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Links from Protein

Items: 13

1.

methyltransferase domain-containing protein

This family appears to be a methyltransferase domain. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025033.5
Method:
HMM
2.

Eco57I restriction-modification methylase domain-containing protein

Homologues of the Escherichia coli Eco57I restriction-modification methylase are found in several phylogenetically diverse bacteria. The structure of TaqI has been solved [1]. [1]. 1334261. Cloning and sequence analysis of the genes coding for Eco57I. type IV restriction-modification enzymes.. Janulaitis A, Vaisvila R, Timinskas A, Klimasauskas S, Butkus V;. Nucleic Acids Res 1992;20:6051-6056.. [2]. 8995524. Differential binding of S-adenosylmethionine. S-adenosylhomocysteine and Sinefungin to the adenine-specific. DNA methyltransferase M.TaqI.. Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W;. J Mol Biol. 1997;265:56-67. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
catalytic activity (GO:0003824)
Biological Process:
DNA modification (GO:0006304)
Date:
2024-08-14
Family Accession:
NF019291.5
Method:
HMM
3.

methyltransferase

This domain is found in ribosomal RNA small subunit methyltransferase C (eg Swiss:P44453) as well as other methyltransferases (eg Swiss:Q53742). (from Pfam)

GO Terms:
Molecular Function:
methyltransferase activity (GO:0008168)
Date:
2024-08-14
Family Accession:
NF017026.5
Method:
HMM
4.

Met-10+ like-protein

The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast (Swiss:P38793) suggesting this protein may be involved in methionine biosynthesis, transport and/or utilisation [1]. [1]. 7557397. Sequence of the met-10+ locus of Neurospora crassa: homology to. a sequence of unknown function in Saccharomyces cerevisiae. chromosome 8.. Chow CM, Kang S, Metzenberg RL, RajBhandary UL;. Gene 1995;162:111-115. (from Pfam)

Date:
2024-08-14
Family Accession:
NF014527.5
Method:
HMM
5.

N-6 DNA methylase

Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (Pfam:PF01420), and R [1]. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes. [1]. 9440532. A type IC restriction-modification system in Lactococcus lactis.. Schouler C, Clier F, Lerayer AL, Ehrlich SD, Chopin MC;. J Bacteriol 1998;180:407-411.. [2]. 9593305. Combinational variation of restriction modification. specificities in Lactococcus lactis.. Schouler C, Gautier M, Ehrlich SD, Chopin MC;. Mol Microbiol 1998;28:169-178.. [3]. 9108149. The specificity of sty SKI, a type I restriction enzyme, implies. a structure with rotational symmetry.. Thorpe PH, Ternent D, Murray NE;. Nucleic Acids Res 1997;25:1694-1700. (from Pfam)

GO Terms:
Molecular Function:
DNA binding (GO:0003677)
Molecular Function:
N-methyltransferase activity (GO:0008170)
Date:
2024-08-14
Family Accession:
NF014442.5
Method:
HMM
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
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8.
new record, indexing in progress
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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
Family Accession:
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