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Conserved domains on  [gi|30699531|ref|NP_178183|]
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SUPPRESSOR OF AUXIN RESISTANCE 3 [Arabidopsis thaliana]

Protein Classification

Nucleoporin2 and Nup96 domain-containing protein( domain architecture ID 10513691)

Nucleoporin2 and Nup96 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nup96 pfam12110
Nuclear protein 96; Nup96 (often known by the name of its yeast homolog Nup145C) is part of ...
579-858 3.92e-96

Nuclear protein 96; Nup96 (often known by the name of its yeast homolog Nup145C) is part of the Nup84 heptameric complex in the nuclear pore complex. Nup96 complexes with Sec13 in the middle of the heptamer. The function of the heptamer is to coat the curvature of the nuclear pore complex between the inner and outer nuclear membranes. Nup96 is predicted to be an alpha helical solenoid. The interaction between Nup96 and Sec13 is the point of curvature in the heptameric complex.


:

Pssm-ID: 463462  Cd Length: 287  Bit Score: 306.06  E-value: 3.92e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    579 EHLFFLLTGRELDSAVELAISKGDVRLACLLSQAGGSTVNRNDILQQLHLWRRNGLDFnFIEKERIKLYELLAGNIHDAL 658
Cdd:pfam12110    1 EKAFALLTGHRVEEACELAIDSGDFRLATLLSQAGGDDSFREDMAEQLDDWRESGVDS-EIDEPRRKLYELLAGNVLVSE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    659 Q---DFTI----DWKRFLGLLMWHHLPPDSSLPIIFRSYQLLLNQAKAP-WPVPIYIDEGPADGFVSDN--KHSDILYYL 728
Cdd:pfam12110   80 GkksTINIseglDWKRAFGLRLWYGIPPDTSIEDAVEAYEEALSQGREPaPPLPWYLEEGDSESWEDPRlkKREDLLYHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    729 MLLHSKeeeEFGFLQTMFSAFSSTDDPLDYHMIWHHRGILEAV----GAFTSDDLHTLDMGFVAQLLSQGLCHWAIYVVL 804
Cdd:pfam12110  160 LKLYAD---PTAPLEAVLDPESSSPDPLDYRLSWHLYQVLSAVrlgyGHLSSAKADQLTLSFASQLESLGLWQWAVFVLL 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 30699531    805 HIPfredHPYLHVTVIREILFQYCETWSSMESQRQFI-KDLGIPSEWMHEALAVY 858
Cdd:pfam12110  237 HLE----DPARRERAVRELLARHAELISEDDAKERFLtEKLKIPEAWIHEAKALY 287
Nucleoporin2 pfam04096
Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional ...
51-187 1.93e-51

Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional transport across the nucleoporin complex in nucleocytoplasmic transport. The mammalian nuclear pore complex (NPC) is comprised of approximately 30 unique proteins, collectively known as nucleoporins. This family includes yeast family members such as Nup145p as well as vertebrate Nup98. The NUP C-terminal domains of Nup98 and Nup145 possess peptidase S59 autoproteolytic activity. The autoproteolytic sites of Nup98 and Nup145 each occur immediately C-terminal to the NUP C-terminal domain. Thus, although this domain occurs in the middle of each precursor polypeptide, it winds up at the C-terminal end of the N-terminal cleavage product. Cleavage of the peptide chains are necessary for the proper targeting to the nuclear pore.


:

Pssm-ID: 461171  Cd Length: 143  Bit Score: 177.30  E-value: 1.93e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531     51 SPDYFLKPCINELVEReieSPDYCSRVPDFTIGRIGYGYIRFLGNTDVRRLDLDHI----VKFHRHEVIVYDDESSKPVV 126
Cdd:pfam04096    1 KGDYWTSPSLEELKKM---SREQLSSVENFTVGRKGYGSVRFLGPVDLTGLDLDEIfgkiVKFEPREVTVYPDESSKPPV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    127 GEGLNKAAEVTLVVNIPDLTWGKQQV---------NHIAyKLKQSterQGATFISFDPDNGLWKFFVPHF 187
Cdd:pfam04096   78 GQGLNVPATITLENVWPRDKDTKEPIkdpsgprleKHIE-RLKRV---QGTEFVSYDPETGTWTFKVEHF 143
 
