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Items: 1 to 20 of 21

1.

aminomethyltransferase beta-barrel domain-containing protein

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 [1]. [1]. 3298234. Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities. Hagervall TG, Edmonds CG, McCloskey JA, Bjork GR;. J Biol Chem 1987;262:8488-8495. (from Pfam)

Date:
2024-10-16
Family Accession:
NF042466.3
Method:
HMM
2.

tRNA methyl transferase PRC-barrel domain-containing protein

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 [1]. [1]. 3298234. Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities. Hagervall TG, Edmonds CG, McCloskey JA, Bjork GR;. J Biol Chem 1987;262:8488-8495. (from Pfam)

Date:
2024-10-16
Family Accession:
NF042467.3
Method:
HMM
3.

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 [1]. [1]. 3298234. Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities. Hagervall TG, Edmonds CG, McCloskey JA, Bjork GR;. J Biol Chem 1987;262:8488-8495. Paper describing PDB structure 1gpm. [2]. 8548458. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL;. Nat Struct Biol 1996;3:74-86. Paper describing PDB structure 2der. [3]. 16871210. Snapshots of tRNA sulphuration via an adenylated intermediate. Numata T, Ikeuchi Y, Fukai S, Suzuki T, Nureki O;. Nature. 2006;442:419-424. Paper describing PDB structure 2vxo. [4]. 23816837. Substrate specificity and oligomerization of human GMP synthetase. Welin M, Lehtio L, Johansson A, Flodin S, Nyman T, Tresaugues L, Hammarstrom M, Graslund S, Nordlund P;. J Mol Biol. 2013;425:4323-4333. Paper describing PDB structure 3vrh. [5]. 23444054. Crystallographic and mutational studies on the tRNA thiouridine synthetase TtuA. Nakagawa H, Kuratani M, Goto-Ito S, Ito T, Katsura K, Terada T, Shirouzu M, Sekine S, Shigi N, Yokoyama S;. Proteins. 2013;81:1232-1244. Paper describing PDB structure 5mko. [6]. 28655838. Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S] cluster. Arragain S, Bimai O, Legrand P, Caillat S, Ravanat JL, T. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-10-16
Family Accession:
NF015042.5
Method:
HMM
4.

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. [1]. 8895556. Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. Rizzi M, Nessi C, Mattevi A, Coda A, Bolognesi M, Galizzi A;. EMBO J 1996;15:5125-5134. (from Pfam)

Date:
2024-10-16
Family Accession:
NF014586.5
Method:
HMM
5.

Thiamine biosynthesis protein (ThiI)

ThiI is required for thiazole synthesis, required for thiamine biosynthesis [1]. [1]. 9209060. Characterization of thiI, a new gene involved in thiazole biosynthesis in Salmonella typhimurium. Webb E, Claas K, Downs DM;. J Bacteriol 1997;179:4399-4402. (from Pfam)

GO Terms:
Molecular Function:
CCA tRNA nucleotidyltransferase activity (GO:0004810)
Date:
2024-10-16
Family Accession:
NF014610.5
Method:
HMM
6.

asparagine synthase-related protein

Most members of this family are asparagine synthase, which catalyzes conversion of aspartate to asparagine. Exceptions that score well against the HMM include isopeptide bond formation proteins for lasso peptide biosynthesis. But note that many additional proteins, such as the 7-cyano-7-deazaguanine synthase QueC, hit with scores barely above the model's cutoff scores to N-terminal regions about 60 amino acids long, whereas the full length of the model is 355.

GO Terms:
Molecular Function:
asparagine synthase (glutamine-hydrolyzing) activity (GO:0004066)
Biological Process:
asparagine biosynthetic process (GO:0006529)
Date:
2024-08-14
Family Accession:
NF012936.5
Method:
HMM
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.
new record, indexing in progress
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17.
new record, indexing in progress
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18.
new record, indexing in progress
Family Accession:
19.

tRNA 2-thiouridine(34) synthase MnmA

Catalyzes a sulfuration reaction to synthesize 2-thiouridine at the U34 position of tRNAs

Gene:
mnmA
GO Terms:
Biological Process:
tRNA processing (GO:0008033)
Molecular Function:
transferase activity (GO:0016740)
Molecular Function:
sulfurtransferase activity (GO:0016783)
Date:
2021-07-21
Family Accession:
NF001138.1
Method:
HMM
20.

MnmA/TRMU family protein

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)

Date:
2024-08-11
Family Accession:
11422314
Method:
Sparcle
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