tRNA 2-thiouridine(34) synthase MnmA [Shewanella piezotolerans]
Protein Classification
MnmA/TRMU family protein( domain architecture ID 11422314)
MnmA/TRMU family protein similar to tRNA-specific 2-thiouridylase MnmA that catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln)
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| MnmA | COG0482 | tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
11-366 | 0e+00 | ||||||
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification : Pssm-ID: 440250 [Multi-domain] Cd Length: 353 Bit Score: 640.95 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| MnmA | COG0482 | tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
11-366 | 0e+00 | ||||||
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440250 [Multi-domain] Cd Length: 353 Bit Score: 640.95 E-value: 0e+00
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| mnmA | PRK00143 | tRNA-specific 2-thiouridylase MnmA; Reviewed |
11-366 | 0e+00 | ||||||
tRNA-specific 2-thiouridylase MnmA; Reviewed Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 636.34 E-value: 0e+00
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| MnmA_TRMU-like | cd01998 | MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
12-365 | 0e+00 | ||||||
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family 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: 467502 [Multi-domain] Cd Length: 349 Bit Score: 567.52 E-value: 0e+00
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| trmU | TIGR00420 | tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
11-365 | 0e+00 | ||||||
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 273069 [Multi-domain] Cd Length: 352 Bit Score: 536.20 E-value: 0e+00
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| tRNA_Me_trans | pfam03054 | tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
11-208 | 2.50e-118 | ||||||
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs. Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 341.15 E-value: 2.50e-118
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| Name | Accession | Description | Interval | E-value | ||||||
| MnmA | COG0482 | tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
11-366 | 0e+00 | ||||||
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440250 [Multi-domain] Cd Length: 353 Bit Score: 640.95 E-value: 0e+00
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| mnmA | PRK00143 | tRNA-specific 2-thiouridylase MnmA; Reviewed |
11-366 | 0e+00 | ||||||
tRNA-specific 2-thiouridylase MnmA; Reviewed Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 636.34 E-value: 0e+00
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| MnmA_TRMU-like | cd01998 | MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
12-365 | 0e+00 | ||||||
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family 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: 467502 [Multi-domain] Cd Length: 349 Bit Score: 567.52 E-value: 0e+00
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| trmU | TIGR00420 | tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ... |
11-365 | 0e+00 | ||||||
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 273069 [Multi-domain] Cd Length: 352 Bit Score: 536.20 E-value: 0e+00
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| tRNA_Me_trans | pfam03054 | tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
11-208 | 2.50e-118 | ||||||
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs. Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 341.15 E-value: 2.50e-118
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| PRK14664 | PRK14664 | tRNA-specific 2-thiouridylase MnmA; Provisional |
11-365 | 9.37e-82 | ||||||
tRNA-specific 2-thiouridylase MnmA; Provisional Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 253.72 E-value: 9.37e-82
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| mnmA | PRK14665 | tRNA-specific 2-thiouridylase MnmA; Provisional |
11-365 | 9.61e-74 | ||||||
tRNA-specific 2-thiouridylase MnmA; Provisional Pssm-ID: 173128 [Multi-domain] Cd Length: 360 Bit Score: 233.29 E-value: 9.61e-74
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| tRNA_Me_trans_C | pfam20258 | Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ... |
289-365 | 2.29e-25 | ||||||
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs. Pssm-ID: 466409 [Multi-domain] Cd Length: 77 Bit Score: 97.73 E-value: 2.29e-25
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| tRNA_Me_trans_M | pfam20259 | tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ... |
213-280 | 6.89e-20 | ||||||
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs. Pssm-ID: 466410 [Multi-domain] Cd Length: 66 Bit Score: 82.27 E-value: 6.89e-20
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| NAD_synthase | pfam02540 | NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
11-191 | 1.51e-10 | ||||||
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation. Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 60.86 E-value: 1.51e-10
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| TilS | COG0037 | tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
10-133 | 5.27e-09 | ||||||
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 55.99 E-value: 5.27e-09
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| LarE-like | cd01990 | Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
12-201 | 5.87e-09 | ||||||
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus. Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 5.87e-09
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| NAD_synthase | cd00553 | NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
