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Conserved domains on  [gi|1246742122|ref|NP_001342890|]
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Ran GTPase-binding protein Hba1 [Schizosaccharomyces pombe]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 257-390 2.63e-42

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member smart00160:

Pssm-ID: 473070  Cd Length: 130  Bit Score: 144.84  E-value: 2.63e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122  257 KSTMHQLSDSEIITGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRGsGSGRLLMRNDAVHRVIMNVPLFQ 336
Cdd:smart00160   1 FKPVVPLPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNG-GKVRIVMRRDGVLKVCANHPIFK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246742122  337 GMSKKSLQiasassgGSANYLKIFVIENGKS----VLYAVRVKDNSLAEQLRNHVLEA 390
Cdd:smart00160  80 SMTLKPLA-------GSNRALKWTPEDFADDipklVLYAVRFKTKEEADSFKNIFEEA 130
 
Name Accession Description Interval E-value
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 257-390 2.63e-42

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: 144.84  E-value: 2.63e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122  257 KSTMHQLSDSEIITGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRGsGSGRLLMRNDAVHRVIMNVPLFQ 336
Cdd:smart00160   1 FKPVVPLPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNG-GKVRIVMRRDGVLKVCANHPIFK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246742122  337 GMSKKSLQiasassgGSANYLKIFVIENGKS----VLYAVRVKDNSLAEQLRNHVLEA 390
Cdd:smart00160  80 SMTLKPLA-------GSNRALKWTPEDFADDipklVLYAVRFKTKEEADSFKNIFEEA 130
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 270-391 1.49e-29

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: 110.40  E-value: 1.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSkkslqIASAS 349
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMT-----VEKVS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1246742122 350 SggsaNYLKIFVIENGKSV-LYAVRVKDnSLAEQLRNHVLEAI 391
Cdd:cd13180    76 E----KSLRITAMDDEGQVkVFLLQASP-EDAKQLYNAIQDRI 113
Ran_BP1 pfam00638
RanBP1 domain;
267-393 5.30e-14

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 68.22  E-value: 5.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 267 EIITGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNvpKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLqia 346
Cdd:pfam00638   1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKIL--KNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPL--- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1246742122 347 sasSGGSANYLKI---FVIENGKSVLYAVRVKDNSLAEQLRNHVLEAIPK 393
Cdd:pfam00638  76 ---AGSDRSWVWTaadFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
199-331 4.81e-04

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 41.16  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 199 VETESGSGKEKENDKKSSeNFDELLANTSAKAFENQKGSAGETKSEPKEADKGSGDSTKST----MHQLSDSEIITGEEE 274
Cdd:COG5171    10 AKIEKEENEQKERSLDVV-SKGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKGPESPNIhfepVVELQRVHLKTNEED 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742122 275 EESIFSVRARLYVVADEKKTWKERGQGILKVNvpKQRGSGSGRLLMRNDAVHRVIMN 331
Cdd:COG5171    89 ETVLFKARAKLFRFDEEAKEWKERGTGDMIIL--KHKKTNKARITMRRDKTLKLCAN 143
 
Name Accession Description Interval E-value
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 257-390 2.63e-42

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: 144.84  E-value: 2.63e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122  257 KSTMHQLSDSEIITGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRGsGSGRLLMRNDAVHRVIMNVPLFQ 336
Cdd:smart00160   1 FKPVVPLPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNG-GKVRIVMRRDGVLKVCANHPIFK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246742122  337 GMSKKSLQiasassgGSANYLKIFVIENGKS----VLYAVRVKDNSLAEQLRNHVLEA 390
Cdd:smart00160  80 SMTLKPLA-------GSNRALKWTPEDFADDipklVLYAVRFKTKEEADSFKNIFEEA 130
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 270-391 1.49e-29

