Summary: KNTase C-terminal domain
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This is the Wikipedia entry entitled "Kanamycin nucleotidyltransferase". More...
Kanamycin nucleotidyltransferase Edit Wikipedia article
| kanamycin nucleotidyltransferase | |||||||||
| Identifiers | |||||||||
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| Symbol | KNTase_C | ||||||||
| Pfam | PF07827 | ||||||||
| Pfam clan | CL0291 | ||||||||
| InterPro | IPR012481 | ||||||||
| SCOP | 1kny | ||||||||
| SUPERFAMILY | 1kny | ||||||||
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In molecular biology, kanamycin nucleotidyltransferase EC 2.7.7.- (KNTase) is an enzyme which is involved in conferring resistance to aminoglycoside antibiotics. It catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two domains. The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site.[1]
[edit] References
- ^ Pedersen LC, Benning MM, Holden HM (October 1995). "Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase". Biochemistry 34 (41): 1330511. DOI:10.1021/bi00041a005. PMID 7577914.
This article incorporates text from the public domain Pfam and InterPro IPR012481
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
KNTase C-terminal domain Provide feedback
Kanamycin nucleotidyltransferase (KNTase) is involved in conferring resistance to aminoglycoside antibiotics and catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two domains. The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site [1].
Literature references
-
Pedersen LC, Benning MM, Holden HM; , Biochemistry 1995;34:13305-13311.: Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. PUBMED:7577914 EPMC:7577914
External database links
| PANDIT: | PF07827 |
| Pseudofam: | PF07827 |
| SCOP: | 1kny |
| SYSTERS: | KNTase_C |
This tab holds annotation information from the InterPro database.
InterPro entry IPR012481
Kanamycin nucleotidyltransferase (KNTase) is involved in conferring resistance to aminoglycoside antibiotics and catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two domains. The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site [PUBMED:7577914].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | nucleotidyltransferase activity (GO:0016779) |
| Biological process | response to antibiotic (GO:0046677) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan KNTase_C (CL0291), which contains the following 8 members:
DUF294_C DUF4145 DUF86 GlnD_UR_UTase HEPN KNTase_C NTase_sub_bind PaREP1Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (2) |
Full (78) |
Representative proteomes | NCBI (39) |
Meta (0) |
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| RP15 (3) |
RP35 (7) |
RP55 (8) |
RP75 (9) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (2) |
Full (78) |
Representative proteomes | NCBI (39) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (3) |
RP35 (7) |
RP55 (8) |
RP75 (9) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_29524 (release 14.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Fenech M |
| Number in seed: | 2 |
| Number in full: | 78 |
| Average length of the domain: | 137.40 aa |
| Average identity of full alignment: | 69 % |
| Average coverage of the sequence by the domain: | 57.06 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 143 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the KNTase_C domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence