Summary: DsrC like protein
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DsrC like protein Provide feedback
Family member P45573 has been observed to co-purify with Desulfovibrio vulgaris dissimilatory sulfite reductase [1] and many members of this family are annotated as the third (gamma) subunit of dissimilatory sulphite reductase. However, this protein appears to be only loosely associated to the sulfite reductase, which suggests that DsrC may not be an integral part of the dissimilatory sulphite reductase. Members of this family are found in organisms such as E. coli and H. influenzae which do not contain dissimilatory sulphite reductases but can synthesise assimilatory sirohaem sulphite and nitrite reductases. It is speculated that DsrC may be involved in the assembly, folding or stabilisation of sirohaem proteins [2]. The strictly conserved cysteine in the C terminus suggests that DsrC may have a catalytic function in the metabolism of sulphur compounds [3].
Literature references
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Pierik AJ, Duyvis MG, van Helvoort JM, Wolbert RB, Hagen WR; , Eur J Biochem 1992;205:111-115.: The third subunit of desulfoviridin-type dissimilatory sulfite reductases. PUBMED:1555572 EPMC:1555572
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Molitor M, Dahl C, Molitor I, Schafer U, Speich N, Huber R, Deutzmann R, Truper HG; , Microbiology 1998;144:529-541.: A dissimilatory sirohaem-sulfite-reductase-type protein from the hyperthermophilic archaeon Pyrobaculum islandicum. PUBMED:9493389 EPMC:9493389
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Pott AS, Dahl C; , Microbiology 1998;144:1881-1894.: Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. PUBMED:9695921 EPMC:9695921
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Cort JR, Mariappan SV, Kim CY, Park MS, Peat TS, Waldo GS, Terwilliger TC, Kennedy MA; , Eur J Biochem 2001;268:5842-5850.: Solution structure of Pyrobaculum aerophilum DsrC, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase. PUBMED:11722571 EPMC:11722571
External database links
| PANDIT: | PF04358 |
| Pseudofam: | PF04358 |
| SCOP: | 1ji8 |
| SYSTERS: | DsrC |
This tab holds annotation information from the InterPro database.
InterPro entry IPR007453
Members of this protein family include TusE, a partner to TusBCD in a sulphur relay system for 2-thiouridine biosynthesis, a tRNA base modification process [PUBMED:16387657]. Other members are DsrC [PUBMED:18829451], a functionally similar protein in species where the sulphur relay system exists primarily for sulphur metabolism rather than tRNA base modification. Some members of this family are known explicitly as the gamma subunit of sulphite reductases.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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...
View options
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 (87) |
Full (1238) |
Representative proteomes | NCBI (699) |
Meta (173) |
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| RP15 (84) |
RP35 (153) |
RP55 (208) |
RP75 (258) |
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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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 (87) |
Full (1238) |
Representative proteomes | NCBI (699) |
Meta (173) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (84) |
RP35 (153) |
RP55 (208) |
RP75 (258) |
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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: | COG2920 |
| Previous IDs: | none |
| Type: | Family |
| Author: | Kerrison ND |
| Number in seed: | 87 |
| Number in full: | 1238 |
| Average length of the domain: | 107.10 aa |
| Average identity of full alignment: | 55 % |
| Average coverage of the sequence by the domain: | 95.17 % |
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: | 109 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
DsrCStructures
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 DsrC domain has been found. There are 8 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