2Y8G


Conserved Protein Domain Family
RanBD_RanBP3

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cd13180: RanBD_RanBP3 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 270001
Aligned: 31 rows
Threshold Bit Score: 110.399
Created: 17-Jul-2012
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative RAN
Conserved site includes 25 residues -Click on image for an interactive view with Cn3D
Feature 1:putative RAN binding site [polypeptide binding site]
Evidence:
  • Comment:Binding of RanBP to the C-terminus of Ran causes dissociation of Ran-GTP from importin-beta-related transport factors

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                      # ###       ######                     # # ##    ###  # #   #   # 
2Y8G_A         9 TGEEAESNVLQMQCKLFVFDkt---sQSWVAVGRGLLRLNDMAstd-dgtLQSRLVMRTQg-SLRLILNTKLWaQMQIDK 83  human
EFO20575     230 TGEEGEINIYRAVCKLHSFDss---aKSWVERGMSCLRINERGee---ppYTYRIVGRVMg-NQRVVLNSQIFpDMIVEK 302 Loa loa
NP_495208    147 TGEENDTNIFQAPCKIWAFDkl---kNAYSEKGVCNLRINKRVen---glTHHRIVARTSsgTLRVIINSKIFsDMLLER 220 nematode
Q09146       270 TGEEEEESIFSVRARLYVVAde---kKTWKERGQGILKVNVPKqr---gsGSGRLLMRNDa-VHRVIMNVPLFqGMSKKS 342 Schizosaccharom...
XP_001275375 346 TGEEEEKTYFSCKAKLFQFTn-----KEWKERGLGTFKVNVKVkdgkedkKAARMLMRADg-VLRVMLNSPIFkGMKVGD 419 Aspergillus cla...
XP_003294034 174 TGEEDETVLFSVRARLYIVQd-----QQYKERGTGVVRINKNIe------NKSRIIMNVDg-SKKVILNTNIFgKMSIDA 241 Dictyostelium p...
XP_642253    260 TGEEDETTLCSTKGKLYILQd-----KQYKERGVGTIRVNKDLe------EKSRIIMNADg-SKKNILNVNIFpKMKVTS 327 Dictyostelium d...
XP_001322207 118 NSEENENILFNNTAKLYAFVvdenekGRYSQRFTGTLHLNECS-------DFSRIVMRNT--LGKVCLNCRLFkQMNPSL 188 Trichomonas vag...
XP_001309379 110 SGEENDEILMDCKAMLHELVvgknksSSWAERGSGNLHFNKSE-------GGYRLTMRRQq-LKTPCLNARLFkGMHVEP 181 Trichomonas vag...
P40517       207 SGEESEECIYQVNAKLYQLSni---kEGWKERGVGIIKINKSKdd----vEKTRIVMRSRg-ILKVILNIQLVkGFTVQK 278 Saccharomyces c...
Feature 1                       # #            #   #                       
2Y8G_A        84 As---------EKSIRITAMDTEDq--gVKVFLISA------SSKDTGQLYAALHHRI 124 human
EFO20575     303 Ls---------MRRVKFSATAPDSe--vPALFLATA------SEFVAAQLYGTLSRIV 343 Loa loa
NP_495208    221 V----------DKRIRISAMGPEIs--gVQIFLLKIgftkteTIPDSDIFYNIMSDLL 266 nematode
Q09146       343 LqiasassggsANYLKIFVIENGK----SVLYAVRVk-----DNSLAEQLRNHVLEAI 391 Schizosaccharomyces pombe 972h-
XP_001275375 420 Gags----epkSKQIHLAGVEDGR----TVPLLLRTg-----NEELAKELYHVIQDLL 464 Aspergillus clavatus NRRL 1
XP_003294034 242 Pn---------EKSIKFIGFDSENqf-kFATFLLKLg-----KAEDVKTFINKVKAQI 284 Dictyostelium purpureum
XP_642253    328 Pn---------EKTLTFIAFEDDK----ICTFVLIA------KPEEIKNFSTVINKQI 366 Dictyostelium discoideum AX4
XP_001322207 189 Qg---------QNFVKILLQNSEGn---YQVSLLQFk-----DSSLANSFLSSLQQLL 229 Trichomonas vaginalis G3
XP_001309379 182 Vk---------TNKIKFNAVKIEKdqqtLATYLLTV------NTADRDPLLTKIQDAL 224 Trichomonas vaginalis G3
P40517       279 Gftgs---lqsEKFIRLLAVDDNGd---PAQYAIKTg-----KKETTDELYNIIVKSV 325 Saccharomyces cerevisiae S288c

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