Name Accession Description Interval E-value
Nup96 pfam12110
Nuclear protein 96; Nup96 (often known by the name of its yeast homolog Nup145C) is part of ...
579-858 3.92e-96

Nuclear protein 96; Nup96 (often known by the name of its yeast homolog Nup145C) is part of the Nup84 heptameric complex in the nuclear pore complex. Nup96 complexes with Sec13 in the middle of the heptamer. The function of the heptamer is to coat the curvature of the nuclear pore complex between the inner and outer nuclear membranes. Nup96 is predicted to be an alpha helical solenoid. The interaction between Nup96 and Sec13 is the point of curvature in the heptameric complex.


Pssm-ID: 463462  Cd Length: 287  Bit Score: 306.06  E-value: 3.92e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    579 EHLFFLLTGRELDSAVELAISKGDVRLACLLSQAGGSTVNRNDILQQLHLWRRNGLDFnFIEKERIKLYELLAGNIHDAL 658
Cdd:pfam12110    1 EKAFALLTGHRVEEACELAIDSGDFRLATLLSQAGGDDSFREDMAEQLDDWRESGVDS-EIDEPRRKLYELLAGNVLVSE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    659 Q---DFTI----DWKRFLGLLMWHHLPPDSSLPIIFRSYQLLLNQAKAP-WPVPIYIDEGPADGFVSDN--KHSDILYYL 728
Cdd:pfam12110   80 GkksTINIseglDWKRAFGLRLWYGIPPDTSIEDAVEAYEEALSQGREPaPPLPWYLEEGDSESWEDPRlkKREDLLYHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    729 MLLHSKeeeEFGFLQTMFSAFSSTDDPLDYHMIWHHRGILEAV----GAFTSDDLHTLDMGFVAQLLSQGLCHWAIYVVL 804
Cdd:pfam12110  160 LKLYAD---PTAPLEAVLDPESSSPDPLDYRLSWHLYQVLSAVrlgyGHLSSAKADQLTLSFASQLESLGLWQWAVFVLL 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 30699531    805 HIPfredHPYLHVTVIREILFQYCETWSSMESQRQFI-KDLGIPSEWMHEALAVY 858
Cdd:pfam12110  237 HLE----DPARRERAVRELLARHAELISEDDAKERFLtEKLKIPEAWIHEAKALY 287
Nucleoporin2 pfam04096
Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional ...
51-187 1.93e-51

Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional transport across the nucleoporin complex in nucleocytoplasmic transport. The mammalian nuclear pore complex (NPC) is comprised of approximately 30 unique proteins, collectively known as nucleoporins. This family includes yeast family members such as Nup145p as well as vertebrate Nup98. The NUP C-terminal domains of Nup98 and Nup145 possess peptidase S59 autoproteolytic activity. The autoproteolytic sites of Nup98 and Nup145 each occur immediately C-terminal to the NUP C-terminal domain. Thus, although this domain occurs in the middle of each precursor polypeptide, it winds up at the C-terminal end of the N-terminal cleavage product. Cleavage of the peptide chains are necessary for the proper targeting to the nuclear pore.


Pssm-ID: 461171  Cd Length: 143  Bit Score: 177.30  E-value: 1.93e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531     51 SPDYFLKPCINELVEReieSPDYCSRVPDFTIGRIGYGYIRFLGNTDVRRLDLDHI----VKFHRHEVIVYDDESSKPVV 126
Cdd:pfam04096    1 KGDYWTSPSLEELKKM---SREQLSSVENFTVGRKGYGSVRFLGPVDLTGLDLDEIfgkiVKFEPREVTVYPDESSKPPV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    127 GEGLNKAAEVTLVVNIPDLTWGKQQV---------NHIAyKLKQSterQGATFISFDPDNGLWKFFVPHF 187
Cdd:pfam04096   78 GQGLNVPATITLENVWPRDKDTKEPIkdpsgprleKHIE-RLKRV---QGTEFVSYDPETGTWTFKVEHF 143
 
