Summary

This is the summary of UniProt entry RSMJ_CITK8 (A8AR83).

Description:

Ribosomal RNA small subunit methyltransferase J EC=2.1.1.242

Source organism:

Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) (NCBI taxonomy ID 290338)
View Pfam proteome data.

Length:

252 amino acids

Please note: when we start each new Pfam data release, we take a copy of the UniProt sequence database. This snapshot of UniProt forms the basis of the overview that you see here. It is important to note that, although some UniProt entries may be removed after a Pfam release, these entries will not be removed from Pfam until the next Pfam data release.

Pfam domains

Source	Domain	Start	End	Gathering threshold (bits)		Score (bits)		E-value
Source	Domain	Start	End	Sequence	Domain	Sequence	Domain	Sequence	Domain
Pfam A	SAM_MT	14	248	26.00	26.00	382.20	382.00	1e-111	1.1e-111

Show or hide domain scores.

Sequence annotations

This section shows a graphical representation of this sequence, with Pfam domains shown in the standard Pfam format. Under the Pfam domain image we show various tracks, illustrating features on this sequence that we found in other databases. You can choose which databases to include using the drop-down panel under the image. More...

We generate the topmost image from data in the Pfam database, but subsequent images are constructed on-the-fly using data retrieved from other sources using the Distributed Annotation System (DAS). DAS is a system for sharing sequence annotations in a standard format and we use it to find features and sequence information from a wide variety of other sources, from UniProt to InterPro to Superfamily.

Each DAS source is represented in a new track, although some sources may generate more than one track, if they have features which overlap. Each feature that we find is shown as a simple box, positioned according to its residue position on the sequence.

Moving your mouse over a feature in the display will highlight the feature and show a tooltip giving details of the feature. If the DAS source supplied a URL, you can also click on the feature to visit that URL. In some browsers you will also see a thin, vertical cursor, which follows the mouse and shows the residue position within the sequence.

You can turn DAS sources on and off using the control panel under the sequence images. Check the boxes for the DAS sources that you want to see; uncheck those that you are not interested in. Press Update to query the new set of DAS sources and re-generate the image. Note that if you have lots of sources turned on, the time taken to generate the images will increase. You can see the homepage for each of the DAS sources by clicking on its name in the update panel. The "source" link next to each source points directly at the DAS source. Depending on how the source is configured, that link may return some usage information or simply an XML fragment with the response to the empty query that you just made.

Please note: this is an experimental feature and there are several known bugs and limitations. Please be patient as we improve the tool.

Note: it can take a few seconds for this image to be generated and loaded.

Loading feature alignment...

Show sources update panel.

Sequence information

This is the amino acid sequence of the UniProt sequence database entry with the accession A8AR83. This sequence is stored in the Pfam database and updated with each new Pfam release, but this means that the sequence we store may differ from that stored by UniProt.

Sequence:

MKICLVDETG AGDGALSVLA ARWGLEHDEN NPMALVLTTA HLELRKRDEP

KLGGIFVDFV GGAMAHRRKF GGGRGEAVAK AVGIKGDYLP DVVDATAGLG

100

101

RDAFVLASVG CRVRMLERNP VVAALLDDGL ARGYADPEIG PWLQERLQLI

150

151

HASSLTALTD ITPRPQVVYL DPMFPHKQKS ALVKKEMRVF QSLVGPDLDA

200

201

DGLLAPARQL ATKRVVVKRP DYAPPLADIA TPNAVVTKGH RFDIYTGTAL

250

251

252

Show the unformatted sequence.

Checksums:

CRC64:48A6C602BA3A784E

MD5:5840c5efc2e607a95b006a882be5abd4

Protein: RSMJ_CITK8 (A8AR83)

Jump to...

Summary

Pfam domains

Sequence annotations

Sequence information