MULTISPECIES: thiazole biosynthesis adenylyltransferase ThiF [Bacillus]
Protein Classification
thiazole biosynthesis adenylyltransferase ThiF( domain architecture ID 11482849)
thiazole biosynthesis adenylyltransferase ThiF catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK07688 | PRK07688 | thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
1-339 | 0e+00 | ||||||
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated : Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 718.31 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK07688 | PRK07688 | thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
1-339 | 0e+00 | ||||||
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 718.31 E-value: 0e+00
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| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
4-245 | 3.56e-117 | ||||||
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 338.26 E-value: 3.56e-117
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| adenyl_thiF | TIGR02356 | thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ... |
4-206 | 1.87e-110 | ||||||
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine] Pssm-ID: 274094 Cd Length: 202 Bit Score: 319.69 E-value: 1.87e-110
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| ThiF_MoeB_HesA_family | cd00757 | ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
4-232 | 3.38e-108 | ||||||
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, 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. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). Pssm-ID: 238386 [Multi-domain] Cd Length: 228 Bit Score: 315.19 E-value: 3.38e-108
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| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
5-241 | 1.31e-93 | ||||||
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1. Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 278.37 E-value: 1.31e-93
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| AlaDh_PNT_C | smart01002 | Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
11-129 | 1.14e-04 | ||||||
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine. Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 41.72 E-value: 1.14e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK07688 | PRK07688 | thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
1-339 | 0e+00 | ||||||
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 718.31 E-value: 0e+00
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| PRK12475 | PRK12475 | thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
1-339 | 0e+00 | ||||||
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 570.90 E-value: 0e+00
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| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
4-245 | 3.56e-117 | ||||||
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 338.26 E-value: 3.56e-117
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| adenyl_thiF | TIGR02356 | thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ... |
4-206 | 1.87e-110 | ||||||
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine] Pssm-ID: 274094 Cd Length: 202 Bit Score: 319.69 E-value: 1.87e-110
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| ThiF_MoeB_HesA_family | cd00757 | ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
4-232 | 3.38e-108 | ||||||
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, 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. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). Pssm-ID: 238386 [Multi-domain] Cd Length: 228 Bit Score: 315.19 E-value: 3.38e-108
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| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
5-241 | 1.31e-93 | ||||||
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1. Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 278.37 E-value: 1.31e-93
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| PRK08762 | PRK08762 | molybdopterin-synthase adenylyltransferase MoeB; |
4-250 | 1.49e-53 | ||||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 180.21 E-value: 1.49e-53
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| PRK05690 | PRK05690 | molybdopterin biosynthesis protein MoeB; Provisional |
4-206 | 6.46e-53 | ||||||
molybdopterin biosynthesis protein MoeB; Provisional Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 174.65 E-value: 6.46e-53
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| PRK08328 | PRK08328 | hypothetical protein; Provisional |
4-227 | 3.70e-45 | ||||||
hypothetical protein; Provisional Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 154.18 E-value: 3.70e-45
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| PRK05597 | PRK05597 | molybdopterin biosynthesis protein MoeB; Validated |
1-206 | 9.40e-42 | ||||||
molybdopterin biosynthesis protein MoeB; Validated Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 148.87 E-value: 9.40e-42
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| PRK05600 | PRK05600 | thiamine biosynthesis protein ThiF; Validated |
4-280 | 2.51e-38 | ||||||
thiamine biosynthesis protein ThiF; Validated Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 140.02 E-value: 2.51e-38
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| PRK07878 | PRK07878 | molybdopterin biosynthesis-like protein MoeZ; Validated |
4-234 | 6.78e-36 | ||||||
molybdopterin biosynthesis-like protein MoeZ; Validated Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 134.06 E-value: 6.78e-36
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| E1_enzyme_family | cd01483 | Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
26-169 | 3.68e-34 | ||||||
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: 122.38 E-value: 3.68e-34
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| PRK07411 | PRK07411 | molybdopterin-synthase adenylyltransferase MoeB; |
