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Items: 1 to 20 of 22

1.

Methyltr_RsmF/B-like, ferredoxin-like domain

This entry represents a ferredoxin-like domain found in methyltransferases RsmB, RsmF and related sequences [1-5]. Paper describing PDB structure 1ixk. [1]. 14997580. Crystal structure of human p120 homologue protein PH1374 from Pyrococcus horikoshii. Ishikawa I, Sakai N, Tamura T, Yao M, Watanabe N, Tanaka I;. Proteins. 2004;54:814-816. Paper describing PDB structure 1sqf. [2]. 14656444. The first structure of an RNA m5C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate. Foster PG, Nunes CR, Greene P, Moustakas D, Stroud RM;. Structure. 2003;11:1609-1620. Paper describing PDB structure 2frx. [3]. 16793063. The structure of the RNA m5C methyltransferase YebU from Escherichia coli reveals a C-terminal RNA-recruiting PUA domain. Hallberg BM, Ericsson UB, Johnson KA, Andersen NM, Douthwaite S, Nordlund P, Beuscher AE 4th, Erlandsen H;. J Mol Biol. 2006;360:774-787. Paper describing PDB structure 2yxl. [4]. 21123870. Structure of an archaeal homologue of the bacterial Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase. Hikida Y, Kuratani M, Bessho Y, Sekine SI, Yokoyama S;. Acta Crystallogr D Biol Crystallogr. 2010;66:1301-1307. Paper describing PDB structure 5zvd. [5]. 30541086. Archaeal NSUN6 catalyzes m5C72 modification on a wide-range of specific tRNAs. Li J, Li H, Long T, Dong H, Wang ED, Liu RJ;. Nucleic Acids Res. 2019;47:2041-2055. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046835.1
Method:
HMM
2.

methyltransferase domain-containing protein

This family appears to have methyltransferase activity. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025217.5
Method:
HMM
3.

methyltransferase domain-containing protein

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

Date:
2024-08-14
Family Accession:
NF025033.5
Method:
HMM
4.

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
5.

SAM-dependent methyltransferase

This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesised that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping [2]. [1]. 10983982. RNA methylation under heat shock control. Bugl H, Fauman EB, Staker BL, Zheng F, Kushner SR, Saper MA, Bardwell JC, Jakob U;. Mol Cell 2000;6:349-360. [2]. 8385698. Computer-assisted identification of a putative methyltransferase domain in NS5 protein of flaviviruses and lambda 2 protein of reovirus. Koonin EV;. J Gen Virol 1993;74:733-740. (from Pfam)

GO Terms:
Molecular Function:
methyltransferase activity (GO:0008168)
Date:
2024-10-16
Family Accession:
NF013856.5
Method:
HMM
6.

16S rRNA methyltransferase RsmB/F

This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme [1,2]. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA [1,2]. [1]. 14997580. Crystal structure of human p120 homologue protein PH1374 from Pyrococcus horikoshii. Ishikawa I, Sakai N, Tamura T, Yao M, Watanabe N, Tanaka I;. Proteins. 2004;54:814-816. [2]. 20558545. Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus. Demirci H, Larsen LH, Hansen T, Rasmussen A, Cadambi A, Gregory ST, Kirpekar F, Jogl G;. RNA. 2010;16:1584-1596. (from Pfam)

GO Terms:
Molecular Function:
methyltransferase activity (GO:0008168)
Date:
2024-10-16
Family Accession:
NF013362.5
Method:
HMM
7.

transcription antitermination factor NusB

The NusB protein is involved in the regulation of rRNA biosynthesis by transcriptional antitermination. NMR structure. [1]. 9670024. Solution structure of the antitermination protein NusB of Escherichia coli: a novel all-helical fold for an RNA-binding protein. Huenges M, Rolz C, Gschwind R, Peteranderl R, Berglechner F, Richter G, Bacher A, Kessler H,Gemmecker G;. EMBO J 1998;17:4092-4100. (from Pfam)

GO Terms:
Molecular Function:
RNA binding (GO:0003723)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Date:
2024-10-16
Family Accession:
NF013216.5
Method:
HMM
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.
new record, indexing in progress
Family Accession:
17.
new record, indexing in progress
Family Accession:
18.
new record, indexing in progress
Family Accession:
19.

16S rRNA (cytosine(967)-C(5))-methyltransferase

16S rRNA (cytosine(967)-C(5))-methyltransferase specifically methylates cytosine(967) at C(5) in 16S rRNA

Date:
2023-03-14
Family Accession:
11485070
Method:
Sparcle
20.

16S rRNA (cytosine(967)-C(5))-methyltransferase RsmB

Catalyzes the methylation of the C5 position of C967 of the 16S rRNA

Gene:
rsmB
GO Terms:
Biological Process:
RNA methylation (GO:0001510)
Molecular Function:
RNA binding (GO:0003723)
Biological Process:
regulation of DNA-templated transcription (GO:0006355)
Biological Process:
rRNA processing (GO:0006364)
Molecular Function:
rRNA methyltransferase activity (GO:0008649)
Date:
2021-07-23
Family Accession:
NF008149.0
Method:
HMM
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