5171    77 LQRVHLKTNEEDETVLFKARAKLFRFDEEAkeWKERGTGDMIILKHKKTN-KARITMRRDKTLKLCANHFINPEFKLQPN 155

                          90       100
                  ....*....|....*....|....*....
gi 1063711796 397 DK--KGITFACVNSVSDAKDGLSTLALKF 423
Cdd:COG5171   156 VGsdRSWVWMSTADTVEGEAKAQTFAIRF 184
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 93-237 8.37e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796   93 ETTKPLSAGKQETLADGRSDATKETDGDSKEKSDA-IDAVGKQETQGD-EISAKTKDIidGGEKEMSEAVNSVEGGGAVN 170
Cdd:TIGR00927  649 GERPTEAEGENGEESGGEAEQEGETETKGENESEGeIPAERKGEQEGEgEIEAKEADH--KGETEAEEVEHEGETEAEGT 726

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063711796  171 KNEDEIKTTMVTEVAAGEETVKDDNNNSNTVEGSDCVVKDTGGNQTEKEGKEGDG----NEDTEKNGDSGA 237
Cdd:TIGR00927  727 EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGeiqaGEDGEMKGDEGA 797
 
Name Accession Description Interval E-value
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 326-443 2.09e-68

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.


Pssm-ID: 269990  Cd Length: 117  Bit Score: 213.85  E-value: 2.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGGWKERGKGELKVNISTTeNRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGITFAC 405
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFIDGGWKERGKGELRVNLSTT-TGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFAC 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063711796 406 VNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDSK 443
Cdd:cd13169    80 VNSAADAKDKLSTFALKFKDPQVVEEFRAAVEAHKDSA 117
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 326-440 7.92e-29

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: 109.61  E-value: 7.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGG--WKERGKGELKVNISTTENrKARLVMRSKGNYRLTLNASLYPEMKLAKMDK--KGI 401
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETkeWKERGVGDLKILKNKDTG-KYRIVMRRDQVLKLCCNHYILPDMKLTKMGNndRAW 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063711796 402 TFACVNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHK 440
Cdd:cd00835    80 VWTAMDDSEDGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 320-438 1.37e-20

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: 87.44  E-value: 1.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796  320 QDVSVETGEENEKAAFTADSVMFEY--LEGGWKERGKGELKVNISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMD 397
Cdd:smart00160   8 PDVEVKTGEEDEEVIFSARAKLYRFanDKKEWKERGVGDLKILKSKDNGGKVRIVMRRDGVLKVCANHPIFKSMTLKPLA 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1063711796  398 K--KGITFACVNSVSDAKDgLSTLALKFKDPTVVEEFRAVIEE 438
Cdd:smart00160  88 GsnRALKWTPEDFADDIPK-LVLYAVRFKTKEEADSFKNIFEE 129
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 326-438 7.97e-16

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: 73.42  E-value: 7.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEY--LEGGWKERGKGELKVNISTTENR-KARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGIT 402
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFdkSKQSWKERGRGTLRLNDSKSDGSgQSRIVMRTQGSLRVILNTKIWPGMTVEKVSEKSLR 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063711796 403 FACVnsvsDAKDGLSTLALKFKDPTvVEEFRAVIEE 438
Cdd:cd13180    81 ITAM----DDEGQVKVFLLQASPED-AKQLYNAIQD 111
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 322-440 1.02e-15

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: 73.76  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 322 VSVETGEENEKAAFTADSVMFEYLEGG----WKERGKGELKVnISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMd 397
Cdd:cd13179    13 VEVKTGEEDEEVLFKMRAKLYRFDTENdppeWKERGTGDVKL-LKHKETKKIRLLMRRDKTLKICANHYITPEMKLKPN- 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063711796 398 kKGITFACVNSVSDAKDG---LSTLALKFKDPTVVEEFRAVIEEHK 440
Cdd:cd13179    91 -AGSDRAWVWTCADFADEepkPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 326-440 1.39e-15

