uncharacterized protein MYCTH_2311735 [Thermothelomyces thermophilus ATCC 42464]
Protein Classification
Uba2_SUMO and UAE_UbL domain-containing protein( domain architecture ID 10845017)
protein containing domains Uba2_SUMO, UBA_e1_thiolCys, and UAE_UbL
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| Uba2_SUMO | cd01489 | Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
16-433 | 0e+00 | |||||||
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: 572.79 E-value: 0e+00
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| UAE_UbL | pfam14732 | Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ... |
441-522 | 7.54e-25 | |||||||
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein. : Pssm-ID: 464286 Cd Length: 88 Bit Score: 98.42 E-value: 7.54e-25
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| UBA_E1_SCCH super family | cl10464 | Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ... |
176-375 | 1.35e-05 | |||||||
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine. The actual alignment was detected with superfamily member pfam10585: Pssm-ID: 463157 Cd Length: 254 Bit Score: 46.84 E-value: 1.35e-05
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| Name | Accession | Description | Interval | E-value | |||||||||
| Uba2_SUMO | cd01489 | Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
16-433 | 0e+00 | |||||||||
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: 572.79 E-value: 0e+00
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| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
13-175 | 1.86e-64 | |||||||||
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: 212.12 E-value: 1.86e-64
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| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
16-493 | 3.38e-60 | |||||||||
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: 217.06 E-value: 3.38e-60
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| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
13-170 | 5.08e-48 | |||||||||
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: 168.38 E-value: 5.08e-48
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| PRK05690 | PRK05690 | molybdopterin biosynthesis protein MoeB; Provisional |
13-158 | 6.82e-28 | |||||||||
molybdopterin biosynthesis protein MoeB; Provisional Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 112.63 E-value: 6.82e-28
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| UAE_UbL | pfam14732 | Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ... |
441-522 | 7.54e-25 | |||||||||
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein. Pssm-ID: 464286 Cd Length: 88 Bit Score: 98.42 E-value: 7.54e-25
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| UBA_E1_SCCH | pfam10585 | Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ... |
176-375 | 1.35e-05 | |||||||||
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine. Pssm-ID: 463157 Cd Length: 254 Bit Score: 46.84 E-value: 1.35e-05
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| Name | Accession | Description | Interval | E-value | |||||||||
| Uba2_SUMO | cd01489 | Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
16-433 | 0e+00 | |||||||||
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: 572.79 E-value: 0e+00
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| E1-2_like | cd01484 | Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ... |
16-394 | 4.84e-87 | |||||||||
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: 270.99 E-value: 4.84e-87
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| Ube1_repeat2 | cd01490 | Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ... |
16-400 | 4.92e-72 | |||||||||
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: 238.73 E-value: 4.92e-72
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| Uba3_RUB | cd01488 | Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ... |
16-434 | 3.57e-69 | |||||||||
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: 226.47 E-value: 3.57e-69
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| ThiF | pfam00899 | ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
13-175 | 1.86e-64 | |||||||||
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: 212.12 E-value: 1.86e-64
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| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
16-493 | 3.38e-60 | |||||||||
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: 217.06 E-value: 3.38e-60
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| ThiF | COG0476 | Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
13-170 | 5.08e-48 | |||||||||
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: 168.38 E-value: 5.08e-48
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| ThiF_MoeB_HesA_family | cd00757 | ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
13-170 | 8.53e-45 | |||||||||
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: 159.18 E-value: 8.53e-45
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| E1_enzyme_family | cd01483 | Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
16-148 | 6.21e-39 | |||||||||
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: 140.10 E-value: 6.21e-39
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| PRK05690 | PRK05690 | molybdopterin biosynthesis protein MoeB; Provisional |
13-158 | 6.82e-28 | |||||||||
molybdopterin biosynthesis protein MoeB; Provisional Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 112.63 E-value: 6.82e-28
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| UAE_UbL | pfam14732 | Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ... |
441-522 | 7.54e-25 | |||||||||
Ubiquitin/SUMO-activating enzyme ubiquitin-like domain; This is the C-terminal domain of ubiquitin-activating enzyme and SUMO-activating enzyme 2. It is structurally similar to ubiquitin. This domain is involved in E1-SUMO-thioester transfer to the SUMO E2 conjugating protein. Pssm-ID: 464286 Cd Length: 88 Bit Score: 98.42 E-value: 7.54e-25
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| PRK08762 | PRK08762 | molybdopterin-synthase adenylyltransferase MoeB; |
14-171 | 5.32e-22 | |||||||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 98.16 E-value: 5.32e-22
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| Aos1_SUMO | cd01492 | Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ... |
13-145 | 3.78e-20 | |||||||||
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: 88.89 E-value: 3.78e-20