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: 110.40  E-value: 1.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSkkslqIASAS 349
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMT-----VEKVS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1246742122 350 SggsaNYLKIFVIENGKSV-LYAVRVKDnSLAEQLRNHVLEAI 391
Cdd:cd13180    76 E----KSLRITAMDDEGQVkVFLLQASP-EDAKQLYNAIQDRI 113
Ran_BP1 pfam00638
RanBP1 domain;
267-393 5.30e-14

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 68.22  E-value: 5.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 267 EIITGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNvpKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLqia 346
Cdd:pfam00638   1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKIL--KNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPL--- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1246742122 347 sasSGGSANYLKI---FVIENGKSVLYAVRVKDNSLAEQLRNHVLEAIPK 393
Cdd:pfam00638  76 ---AGSDRSWVWTaadFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 270-391 3.15e-13

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: 65.70  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNvpKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLqiasas 349
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKIL--KNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKM------ 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1246742122 350 sGGSANYLKIFVI-----ENGKSVLYAVRVKDNSLAEQLRNHVLEAI 391
Cdd:cd00835    73 -GNNDRAWVWTAMddsedGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 270-391 7.89e-13

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: 64.55  E-value: 7.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVaDEKKTWKERGQGILKVNvpKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMsKKSLQiasas 349
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKK-KDDGEWKDKGVGTLRLK--KHKTTGKARILVRADTLGKILLNFLLYKGM-PYSVA----- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1246742122 350 sgGSANYLKIFVIENGKSVLYAVRVKDNSLAEQLRNHVLEAI 391
Cdd:cd13170    72 --GKNNVFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK 111
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 270-394 3.94e-12

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: 62.85  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADekKTWKERGQGILKVNVPKqrGSGSGRLLMRNDAVHRVIMNVPLFQGMS-----KKSLQ 344
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLST--TTGQARLVMRARGNYRLILNANLYPDMKltkmgGKGVT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1246742122 345 IASASSGGSAnylkifvieNGKSVLYAVRVKDNSLAEQLRNHVLEAIPKG 394
Cdd:cd13169    77 FACVNSAADA---------KDKLSTFALKFKDPQVVEEFRAAVEAHKDSA 117
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 270-391 1.91e-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: 55.11  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRgsGSGRLLMRNDAVHRVIMNVPLFQ-------GMSKKS 342
Cdd:cd13174     1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPEL--NTYRLLMRREQVHKVVLNMLITSdlqlrpmNTSDKS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1246742122 343 LqiasasSGGSANYlkifvIENGKSVL--YAVRVKDNSLAEQLRNHVLEAI 391
Cdd:cd13174    79 F------TWGGMNY-----AEDAEPEVetLAVRFKNEEIASQFKNVVDQCQ 118
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 270-390 1.40e-08

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: 52.66  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKvnVPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLQiasas 349
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIK--ILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNA----- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1246742122 350 sgGSANYLKIFVI----ENGKSVLYAVRVKDNSLAEQLRNHVLEA 390
Cdd:cd13176    74 --GSDRSWVWTALdfseEEPKVEQLAVKFKTPEVADEFKKKFEEA 116
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 262-343 3.34e-07

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: 49.10  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 262 QLSDSEIITGEEEEESIFSVRARLYVVADE--KKTWKERGQGILKvnVPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMS 339
Cdd:cd13179     9 KLPEVEVKTGEEDEEVLFKMRAKLYRFDTEndPPEWKERGTGDVK--LLKHKETKKIRLLMRRDKTLKICANHYITPEMK 86


                  ....
gi 1246742122 340 KKSL 343
Cdd:cd13179    87 LKPN 90
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 270-355 5.93e-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: 47.85  E-value: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADekKTWKERGQGILKVnvPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLQIASAS 349
Cdd:cd13171     1 TGEENEEVLFCARAKLFRYVD--KEWKERGIGNLKI--LKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKA 76