Name Accession Description Interval E-value
Nup96 pfam12110
Nuclear protein 96; Nup96 (often known by the name of its yeast homolog Nup145C) is part of ...
579-858 3.92e-96

Nuclear protein 96; Nup96 (often known by the name of its yeast homolog Nup145C) is part of the Nup84 heptameric complex in the nuclear pore complex. Nup96 complexes with Sec13 in the middle of the heptamer. The function of the heptamer is to coat the curvature of the nuclear pore complex between the inner and outer nuclear membranes. Nup96 is predicted to be an alpha helical solenoid. The interaction between Nup96 and Sec13 is the point of curvature in the heptameric complex.


Pssm-ID: 463462  Cd Length: 287  Bit Score: 306.06  E-value: 3.92e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    579 EHLFFLLTGRELDSAVELAISKGDVRLACLLSQAGGSTVNRNDILQQLHLWRRNGLDFnFIEKERIKLYELLAGNIHDAL 658
Cdd:pfam12110    1 EKAFALLTGHRVEEACELAIDSGDFRLATLLSQAGGDDSFREDMAEQLDDWRESGVDS-EIDEPRRKLYELLAGNVLVSE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    659 Q---DFTI----DWKRFLGLLMWHHLPPDSSLPIIFRSYQLLLNQAKAP-WPVPIYIDEGPADGFVSDN--KHSDILYYL 728
Cdd:pfam12110   80 GkksTINIseglDWKRAFGLRLWYGIPPDTSIEDAVEAYEEALSQGREPaPPLPWYLEEGDSESWEDPRlkKREDLLYHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    729 MLLHSKeeeEFGFLQTMFSAFSSTDDPLDYHMIWHHRGILEAV----GAFTSDDLHTLDMGFVAQLLSQGLCHWAIYVVL 804
Cdd:pfam12110  160 LKLYAD---PTAPLEAVLDPESSSPDPLDYRLSWHLYQVLSAVrlgyGHLSSAKADQLTLSFASQLESLGLWQWAVFVLL 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 30699531    805 HIPfredHPYLHVTVIREILFQYCETWSSMESQRQFI-KDLGIPSEWMHEALAVY 858
Cdd:pfam12110  237 HLE----DPARRERAVRELLARHAELISEDDAKERFLtEKLKIPEAWIHEAKALY 287
Nucleoporin2 pfam04096
Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional ...
51-187 1.93e-51

Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional transport across the nucleoporin complex in nucleocytoplasmic transport. The mammalian nuclear pore complex (NPC) is comprised of approximately 30 unique proteins, collectively known as nucleoporins. This family includes yeast family members such as Nup145p as well as vertebrate Nup98. The NUP C-terminal domains of Nup98 and Nup145 possess peptidase S59 autoproteolytic activity. The autoproteolytic sites of Nup98 and Nup145 each occur immediately C-terminal to the NUP C-terminal domain. Thus, although this domain occurs in the middle of each precursor polypeptide, it winds up at the C-terminal end of the N-terminal cleavage product. Cleavage of the peptide chains are necessary for the proper targeting to the nuclear pore.


Pssm-ID: 461171  Cd Length: 143  Bit Score: 177.30  E-value: 1.93e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531     51 SPDYFLKPCINELVEReieSPDYCSRVPDFTIGRIGYGYIRFLGNTDVRRLDLDHI----VKFHRHEVIVYDDESSKPVV 126
Cdd:pfam04096    1 KGDYWTSPSLEELKKM---SREQLSSVENFTVGRKGYGSVRFLGPVDLTGLDLDEIfgkiVKFEPREVTVYPDESSKPPV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699531    127 GEGLNKAAEVTLVVNIPDLTWGKQQV---------NHIAyKLKQSterQGATFISFDPDNGLWKFFVPHF 187
Cdd:pfam04096   78 GQGLNVPATITLENVWPRDKDTKEPIkdpsgprleKHIE-RLKRV---QGTEFVSYDPETGTWTFKVEHF 143
 
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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