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8  structures 2815  species 2  interactions 4691  sequences 41  architectures

Family: MOSC (PF03473)

Summary: MOSC domain

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MOSC domain Provide feedback

The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich domains identified in the molybdenum cofactor sulfurase and several other proteins from both prokaryotes and eukaryotes. These MOSC domains contain an absolutely conserved cysteine and occur either as stand-alone forms such as P32157 or fused to other domains such as NifS-like catalytic domain in Molybdenum cofactor sulfurase. The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters.

Literature references

  1. Anantharaman V, Aravind L; , FEMS Microbiol Lett 2002;207:55-61.: MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal--sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases. PUBMED:11886751 EPMC:11886751


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR005302

Molybdenum cofactor (MOCO) sulphurases [PUBMED:16784786] catalyse the insertion of a terminal sulphur ligand into the molybdenum cofactor, thereby converting the oxo form of MOCO to a sulphurylated form. Suphurylated MOCO is required by several enzymes, including: aldehyde oxidase (EC), which function in the last step of abscisic acid biosynthesis in plants [PUBMED:11549764]; and xanthine dehydrogenase (EC), which synthesis uric acid from xanthine during nitrogen metabolism [PUBMED:12650690].

This entry represents the beta-barrel C-terminal domain of MOCO sulphurase (MOSC domain), which has a beta-barrel structure similar to that of the beta-barrel domain in pyruvate kinase and contains a highly conserved cysteine residue required for activity. MOSC domains are found in several diverse metal-sulphur cluster biosynthesis proteins from both eukaryotes and prokaryotes. MOSC domains occu as either stand-alone forms, such as the YiiM protein from Escherichia coli, or fused to other domains, such as a NifS-like catalytic domain in MOCO sulphurase. The MOSC domain is predicted to be a sulphur-carrier domain that receives sulphur abstracted from pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulphur-metal clusters [PUBMED:11886751].

The MOSC domain contains several patches of hydrophobic residues and an absolutely conserved cysteine residue situated closer to the C-terminal end of the domain. The absolutely conserved cysteine in the MOSC domain is reminiscent of the analogous conservation of a cysteine in the active site of the thioredoxin and rhodanese superfamilies. Members of both these superfamilies, especially of the latter one, have been implicated in the synthesis of Fe-S clusters, through mobilisation of sulphur with their active cysteine.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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...

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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
(30)
Full
(4691)
Representative proteomes NCBI
(3587)
Meta
(1209)
RP15
(425)
RP35
(840)
RP55
(1217)
RP75
(1479)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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Format an alignment

  Seed
(30)
Full
(4691)
Representative proteomes NCBI
(3587)
Meta
(1209)
RP15
(425)
RP35
(840)
RP55
(1217)
RP75
(1479)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(30)
Full
(4691)
Representative proteomes NCBI
(3587)
Meta
(1209)
RP15
(425)
RP35
(840)
RP55
(1217)
RP75
(1479)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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 View help on the curation process

Seed source: Aravind L, Anantharaman V
Previous IDs: none
Type: Domain
Author: Aravind L, Anantharaman V
Number in seed: 30
Number in full: 4691
Average length of the domain: 130.30 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 44.61 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.3 21.3
Noise cut-off 20.9 21.2
Model length: 133
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

MOSC 3-alpha

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 MOSC 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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