NEDD8-activating enzyme E1 regulatory subunit isoform c [Homo sapiens]
NEDD8-activating enzyme E1 regulatory subunit( domain architecture ID 10107339)
NEDD8-activating enzyme E1 regulatory subunit is a component of the dimeric UBA3-NAE1 E1 enzyme that activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP
List of domain hits
Name | Accession | Description | Interval | E-value | |||||||
APPBP1_RUB | cd01493 | Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ... |
1-443 | 0e+00 | |||||||
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain. : Pssm-ID: 238770 [Multi-domain] Cd Length: 425 Bit Score: 569.24 E-value: 0e+00
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Ube1 super family | cl36897 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
321-424 | 3.08e-07 | |||||||
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions. The actual alignment was detected with superfamily member TIGR01408: Pssm-ID: 273603 [Multi-domain] Cd Length: 1006 Bit Score: 52.97 E-value: 3.08e-07
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Name | Accession | Description | Interval | E-value | |||||||
APPBP1_RUB | cd01493 | Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ... |
1-443 | 0e+00 | |||||||
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain. Pssm-ID: 238770 [Multi-domain] Cd Length: 425 Bit Score: 569.24 E-value: 0e+00
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Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
321-424 | 3.08e-07 | |||||||
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions. Pssm-ID: 273603 [Multi-domain] Cd Length: 1006 Bit Score: 52.97 E-value: 3.08e-07
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Name | Accession | Description | Interval | E-value | |||||||
APPBP1_RUB | cd01493 | Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ... |
1-443 | 0e+00 | |||||||
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain. Pssm-ID: 238770 [Multi-domain] Cd Length: 425 Bit Score: 569.24 E-value: 0e+00
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E1-1_like | cd01485 | Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ... |
1-77 | 7.26e-31 | |||||||
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1. Pssm-ID: 238762 [Multi-domain] Cd Length: 198 Bit Score: 117.52 E-value: 7.26e-31
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E1-1_like | cd01485 | Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ... |
403-443 | 8.59e-13 | |||||||
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1. Pssm-ID: 238762 [Multi-domain] Cd Length: 198 Bit Score: 67.06 E-value: 8.59e-13
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E1_enzyme_family | cd01483 | Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
1-77 | 3.22e-10 | |||||||
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. Pssm-ID: 238760 [Multi-domain] Cd Length: 143 Bit Score: 58.05 E-value: 3.22e-10
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Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
321-424 | 3.08e-07 | |||||||
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions. Pssm-ID: 273603 [Multi-domain] Cd Length: 1006 Bit Score: 52.97 E-value: 3.08e-07
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Aos1_SUMO | cd01492 | Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ... |
404-437 | 9.88e-03 | |||||||
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain. Pssm-ID: 238769 [Multi-domain] Cd Length: 197 Bit Score: 37.27 E-value: 9.88e-03
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Blast search parameters | ||||
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