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: 72.64  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGG-WKERGKGELKVNiSTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGITFA 404
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKKDDGeWKDKGVGTLRLK-KHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVG 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063711796 405 CVNSvsdaKDGLSTLALKFKDPTVVEEFRAVIEEHK 440
Cdd:cd13170    80 CVPN----PGKPVTYLLRVKTAEDADELAKALEEEK 111
Ran_BP1 pfam00638
RanBP1 domain;
324-440 3.65e-15

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 71.69  E-value: 3.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 324 VETGEENEKAAFTADSVMFEY--LEGGWKERGKGELKVNISTtENRKARLVMRSKGNYRLTLNASLYPEMKLAKMdkKGI 401
Cdd:pfam00638   2 VKTGEEDEEVLFSQRAKLFRFdaEVKQWKERGVGDIKILKNK-DDGKVRILMRRDQVLKVCANHYITPDMTLKPL--AGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063711796 402 TFACVNSVSDAKDG---LSTLALKFKDPTVVEEFRAVIEEHK 440
Cdd:pfam00638  79 DRSWVWTAADFADGegkPEQLAIRFKTKEEADSFKKKFEEAQ 120
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 326-438 4.14e-15

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: 71.28  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGG--WKERGKGELKVnISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMD--KKGI 401
Cdd:cd13174     1 TGEEDETKLFGERAKLYRFDADTkeWKERGVGEMKI-LYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNtsDKSF 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063711796 402 TFACVNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEE 438
Cdd:cd13174    80 TWGGMNYAEDAEPEVETLAVRFKNEEIASQFKNVVDQ 116
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 326-440 8.22e-15

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: 70.77  E-value: 8.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLE--GGWKERGKGELKVnISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMdkKGITF 403
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKdaAQWKERGIGDLKI-LQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPM--KGSER 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063711796 404 ACVNSVSDAKDG---LSTLALKFKDPTVVEEFRAVIEEHK 440
Cdd:cd14685    78 AWVWTAMDFAEGegkIEQLAVRFKLQETADTFKQIFDEAK 117
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 326-442 1.21e-14

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: 70.19  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGGWKERGKGELKVnISTTENRKARLVMRSKGNYRLTLNASLYPEMKL--AKMDKKGITF 403
Cdd:cd13171     1 TGEENEEVLFCARAKLFRYVDKEWKERGIGNLKI-LKNPATGKVRLLMRREQVHKVCANHFITKDMELtpMKKEDKAYIW 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063711796 404 AcVNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDS 442
Cdd:cd13171    80 A-ANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKKE 117
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 326-442 2.12e-14

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: 69.43  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGGWKERGKGELKVnISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGITFAc 405
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVDKEWKERGLGDVKI-LRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKKDEKSWMWA- 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063711796 406 VNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEEHKDS 442
Cdd:cd13173    79 AHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE 115
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 326-438 6.14e-13

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: 65.16  E-value: 6.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLEGG--WKERGKGELKVNISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMDK--KGI 401
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATkeWKERGLGNIKLLRNKEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNnpKAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063711796 402 TFaCVNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEE 438
Cdd:cd13172    81 TW-CAQDYSEGELKPETFAIRFKTQEICKDFLDAVKK 116
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 326-438 6.68e-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: 64.99  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLE--GGWKERGKGELKVnISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMdkKGITF 403
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKdvKQWKERGVGDIKI-LQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPN--AGSDR 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063711796 404 ACVNSVSDAKDGLST---LALKFKDPTVVEEFRAVIEE 438
Cdd:cd13176    78 SWVWTALDFSEEEPKveqLAVKFKTPEVADEFKKKFEE 115
NUP50 pfam08911
NUP50 (Nucleoporin 50 kDa); Nucleoporin 50 kDa (NUP50) acts as a cofactor for the ...
 13-77 8.05e-13