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| PRK07878 | PRK07878 | molybdopterin biosynthesis-like protein MoeZ; Validated |
13-164 | 2.62e-19 | |||||||||
molybdopterin biosynthesis-like protein MoeZ; Validated Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 90.54 E-value: 2.62e-19
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| PRK05600 | PRK05600 | thiamine biosynthesis protein ThiF; Validated |
5-151 | 1.50e-18 | |||||||||
thiamine biosynthesis protein ThiF; Validated Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 87.63 E-value: 1.50e-18
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| YgdL_like | cd00755 | Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
13-140 | 3.46e-18 | |||||||||
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: 83.81 E-value: 3.46e-18
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| E1-1_like | cd01485 | Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ... |
13-145 | 1.28e-16 | |||||||||
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: 78.62 E-value: 1.28e-16
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| E1_ThiF_like | cd01487 | E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ... |
16-141 | 1.72e-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: 77.42 E-value: 1.72e-16
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| PRK08644 | PRK08644 | sulfur carrier protein ThiS adenylyltransferase ThiF; |
3-141 | 5.12e-16 | |||||||||
sulfur carrier protein ThiS adenylyltransferase ThiF; Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 77.20 E-value: 5.12e-16
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| Ube1_repeat1 | cd01491 | Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ... |
14-145 | 5.95e-16 | |||||||||
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: 78.46 E-value: 5.95e-16
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| PRK12475 | PRK12475 | thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
11-170 | 1.08e-15 | |||||||||
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 78.62 E-value: 1.08e-15
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| PRK08328 | PRK08328 | hypothetical protein; Provisional |
13-153 | 1.57e-15 | |||||||||
hypothetical protein; Provisional Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 76.37 E-value: 1.57e-15
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| PRK07688 | PRK07688 | thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
13-170 | 1.85e-14 | |||||||||
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 75.03 E-value: 1.85e-14
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| TcdA | COG1179 | tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
13-140 | 1.82e-13 | |||||||||
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: 70.50 E-value: 1.82e-13
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| PRK05597 | PRK05597 | molybdopterin biosynthesis protein MoeB; Validated |
8-171 | 2.81e-13 | |||||||||
molybdopterin biosynthesis protein MoeB; Validated Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 71.44 E-value: 2.81e-13
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| PRK07411 | PRK07411 | molybdopterin-synthase adenylyltransferase MoeB; |
13-164 | 1.51e-12 | |||||||||
molybdopterin-synthase adenylyltransferase MoeB; Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 69.76 E-value: 1.51e-12
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| APPBP1_RUB | cd01493 | Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ... |
15-150 | 4.29e-11 | |||||||||
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: 65.40 E-value: 4.29e-11
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| PRK14851 | PRK14851 | hypothetical protein; Provisional |
14-147 | 3.79e-10 | |||||||||
hypothetical protein; Provisional Pssm-ID: 184853 [Multi-domain] Cd Length: 679 Bit Score: 62.96 E-value: 3.79e-10
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| PRK15116 | PRK15116 | sulfur acceptor protein CsdL; Provisional |
14-145 | 2.64e-08 | |||||||||
sulfur acceptor protein CsdL; Provisional Pssm-ID: 185071 Cd Length: 268 Bit Score: 55.58 E-value: 2.64e-08
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| PRK08223 | PRK08223 | hypothetical protein; Validated |
13-147 | 3.61e-08 | |||||||||
hypothetical protein; Validated Pssm-ID: 181302 [Multi-domain] Cd Length: 287 Bit Score: 55.07 E-value: 3.61e-08
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| E1_like_apg7 | TIGR01381 | E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ... |
5-209 | 9.19e-07 | |||||||||
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: 51.86 E-value: 9.19e-07
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| PRK14852 | PRK14852 | hypothetical protein; Provisional |
14-151 | 2.27e-06 | |||||||||
hypothetical protein; Provisional Pssm-ID: 184854 [Multi-domain] Cd Length: 989 Bit Score: 50.85 E-value: 2.27e-06
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| Ube1 | TIGR01408 | ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
9-126 | 2.42e-06 | |||||||||
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: 50.66 E-value: 2.42e-06
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| Apg7 | cd01486 | Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ... |
16-209 | 3.66e-06 | |||||||||
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: 49.29 E-value: 3.66e-06
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| UBA_E1_SCCH | pfam10585 | Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ... |
176-375 | 1.35e-05 | |||||||||
Ubiquitin-activating enzyme, SCCH domain; Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2). This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP. The catalytic cysteine domain contains the E1 active site cysteine, and is divided in two half-domains, FCCH and SCCH, for 'first' and 'second' catalytic cysteine half-domain, respectively. This is the SCCH domain in which resides the catalytic cysteine. Pssm-ID: 463157 Cd Length: 254 Bit Score: 46.84 E-value: 1.35e-05
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| UDP_invert_4-6DH_SDR_e | cd05237 | UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ... |
13-122 | 1.43e-03 | |||||||||
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. 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: 187548 [Multi-domain] Cd Length: 287 Bit Score: 41.06 E-value: 1.43e-03
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