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Links from Protein

Items: 1 to 20 of 27

1.

ribonuclease J1

Ribonuclease J1, as the term is used in Staphylococcus aureus, is one of two RNase J paralogs that are about 40 percent identical.

Gene:
rnjA
Date:
2024-08-03
Family Accession:
NF047419.1
Method:
HMM
2.

Ribonuclease J C-terminal domain

This domain is found at the C-terminus of Ribonuclease J proteins. Its function is unknown, but deletion of this domain causes dissociation to monomers [2]. [1]. 21893286. Molecular basis for the recognition and cleavage of RNA by the. bifunctional 5'-3' exo/endoribonuclease RNase J.. Dorleans A, Li de la Sierra-Gallay I, Piton J, Zig L, Gilet L,. Putzer H, Condon C;. Structure. 2011;19:1252-1261.. [2]. 18204464. Structural insights into the dual activity of RNase J.. Li de la Sierra-Gallay I, Zig L, Jamalli A, Putzer H;. Nat Struct Mol Biol. 2008;15:206-212. (from Pfam)

Date:
2024-08-14
Family Accession:
NF036802.5
Method:
HMM
3.

Ribonuclease J, beta-CASP domain

Date:
2024-08-14
Family Accession:
NF046302.1
Method:
HMM
4.

MBL fold metallo-hydrolase

The MBL fold superfamily includes the metallo-beta-lactamases (class B beta-lactamases), but includes also a much larger family of hydrolases that are not beta-lactamases at all. See also the related family PF00753.

Date:
2024-08-14
Family Accession:
NF024118.5
Method:
HMM
5.

MBL fold metallo-hydrolase RNA specificity domain-containing protein

The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in Pfam:PF00753 and are common to all metallo-beta-lactamases. This, the fifth motif [1], appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 [4] which are involved in the processing of mRNA [2,3]. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases [2,3,4]. [1]. 12177301. Metallo-beta-lactamase fold within nucleic acids processing. enzymes: the beta-CASP family.. Callebaut I, Moshous D, Mornon JP, de Villartay JP;. Nucleic Acids Res 2002;30:3592-3601.. [2]. 17128255. Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing. endonuclease.. Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley. JL, Tong L;. Nature. 2006;444:953-956.. [3]. 20544974. Crystal structure of an archaeal cleavage and polyadenylation. specificity factor subunit from Pyrococcus horikoshii.. Nishida Y, Ishikawa H, Baba S, Nakagawa N, Kuramitsu S, Masui R;. Proteins. 2010;78:2395-2398.. [4]. 21764917. Characterization of components of the Staphylococcus aureus mRNA. degradosome holoenzyme-like complex.. Roux CM, DeMuth JP, Dunman PM;. J Bacteriol. 2011;193:5520-5526. (from Pfam)

Date:
2024-08-14
Family Accession:
NF019159.5
Method:
HMM
6.

MBL fold metallo-hydrolase

Date:
2024-08-14
Family Accession:
NF012955.5
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.

ribonuclease J

ribonuclease J plays a key part in RNA processing and in RNA degradation; it can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end

Date:
2024-05-13
Family Accession:
11426779
Method:
Sparcle
20.
new record, indexing in progress
Family Accession:
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