11-91 | 5.76e-08 | ||||||
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source. Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 53.33 E-value: 5.76e-08
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| nadE | TIGR00552 | NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
11-191 | 8.14e-08 | ||||||
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides] Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 52.78 E-value: 8.14e-08
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| NadE | COG0171 | NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
11-78 | 1.87e-07 | ||||||
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 52.93 E-value: 1.87e-07
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| PRK13980 | PRK13980 | NAD synthetase; Provisional |
11-191 | 4.57e-07 | ||||||
NAD synthetase; Provisional Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 50.59 E-value: 4.57e-07
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| QueC-like | cd01995 | 7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
11-79 | 4.82e-07 | ||||||
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: 49.92 E-value: 4.82e-07
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| TtuA-like | cd01993 | tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ... |
10-83 | 5.84e-07 | ||||||
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus. Pssm-ID: 467497 [Multi-domain] Cd Length: 190 Bit Score: 49.25 E-value: 5.84e-07
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| AANH-like | cd01986 | adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
13-63 | 3.23e-06 | ||||||
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide. Pssm-ID: 467490 [Multi-domain] Cd Length: 74 Bit Score: 44.37 E-value: 3.23e-06
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| PPase_ThiI | cd01712 | pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ... |
12-44 | 3.77e-06 | ||||||
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: 46.78 E-value: 3.77e-06
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| ThiI | COG0301 | Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ... |
12-79 | 1.45e-05 | ||||||
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: 46.62 E-value: 1.45e-05
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| lysidine_TilS_N | TIGR02432 | tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ... |
12-133 | 1.56e-05 | ||||||
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification] Pssm-ID: 274129 [Multi-domain] Cd Length: 189 Bit Score: 45.32 E-value: 1.56e-05
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| QueC | pfam06508 | Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
12-78 | 8.42e-05 | ||||||
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0. Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 43.37 E-value: 8.42e-05
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| PRK13981 | PRK13981 | NAD synthetase; Provisional |
11-105 | 1.10e-04 | ||||||
NAD synthetase; Provisional Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 43.99 E-value: 1.10e-04
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| ThiI | pfam02568 | Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ... |
12-44 | 1.13e-04 | ||||||
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis. Pssm-ID: 280691 [Multi-domain] Cd Length: 197 Bit Score: 42.80 E-value: 1.13e-04
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| guaA | PRK00074 | GMP synthase; Reviewed |
11-82 | 2.58e-04 | ||||||
GMP synthase; Reviewed Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 42.73 E-value: 2.58e-04
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| QueC | COG0603 | 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
11-77 | 4.07e-04 | ||||||
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 41.30 E-value: 4.07e-04
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| GMP_synthase_C | cd01997 | C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
10-32 | 5.58e-04 | ||||||
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus. Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 41.37 E-value: 5.58e-04
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| PRK04527 | PRK04527 | argininosuccinate synthase; Provisional |
11-132 | 8.57e-04 | ||||||
argininosuccinate synthase; Provisional Pssm-ID: 235305 Cd Length: 400 Bit Score: 40.97 E-value: 8.57e-04
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| nadE | PRK00876 | NAD(+) synthase; |
13-72 | 1.61e-03 | ||||||
NAD(+) synthase; Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 39.94 E-value: 1.61e-03
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| TilS_N | cd01992 | N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ... |
12-192 | 3.52e-03 | ||||||
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus. Pssm-ID: 467496 [Multi-domain] Cd Length: 185 Bit Score: 37.96 E-value: 3.52e-03
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| ATP_bind_3 | pfam01171 | PP-loop family; This family of proteins belongs to the PP-loop superfamily. |
15-192 | 4.26e-03 | ||||||
PP-loop family; This family of proteins belongs to the PP-loop superfamily. Pssm-ID: 426097 [Multi-domain] Cd Length: 178 Bit Score: 37.61 E-value: 4.26e-03
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| Asn_synthase_B_C | cd01991 | C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
18-82 | 8.07e-03 | ||||||
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase. Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 37.25 E-value: 8.07e-03
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