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thiamine biosynthesis/tRNA modification protein ThiI [Klebsiella variicola At-22]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||||
ThiI | COG0301 | Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
3-379 | 0e+00 | ||||||
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis : Pssm-ID: 440070 [Multi-domain] Cd Length: 382 Bit Score: 520.80 E-value: 0e+00
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ThiI_C_thiazole | TIGR04271 | thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ... |
382-482 | 7.51e-59 | ||||||
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein. : Pssm-ID: 275094 [Multi-domain] Cd Length: 101 Bit Score: 188.92 E-value: 7.51e-59
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Name | Accession | Description | Interval | E-value | ||||||
ThiI | COG0301 | Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
3-379 | 0e+00 | ||||||
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis Pssm-ID: 440070 [Multi-domain] Cd Length: 382 Bit Score: 520.80 E-value: 0e+00
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TIGR00342 | TIGR00342 | tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ... |
4-376 | 1.01e-169 | ||||||
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase involved in 4-thiouridine modification of tRNA. This protein often is bifunctional, with genetically separable activities, where the C-terminal rhodanese-like domain (residues 385 to 482 in E. coli ThiI), a domain not included in this model, is sufficient to synthesize the thiazole moiety of thiamine (see TIGR04271). Note that ThiI, because of its role in tRNA modification, may occur in species (such as Mycoplasma genitalium) that lack de novo thiamine biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine, Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 273025 [Multi-domain] Cd Length: 371 Bit Score: 482.68 E-value: 1.01e-169
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ThiI | pfam02568 | Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ... |
175-369 | 2.08e-101 | ||||||
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis. Pssm-ID: 280691 [Multi-domain] Cd Length: 197 Bit Score: 302.04 E-value: 2.08e-101
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PPase_ThiI | cd01712 | pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ... |
174-355 | 4.55e-86 | ||||||
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide. Pssm-ID: 467485 [Multi-domain] Cd Length: 185 Bit Score: 262.10 E-value: 4.55e-86
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ThiI_C_thiazole | TIGR04271 | thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ... |
382-482 | 7.51e-59 | ||||||
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein. Pssm-ID: 275094 [Multi-domain] Cd Length: 101 Bit Score: 188.92 E-value: 7.51e-59
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PRK08349 | PRK08349 | hypothetical protein; Validated |
180-355 | 3.28e-27 | ||||||
hypothetical protein; Validated Pssm-ID: 169396 Cd Length: 198 Bit Score: 108.29 E-value: 3.28e-27
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THUMP | smart00981 | The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
86-161 | 7.89e-19 | ||||||
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 214952 [Multi-domain] Cd Length: 83 Bit Score: 80.78 E-value: 7.89e-19
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PspE | COG0607 | Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
410-481 | 4.41e-08 | ||||||
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle Pssm-ID: 440372 [Multi-domain] Cd Length: 106 Bit Score: 51.12 E-value: 4.41e-08
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Name | Accession | Description | Interval | E-value | ||||||
ThiI | COG0301 | Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
3-379 | 0e+00 | ||||||
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis Pssm-ID: 440070 [Multi-domain] Cd Length: 382 Bit Score: 520.80 E-value: 0e+00
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TIGR00342 | TIGR00342 | tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ... |
4-376 | 1.01e-169 | ||||||
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase involved in 4-thiouridine modification of tRNA. This protein often is bifunctional, with genetically separable activities, where the C-terminal rhodanese-like domain (residues 385 to 482 in E. coli ThiI), a domain not included in this model, is sufficient to synthesize the thiazole moiety of thiamine (see TIGR04271). Note that ThiI, because of its role in tRNA modification, may occur in species (such as Mycoplasma genitalium) that lack de novo thiamine biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine, Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 273025 [Multi-domain] Cd Length: 371 Bit Score: 482.68 E-value: 1.01e-169
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ThiI | pfam02568 | Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ... |
175-369 | 2.08e-101 | ||||||
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis. Pssm-ID: 280691 [Multi-domain] Cd Length: 197 Bit Score: 302.04 E-value: 2.08e-101
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PPase_ThiI | cd01712 | pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ... |
174-355 | 4.55e-86 | ||||||
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide. Pssm-ID: 467485 [Multi-domain] Cd Length: 185 Bit Score: 262.10 E-value: 4.55e-86
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ThiI_C_thiazole | TIGR04271 | thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ... |
382-482 | 7.51e-59 | ||||||
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein. Pssm-ID: 275094 [Multi-domain] Cd Length: 101 Bit Score: 188.92 E-value: 7.51e-59
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THUMP_ThiI | cd11716 | THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ... |
2-170 | 3.25e-50 | ||||||
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 212585 Cd Length: 166 Bit Score: 168.78 E-value: 3.25e-50
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PRK08349 | PRK08349 | hypothetical protein; Validated |
180-355 | 3.28e-27 | ||||||
hypothetical protein; Validated Pssm-ID: 169396 Cd Length: 198 Bit Score: 108.29 E-value: 3.28e-27
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THUMP | smart00981 | The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ... |
86-161 | 7.89e-19 | ||||||
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 214952 [Multi-domain] Cd Length: 83 Bit Score: 80.78 E-value: 7.89e-19
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THUMP | pfam02926 | THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ... |
28-161 | 1.42e-18 | ||||||
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 460749 Cd Length: 143 Bit Score: 82.10 E-value: 1.42e-18
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Tan1 | COG1818 | tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ... |
63-154 | 4.03e-13 | ||||||
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure and biogenesis]; tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 441423 Cd Length: 162 Bit Score: 67.22 E-value: 4.03e-13
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THUMP_SPOUT | cd11718 | THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ... |
69-161 | 4.33e-10 | ||||||
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are characterized by containing an N-terminal THUMP domain and a C-terminal SPOUT RNA methyltransferase domain. No functional information is available The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 212587 Cd Length: 145 Bit Score: 58.06 E-value: 4.33e-10
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THUMP_AdoMetMT | cd11715 | THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ... |
73-161 | 9.42e-09 | ||||||
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 212584 Cd Length: 152 Bit Score: 54.12 E-value: 9.42e-09
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PspE | COG0607 | Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
410-481 | 4.41e-08 | ||||||
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle Pssm-ID: 440372 [Multi-domain] Cd Length: 106 Bit Score: 51.12 E-value: 4.41e-08
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THUMP_THUMPD1_like | cd11717 | THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins ... |
73-154 | 1.26e-05 | ||||||
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins including THUMP domain-containing protein 1 and Saccharomyces cerevisiae Tan1. Tan1 is non essential and has been shown to be required for the formation of the modified nucleoside N(4)-acetylcytidine (ac(4)C) in tRNA. To date, there is no functional information available about THUMPD1. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 212586 Cd Length: 158 Bit Score: 45.27 E-value: 1.26e-05
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QueC-like | cd01995 | 7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
178-346 | 5.14e-04 | ||||||
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Pssm-ID: 467499 [Multi-domain] Cd Length: 208 Bit Score: 41.45 E-value: 5.14e-04
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THUMP | cd11688 | THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ... |
103-158 | 2.16e-03 | ||||||
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets. Pssm-ID: 212583 Cd Length: 148 Bit Score: 38.62 E-value: 2.16e-03
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Blast search parameters | ||||
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