Moeb/ThiF domain-containing protein [Schizosaccharomyces pombe]
Protein Classification
tRNA threonylcarbamoyladenosine dehydratase( domain architecture ID 10091512)
tRNA threonylcarbamoyladenosine dehydratase catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine to form cyclic t(6)A in tRNA
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| YgdL_like | cd00755 | Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
99-335 | 7.20e-99 | ||||
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: 296.05 E-value: 7.20e-99
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| Name | Accession | Description | Interval | E-value | |||||
| YgdL_like | cd00755 | Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
99-335 | 7.20e-99 | |||||
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: 296.05 E-value: 7.20e-99
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| TcdA | COG1179 | tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
99-340 | 1.78e-55 | |||||
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: 184.90 E-value: 1.78e-55
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| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
92-368 | 2.67e-47 | |||||
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: 163.20 E-value: 2.67e-47
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| PRK15116 | PRK15116 | sulfur acceptor protein CsdL; Provisional |
120-280 | 3.80e-28 | |||||
sulfur acceptor protein CsdL; Provisional Pssm-ID: 185071 Cd Length: 268 Bit Score: 112.59 E-value: 3.80e-28
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| thiF_fam2 | TIGR02354 | thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ... |
128-249 | 1.74e-14 | |||||
thiamine biosynthesis protein ThiF, family 2; 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 one the E. 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 divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine] Pssm-ID: 162819 Cd Length: 200 Bit Score: 71.82 E-value: 1.74e-14
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| Name | Accession | Description | Interval | E-value | |||||
| YgdL_like | cd00755 | Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
99-335 | 7.20e-99 | |||||
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: 296.05 E-value: 7.20e-99
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| TcdA | COG1179 | tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
99-340 | 1.78e-55 | |||||
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: 184.90 E-value: 1.78e-55
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| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
92-368 | 2.67e-47 | |||||
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: 163.20 E-value: 2.67e-47
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| E1_enzyme_family | cd01483 | Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
120-251 | 1.54e-33 | |||||
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: 123.53 E-value: 1.54e-33
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| PRK15116 | PRK15116 | sulfur acceptor protein CsdL; Provisional |
120-280 | 3.80e-28 | |||||
sulfur acceptor protein CsdL; Provisional Pssm-ID: 185071 Cd Length: 268 Bit Score: 112.59 E-value: 3.80e-28
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| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
84-229 | 1.25e-27 | |||||
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: 110.22 E-value: 1.25e-27
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| ThiF_MoeB_HesA_family | cd00757 | ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
99-229 | 5.24e-22 | |||||
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: 94.08 E-value: 5.24e-22
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| PRK08644 | PRK08644 | sulfur carrier protein ThiS adenylyltransferase ThiF; |
127-231 | 4.57e-21 | |||||
sulfur carrier protein ThiS adenylyltransferase ThiF; Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 91.07 E-value: 4.57e-21
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| PRK05690 | PRK05690 | molybdopterin biosynthesis protein MoeB; Provisional |
128-235 | 5.17e-17 | |||||
molybdopterin biosynthesis protein MoeB; Provisional Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 80.27 E-value: 5.17e-17
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| E1_ThiF_like | cd01487 | E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ... |
118-249 | 2.00e-16 | |||||
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: 77.04 E-value: 2.00e-16
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| thiF_fam2 | TIGR02354 | thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ... |
128-249 | 1.74e-14 | |||||
thiamine biosynthesis protein ThiF, family 2; 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 one the E. 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 divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine] Pssm-ID: 162819 Cd Length: 200 Bit Score: 71.82 E-value: 1.74e-14
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| PRK07688 | PRK07688 | thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
89-229 | 6.85e-13 | |||||
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 69.64 E-value: 6.85e-13
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| PRK08762 | PRK08762 | molybdopterin-synthase adenylyltransferase MoeB; |
128-229 | 8.15e-12 | |||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 66.57 E-value: 8.15e-12
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| PRK05600 | PRK05600 | thiamine biosynthesis protein ThiF; Validated |
81-214 | 3.00e-11 | |||||
thiamine biosynthesis protein ThiF; Validated Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 64.90 E-value: 3.00e-11
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| PRK05597 | PRK05597 | molybdopterin biosynthesis protein MoeB; Validated |
99-214 | 5.06e-11 | |||||
molybdopterin biosynthesis protein MoeB; Validated Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 64.12 E-value: 5.06e-11
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| PRK08328 | PRK08328 | hypothetical protein; Provisional |
90-229 | 2.63e-10 | |||||
hypothetical protein; Provisional Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 60.19 E-value: 2.63e-10
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| PRK07878 | PRK07878 | molybdopterin biosynthesis-like protein MoeZ; Validated |
82-214 | 1.80e-09 | |||||
molybdopterin biosynthesis-like protein MoeZ; Validated Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 59.34 E-value: 1.80e-09
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| PRK07411 | PRK07411 | molybdopterin-synthase adenylyltransferase MoeB; |
128-214 | 5.39e-08 | |||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 54.74 E-value: 5.39e-08
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| PRK12475 | PRK12475 | thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
90-214 | 3.57e-07 | |||||
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 52.04 E-value: 3.57e-07
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| PRK07877 | PRK07877 | Rv1355c family protein; |
137-232 | 2.73e-06 | |||||
Rv1355c family protein; Pssm-ID: 236122 [Multi-domain] Cd Length: 722 Bit Score: 49.99 E-value: 2.73e-06
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| Uba2_SUMO | cd01489 | Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
118-231 | 1.53e-05 | |||||
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: 46.60 E-value: 1.53e-05
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| PRK14851 | PRK14851 | hypothetical protein; Provisional |
63-215 | 1.97e-05 | |||||
hypothetical protein; Provisional Pssm-ID: 184853 [Multi-domain] Cd Length: 679 Bit Score: 47.16 E-value: 1.97e-05
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| Ube1_repeat2 | cd01490 | Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ... |
135-225 | 2.57e-05 | |||||
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: 46.51 E-value: 2.57e-05
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| PRK08223 | PRK08223 | hypothetical protein; Validated |
87-209 | 7.68e-05 | |||||
hypothetical protein; Validated Pssm-ID: 181302 [Multi-domain] Cd Length: 287 Bit Score: 44.29 E-value: 7.68e-05
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| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
135-255 | 2.56e-04 | |||||
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: 43.72 E-value: 2.56e-04
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| Apg7 | cd01486 | Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ... |
129-183 | 2.70e-03 | |||||
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: 39.66 E-value: 2.70e-03
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| E1-2_like | cd01484 | Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ... |
118-231 | 9.45e-03 | |||||
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: 37.56 E-value: 9.45e-03
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