RecName: Full=Nuclear pore complex protein NUP96; Short=AtNUP96; AltName: Full=Nucleoporin 96; AltName: Full=Nucleoporin PRECOCIOUS; AltName: Full=Nucleoporin PRECOZ; AltName: Full=Protein MODIFIER OF SNC1 3; AltName: Full=Protein SUPPRESSOR OF AUXIN RESISTANCE 3
Protein Classification
Nucleoporin2 and Nup96 domain-containing protein( domain architecture ID 10513691)
Nucleoporin2 and Nup96 domain-containing protein
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
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| 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
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| 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
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| 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
|
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| 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
|
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| 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
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