4-224 | 1.48e-31 | ||||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 122.15 E-value: 1.48e-31
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| PRK08644 | PRK08644 | sulfur carrier protein ThiS adenylyltransferase ThiF; |
7-154 | 6.04e-30 | ||||||
sulfur carrier protein ThiS adenylyltransferase ThiF; Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 113.41 E-value: 6.04e-30
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| YgdL_like | cd00755 | Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
14-129 | 1.60e-29 | ||||||
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, 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 the substrate. The exact function of this family is unknown. Pssm-ID: 238384 [Multi-domain] Cd Length: 231 Bit Score: 113.08 E-value: 1.60e-29
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| TcdA | COG1179 | tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
1-127 | 3.88e-29 | ||||||
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440792 Cd Length: 247 Bit Score: 112.10 E-value: 3.88e-29
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| E1_ThiF_like | cd01487 | E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ... |
26-203 | 3.53e-25 | ||||||
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, 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 the substrate. The exact function of this family is unknown. Pssm-ID: 238764 [Multi-domain] Cd Length: 174 Bit Score: 99.76 E-value: 3.53e-25
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| E1-1_like | cd01485 | Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ... |
5-161 | 3.12e-23 | ||||||
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: 95.18 E-value: 3.12e-23
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| Aos1_SUMO | cd01492 | Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ... |
5-154 | 1.89e-19 | ||||||
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: 84.65 E-value: 1.89e-19
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| E1-2_like | cd01484 | Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ... |
27-181 | 3.17e-19 | ||||||
Ubiquitin activating enzyme (E1), repeat 2-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. 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 second repeat of Ub-E1. Pssm-ID: 238761 [Multi-domain] Cd Length: 234 Bit Score: 85.32 E-value: 3.17e-19
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| Uba2_SUMO | cd01489 | Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
27-169 | 9.16e-18 | ||||||
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 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. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2. Pssm-ID: 238766 [Multi-domain] Cd Length: 312 Bit Score: 82.43 E-value: 9.16e-18
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| Apg7 | cd01486 | Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ... |
27-130 | 5.02e-17 | ||||||
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole. Pssm-ID: 238763 [Multi-domain] Cd Length: 307 Bit Score: 80.11 E-value: 5.02e-17
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| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
2-164 | 6.35e-17 | ||||||
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: 81.86 E-value: 6.35e-17
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| Uba3_RUB | cd01488 | Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ... |
26-175 | 1.23e-15 | ||||||
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 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. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2. Pssm-ID: 238765 [Multi-domain] Cd Length: 291 Bit Score: 75.86 E-value: 1.23e-15
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| APPBP1_RUB | cd01493 | Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ... |
4-159 | 2.14e-14 | ||||||
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: 73.49 E-value: 2.14e-14
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| Ube1_repeat2 | cd01490 | Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ... |
26-164 | 4.36e-14 | ||||||
Ubiquitin activating enzyme (E1), repeat 2. 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. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1. Pssm-ID: 238767 [Multi-domain] Cd Length: 435 Bit Score: 72.71 E-value: 4.36e-14
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| Ube1_repeat1 | cd01491 | Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ... |
5-154 | 1.01e-12 | ||||||
Ubiquitin activating enzyme (E1), repeat 1. 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. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1. Pssm-ID: 238768 [Multi-domain] Cd Length: 286 Bit Score: 67.68 E-value: 1.01e-12
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| PRK15116 | PRK15116 | sulfur acceptor protein CsdL; Provisional |
18-143 | 1.07e-11 | ||||||
sulfur acceptor protein CsdL; Provisional Pssm-ID: 185071 Cd Length: 268 Bit Score: 64.44 E-value: 1.07e-11
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| PRK08223 | PRK08223 | hypothetical protein; Validated |
14-151 | 2.84e-11 | ||||||
hypothetical protein; Validated Pssm-ID: 181302 [Multi-domain] Cd Length: 287 Bit Score: 63.16 E-value: 2.84e-11
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| PRK14851 | PRK14851 | hypothetical protein; Provisional |
10-151 | 3.65e-09 | ||||||
hypothetical protein; Provisional Pssm-ID: 184853 [Multi-domain] Cd Length: 679 Bit Score: 57.95 E-value: 3.65e-09
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| E1_like_apg7 | TIGR01381 | E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ... |
22-132 | 6.62e-09 | ||||||
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy. Pssm-ID: 273590 [Multi-domain] Cd Length: 664 Bit Score: 57.26 E-value: 6.62e-09