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: 63.51  E-value: 8.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796  13 KRTALKELSRDNPgldDDDEDTSALESGTFNTASKEVLASRRIIRVRR-----TDRSATAPPASNPFTGI 77
Cdd:pfam08911   2 KRGADKQLTRDNW---DEDEDEDEEEAGTFKKASEEVLAKRKIKKAKRrmgssTPSSAASSSAFSGFSGF 68
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 326-438 2.30e-12

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: 63.53  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEY--LEGGWKERGKGELKVnISTTENRKARLVMRSK------GNYRLTLNASLYPemkLAKMD 397
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFdaSVSQWKERGVGNLKI-LKNAVNGKLRMLMRREqvlkvcANHWITTTMNLKP---LAGSD 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1063711796 398 KKGITFAcvNSVSDAKDGLSTLALKFKDPTVVEEFRAVIEE 438
Cdd:cd13177    77 RAWMWMA--NDFSDGDAKLEQLAAKFKTPELAEEFKLKFEE 115
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 326-438 1.22e-08

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: 53.03  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEYLE--GGWKERGKGELKVNISTTENrKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGITF 403
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRdvGQWKERGVGDIKILFHPSKH-YYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTL 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063711796 404 acVNSVSDAKDG---LSTLALKFKDPTVVEEFRAVIEE 438
Cdd:cd13178    80 --VWTATDYADGegkVEQLAVRFKTKEIADSFKKVFEE 115
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 326-440 1.28e-08

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: 52.82  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEY----LEGGWKERGKGELKVnISTTENRKARLVMRSKGNYRLTLNASLYPEMKLAKMDKKGI 401
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFdpsnTESPYTSKGVGELKL-LKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGSL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063711796 402 TFACVNSvSDAKdgLSTLALKFKDPTVVEEFRAVIEEHK 440
Cdd:cd13181    80 VRVPTIN-SDGK--IETYVIKVKTAADGEELLKALNDAK 115
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 326-438 1.14e-06

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: 47.33  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 326 TGEENEKAAFTADSVMFEY--LEGGWKERGKGELKVNISTTENrKARLVMRSKGNYRLTLNASLYPEMKL---AKMDKKG 400
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFdvETKEWKERGIGNVKILRHKTSG-KIRLLMRREQVLKICANHYISADMKLkpnAGSDKSF 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063711796 401 ITFACvnSVSDAKDGLSTLALKFKDPTVVEEFRAVIEE 438
Cdd:cd14684    80 VWNAL--DYADELPKPEQLAIRFKTVEEAALFKCKFEE 115
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
319-423 3.40e-05

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 45.01  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796 319 KQDVSVETGEENEKAAFTADSVMFEYLEGG--WKERGKGELKVNISTTENrKARLVMRSKGNYRLTLNASLYPEMKLAKM 396
Cdd:COG5171    77 LQRVHLKTNEEDETVLFKARAKLFRFDEEAkeWKERGTGDMIILKHKKTN-KARITMRRDKTLKLCANHFINPEFKLQPN 155

                          90       100
                  ....*....|....*....|....*....
gi 1063711796 397 DK--KGITFACVNSVSDAKDGLSTLALKF 423
Cdd:COG5171   156 VGsdRSWVWMSTADTVEGEAKAQTFAIRF 184
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 93-237 8.37e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 41.90  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063711796   93 ETTKPLSAGKQETLADGRSDATKETDGDSKEKSDA-IDAVGKQETQGD-EISAKTKDIidGGEKEMSEAVNSVEGGGAVN 170
Cdd:TIGR00927  649 GERPTEAEGENGEESGGEAEQEGETETKGENESEGeIPAERKGEQEGEgEIEAKEADH--KGETEAEEVEHEGETEAEGT 726

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063711796  171 KNEDEIKTTMVTEVAAGEETVKDDNNNSNTVEGSDCVVKDTGGNQTEKEGKEGDG----NEDTEKNGDSGA 237
Cdd:TIGR00927  727 EDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGeiqaGEDGEMKGDEGA 797
 
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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