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Conserved domains on  [gi|2072556378]
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Chain B, Nuclear pore complex protein Nup98

Protein Classification

Nucleoporin2 domain-containing protein( domain architecture ID 10513689)

Nucleoporin2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nucleoporin2 pfam04096
Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional ...
 10-152 6.34e-66

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: 196.94  E-value: 6.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072556378  10 RDSYYTIPSMEELaRSVDENGECIVNGFTIGREGFGSIYFEGIVNLTNLDLDSI----VHIRRKEVIVYVDDQNKPPLGE 85
Cdd:pfam04096   1 KGDYWTSPSLEEL-KKMSREQLSSVENFTVGRKGYGSVRFLGPVDLTGLDLDEIfgkiVKFEPREVTVYPDESSKPPVGQ 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2072556378  86 GLNRPAQVTLDEVWPIDKTSRCMITSPERLSEMNYKSKLEnasRKQGAQFVDYRPESGSWVFKVNHF 152
Cdd:pfam04096  80 GLNVPATITLENVWPRDKDTKEPIKDPSGPRLEKHIERLK---RVQGTEFVSYDPETGTWTFKVEHF 143
 
Name Accession Description Interval E-value
Nucleoporin2 pfam04096
Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional ...
 10-152 6.34e-66

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: 196.94  E-value: 6.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072556378  10 RDSYYTIPSMEELaRSVDENGECIVNGFTIGREGFGSIYFEGIVNLTNLDLDSI----VHIRRKEVIVYVDDQNKPPLGE 85
Cdd:pfam04096   1 KGDYWTSPSLEEL-KKMSREQLSSVENFTVGRKGYGSVRFLGPVDLTGLDLDEIfgkiVKFEPREVTVYPDESSKPPVGQ 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2072556378  86 GLNRPAQVTLDEVWPIDKTSRCMITSPERLSEMNYKSKLEnasRKQGAQFVDYRPESGSWVFKVNHF 152
Cdd:pfam04096  80 GLNVPATITLENVWPRDKDTKEPIKDPSGPRLEKHIERLK---RVQGTEFVSYDPETGTWTFKVEHF 143
 
Name Accession Description Interval E-value
Nucleoporin2 pfam04096
Nucleoporin autopeptidase; The nuclear pore complex protein plays a role in bidirectional ...
 10-152 6.34e-66

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: 196.94  E-value: 6.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2072556378  10 RDSYYTIPSMEELaRSVDENGECIVNGFTIGREGFGSIYFEGIVNLTNLDLDSI----VHIRRKEVIVYVDDQNKPPLGE 85
Cdd:pfam04096   1 KGDYWTSPSLEEL-KKMSREQLSSVENFTVGRKGYGSVRFLGPVDLTGLDLDEIfgkiVKFEPREVTVYPDESSKPPVGQ 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2072556378  86 GLNRPAQVTLDEVWPIDKTSRCMITSPERLSEMNYKSKLEnasRKQGAQFVDYRPESGSWVFKVNHF 152
Cdd:pfam04096  80 GLNVPATITLENVWPRDKDTKEPIKDPSGPRLEKHIERLK---RVQGTEFVSYDPETGTWTFKVEHF 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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