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| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
5-143 | 6.79e-08 | ||||||
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: 54.12 E-value: 6.79e-08
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| PRK14852 | PRK14852 | hypothetical protein; Provisional |
18-151 | 1.76e-07 | ||||||
hypothetical protein; Provisional Pssm-ID: 184854 [Multi-domain] Cd Length: 989 Bit Score: 52.78 E-value: 1.76e-07
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| PRK07877 | PRK07877 | Rv1355c family protein; |
14-143 | 2.34e-06 | ||||||
Rv1355c family protein; Pssm-ID: 236122 [Multi-domain] Cd Length: 722 Bit Score: 49.22 E-value: 2.34e-06
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| NAD_bind_Shikimate_DH | cd01065 | NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
16-124 | 2.33e-05 | ||||||
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 43.80 E-value: 2.33e-05
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| hemA | PRK00045 | glutamyl-tRNA reductase; Reviewed |
22-124 | 2.51e-05 | ||||||
glutamyl-tRNA reductase; Reviewed Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 45.56 E-value: 2.51e-05
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| AroE | COG0169 | Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
21-124 | 4.16e-05 | ||||||
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 44.36 E-value: 4.16e-05
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| Sacchrp_dh_NADP | pfam03435 | Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
27-130 | 7.01e-05 | ||||||
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase. Pssm-ID: 397480 [Multi-domain] Cd Length: 120 Bit Score: 41.81 E-value: 7.01e-05
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| AlaDh_PNT_C | smart01002 | Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
11-129 | 1.14e-04 | ||||||
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine. Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 41.72 E-value: 1.14e-04
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| HemA | COG0373 | Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
22-124 | 1.57e-04 | ||||||
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440142 [Multi-domain] Cd Length: 425 Bit Score: 43.18 E-value: 1.57e-04
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| NAD_bind_Glutamyl_tRNA_reduct | cd05213 | NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
22-124 | 1.65e-04 | ||||||
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 43.02 E-value: 1.65e-04
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| Shikimate_DH | pfam01488 | Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
20-124 | 2.36e-04 | ||||||
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate. Pssm-ID: 460229 [Multi-domain] Cd Length: 136 Bit Score: 40.63 E-value: 2.36e-04
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| TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
19-129 | 5.58e-04 | ||||||
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 41.21 E-value: 5.58e-04
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| Malic_M | smart00919 | Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ... |
21-57 | 3.32e-03 | ||||||
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate. Pssm-ID: 214912 Cd Length: 231 Bit Score: 38.55 E-value: 3.32e-03
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| FadB | COG1250 | 3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
25-123 | 6.12e-03 | ||||||
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 37.78 E-value: 6.12e-03
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| NAD_bind_amino_acid_DH | cd05191 | NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH) ... |
21-59 | 8.32e-03 | ||||||
NAD(P) binding domain of amino acid dehydrogenase-like proteins; Amino acid dehydrogenase(DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and are found in glutamate, leucine, and phenylalanine DHs (DHs), methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133449 [Multi-domain] Cd Length: 86 Bit Score: 35.05 E-value: 8.32e-03
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| ADP_GME_SDR_e | cd05248 | ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ... |
31-156 | 9.64e-03 | ||||||
ADP-L-glycero-D-mannoheptose 6-epimerase (GME), extended (e) SDRs; This subgroup contains ADP-L-glycero-D-mannoheptose 6-epimerase, an extended SDR, which catalyzes the NAD-dependent interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. This subgroup has the canonical active site tetrad and NAD(P)-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Pssm-ID: 187559 [Multi-domain] Cd Length: 317 Bit Score: 37.28 E-value: 9.64e-03
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| NAD_bind_2_malic_enz | cd05311 | NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the ... |
21-109 | 9.90e-03 | ||||||
NAD(P) binding domain of malic enzyme (ME), subgroup 2; Malic enzyme (ME), a member of the amino acid dehydrogenase (DH)-like domain family, catalyzes the oxidative decarboxylation of L-malate to pyruvate in the presence of cations (typically Mg++ or Mn++) with the concomitant reduction of cofactor NAD+ or NADP+. ME has been found in all organisms, and plays important roles in diverse metabolic pathways such as photosynthesis and lipogenesis. This enzyme generally forms homotetramers. The conversion of malate to pyruvate by ME typically involves oxidation of malate to produce oxaloacetate, followed by decarboxylation of oxaloacetate to produce pyruvate and CO2. This subfamily consists primarily of archaeal and bacterial ME. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133453 [Multi-domain] Cd Length: 226 Bit Score: 36.86 E-value: 9.90e-03
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