Summary: Copper type II ascorbate-dependent monooxygenase, N-terminal domain
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This is the Wikipedia entry entitled "Copper type II ascorbate-dependent monooxygenase". More...
Copper type II ascorbate-dependent monooxygenase Edit Wikipedia article
Copper type II ascorbate-dependent monooxygenase, N-terminal domain | |||||||||
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![]() reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form | |||||||||
Identifiers | |||||||||
Symbol | Cu2_monooxygen | ||||||||
Pfam | PF01082 | ||||||||
InterPro | IPR000323 | ||||||||
PROSITE | PDOC00080 | ||||||||
SCOPe | 1phm / SUPFAM | ||||||||
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Copper type II ascorbate-dependent monooxygenase, C-terminal domain | |||||||||
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![]() reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form | |||||||||
Identifiers | |||||||||
Symbol | Cu2_monoox_C | ||||||||
Pfam | PF03712 | ||||||||
PROSITE | PDOC00080 | ||||||||
SCOPe | 1phm / SUPFAM | ||||||||
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In molecular biology, the copper type II ascorbate-dependent monooxygenases are a class of enzymes that require copper as a cofactor and which use ascorbate as an electron donor. This family contains two related enzymes, dopamine beta-monooxygenase EC 1.14.17.1 and peptidylglycine alpha-amidating monooxygenase EC 1.14.17.3. There are a few regions of sequence similarities between these two enzymes, two of these regions contain clusters of conserved histidine residues which are most probably involved in binding copper.[1]
References
- ^ Southan C, Kruse LI (September 1989). "Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain". FEBS Letters. 255 (1): 116–20. doi:10.1016/0014-5793(89)81072-5. PMID 2792366.
External links
- Eukaryotic Linear Motif resource motif class MOD_Cter_Amidation
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The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.
External database links
PROSITE: | PDOC00080 |
SCOP: | 1phm |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000323
Copper type II, ascorbate-dependent monooxygenases [PUBMED:2792366] are a class of enzymes that requires copper as a cofactor and which uses ascorbate as an electron donor. This family contains two related enzymes, dopamine-beta-monooxygenase (EC) and peptidyl-glycine alpha-amidating monooxygenase (EC). There are a few regions of sequence similarities between these two enzymes, two of these regions contain clusters of conserved histidine residues which are most probably involved in binding copper.
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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Pfam Clan
This family is a member of clan PHM_PNGase_F (CL0612), which has the following description:
Members of this superfamily adopt a beta-sandwich fold. With two adjacent domains in a protein interacting in the same way as nucleoplasmins that share the same fold. This superfamily includes the Peptide-N-glycosidase F enzymes and the peptidylglycine alpha-hydroxylating monooxygenase enzymes.
The clan contains the following 4 members:
Cu2_monoox_C Cu2_monooxygen N-glycanase_C N-glycanase_NAlignments
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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, 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 (123) |
Full (1880) |
Representative proteomes | UniProt (3243) |
NCBI (5174) |
Meta (16) |
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RP15 (608) |
RP35 (899) |
RP55 (1373) |
RP75 (1935) |
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Jalview | |||||||||
HTML | |||||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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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 (123) |
Full (1880) |
Representative proteomes | UniProt (3243) |
NCBI (5174) |
Meta (16) |
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RP15 (608) |
RP35 (899) |
RP55 (1373) |
RP75 (1935) |
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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.
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: | Prosite |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 123 |
Number in full: | 1880 |
Average length of the domain: | 120.30 aa |
Average identity of full alignment: | 31 % |
Average coverage of the sequence by the domain: | 19.02 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 131 | ||||||||||||
Family (HMM) version: | 21 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
Cu2_monoox_CStructures
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 Cu2_monooxygen domain has been found. There are 33 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 sequence.
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