                  ....*.
gi 1246742122 350 SGGSAN 355
Cdd:cd13171    77 YIWAAN 82
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 270-390 1.41e-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: 46.67  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVnVPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMS-KKSLQIASA 348
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKL-LRNKEDNNKVRLLMRREQVLKVCCNQRLTKDMEfKYLTNNPKA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1246742122 349 SSGGSANYLKifviENGKSVLYAVRVKDNSLAEQLRNHVLEA 390
Cdd:cd13172    80 LTWCAQDYSE----GELKPETFAIRFKTQEICKDFLDAVKKA 117
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 270-331 1.88e-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: 46.56  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGilKVNVPKQRGSGSGRLLMRNDAVHRVIMN 331
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIG--NVKILRHKTSGKIRLLMRREQVLKICAN 60
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 270-354 3.19e-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 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: 45.81  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKvnVPKQRGSGSGRLLMRNDAVHRV--------IMNVPLFQGMSKK 341
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLK--ILKNAVNGKLRMLMRREQVLKVcanhwittTMNLKPLAGSDRA 78

                          90
                  ....*....|...
gi 1246742122 342 SLQIASASSGGSA 354
Cdd:cd13177    79 WMWMANDFSDGDA 91
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 270-385 5.31e-06

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: 45.33  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKVNVPKQRgsGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLQIASAS 349
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSK--HYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNT 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1246742122 350 SGGSANYlkiFVIENGKSVLYAVRVKDNSLAEQLRN 385
Cdd:cd13178    79 LVWTATD---YADGEGKVEQLAVRFKTKEIADSFKK 111
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 270-331 5.38e-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 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: 42.26  E-value: 5.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246742122 270 TGEEEEESIFSVRARLYVVADEKKTWKERGQGILKvnVPKQRGSGSGRLLMRNDAVHRVIMN 331
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLK--ILQNYDNKQVRLVMRRDQVLKLCAN 60
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 270-331 2.38e-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: 40.54  E-value: 2.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246742122 270 TGEEEEESIFSVRARLYVVADekKTWKERGQGilKVNVPKQRGSGSGRLLMRNDAVHRVIMN 331
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLG--DVKILRHKETGKLRLLMRRDQVLKICLN 58
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
199-331 4.81e-04

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 41.16  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 199 VETESGSGKEKENDKKSSeNFDELLANTSAKAFENQKGSAGETKSEPKEADKGSGDSTKST----MHQLSDSEIITGEEE 274
Cdd:COG5171    10 AKIEKEENEQKERSLDVV-SKGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKGPESPNIhfepVVELQRVHLKTNEED 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742122 275 EESIFSVRARLYVVADEKKTWKERGQGILKVNvpKQRGSGSGRLLMRNDAVHRVIMN 331
Cdd:COG5171    89 ETVLFKARAKLFRFDEEAKEWKERGTGDMIIL--KHKKTNKARITMRRDKTLKLCAN 143
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 277-338 5.54e-03

EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269909  Cd Length: 103  Bit Score: 36.29  E-value: 5.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246742122 277 SIFSVRARLYVVADEKKTW-KERGQGILKVNVPKQRGSGSGRLLMRNDAVHRVIMNVPLFQGM 338
Cdd:cd00837     1 SIFSARAHVMQIDDSNKNWvPAGGKGASRVSYFKDTTRNSFRIIGVDIKDKKVVINCTITKNL 63
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 270-375 7.98e-03

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: 35.88  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742122 270 TGEEEEESIFSVRARL--YVVADEKKTWKERGQGILKVNvpKQRGSGSGRLLMRNDAVHRVIMNVPLFQGMSKKSLqias 347
Cdd:cd13181     1 TGEENEEVLYTKRAKLmlFDPSNTESPYTSKGVGELKLL--KNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKM---- 74

                          90       100
                  ....*....|....*....|....*....
gi 1246742122 348 assgGSANYLKIFVI-ENGKSVLYAVRVK 375
Cdd:cd13181    75 ----GNGSLVRVPTInSDGKIETYVIKVK 99
 
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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