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Hemocyanin, N-terminal domain superfamily
SCOP classification
Superfamily statistics
Functional annotation
| General category | Metabolism |
| Detailed category | Energy |
Document: Function annotation of SCOP domain superfamilies
Gene Ontology (high-coverage) (show details)
Highlighted in gray are those with either FDR_singleton>0.001 or FDR_all>0.001
|
GO term |
FDR (all) |
IC level |
SDFO level |
Annotation (direct or inherited) |
| Biological Process (BP) |
metabolic process |
1 |
0.2411 |
-- |
INHERITED FROM: phenol-containing compound metabolic process || organic hydroxy compound metabolic process |
| Biological Process (BP) |
biological_process |
1 |
0 |
-- |
INHERITED FROM: phenol-containing compound metabolic process || organic hydroxy compound metabolic process |
| Biological Process (BP) |
organic substance metabolic process |
1 |
0.2676 |
-- |
INHERITED FROM: phenol-containing compound metabolic process || organic hydroxy compound metabolic process |
| Biological Process (BP) |
cellular process |
1 |
0.1415 |
-- |
INHERITED FROM: phenol-containing compound metabolic process |
| Biological Process (BP) |
cellular metabolic process |
1 |
0.2708 |
-- |
INHERITED FROM: phenol-containing compound metabolic process |
| Biological Process (BP) |
cellular aromatic compound metabolic process |
0.1026 |
0.6271 |
Least Informative |
INHERITED FROM: phenol-containing compound metabolic process |
| Biological Process (BP) |
organic cyclic compound metabolic process |
0.1418 |
0.5817 |
Least Informative |
INHERITED FROM: phenol-containing compound metabolic process |
| Biological Process (BP) |
organic hydroxy compound metabolic process |
1.032e-06 |
1.208 |
Moderately Informative |
DIRECT |
| Biological Process (BP) |
phenol-containing compound metabolic process |
6.257e-12 |
2 |
Highly Informative |
DIRECT |
| Molecular Function (MF) |
metal ion binding |
0 |
1.134 |
-- |
DIRECT |
| Molecular Function (MF) |
ion binding |
0 |
0.8334 |
-- |
DIRECT |
| Molecular Function (MF) |
molecular_function |
0.068 |
0 |
-- |
INHERITED FROM: cation binding || monooxygenase activity || transition metal ion binding || copper ion binding || oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxyge || anion binding || chloride ion binding || monophenol monooxygenase activity || ion binding || oxidoreductase activity || metal ion binding || binding || oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxyge |
| Molecular Function (MF) |
catalytic activity |
1 |
0.2686 |
-- |
INHERITED FROM: monooxygenase activity || monophenol monooxygenase activity || oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxyge || oxidoreductase activity || oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxyge |
| Molecular Function (MF) |
binding |
7.828e-07 |
0.3952 |
Least Informative |
DIRECT |
| Molecular Function (MF) |
cation binding |
0 |
1.099 |
Moderately Informative |
DIRECT |
| Molecular Function (MF) |
anion binding |
3.234e-06 |
1.076 |
Moderately Informative |
DIRECT |
| Molecular Function (MF) |
oxidoreductase activity |
0.0002161 |
0.9883 |
Moderately Informative |
DIRECT |
| Molecular Function (MF) |
transition metal ion binding |
0 |
1.317 |
Informative |
DIRECT |
| Molecular Function (MF) |
copper ion binding |
0 |
1.9 |
Highly Informative |
DIRECT |
| Molecular Function (MF) |
monooxygenase activity |
3.528e-05 |
1.98 |
Highly Informative |
DIRECT |
| Molecular Function (MF) |
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxyge |
0.0002067 |
1.775 |
Highly Informative |
DIRECT |
| Cellular Component (CC) |
extracellular region part |
0.000265 |
1.127 |
-- |
DIRECT |
| Cellular Component (CC) |
cell |
1 |
0.08068 |
-- |
INHERITED FROM: lipid particle |
| Cellular Component (CC) |
intracellular part |
1 |
0.1266 |
-- |
INHERITED FROM: lipid particle |
| Cellular Component (CC) |
intracellular |
1 |
0.1266 |
-- |
INHERITED FROM: lipid particle |
| Cellular Component (CC) |
cytoplasm |
1 |
0.2515 |
-- |
INHERITED FROM: lipid particle |
| Cellular Component (CC) |
cell part |
1 |
0.08068 |
-- |
INHERITED FROM: lipid particle |
| Cellular Component (CC) |
cellular_component |
1 |
0 |
-- |
INHERITED FROM: extracellular space || extracellular region part || lipid particle || extracellular region |
| Cellular Component (CC) |
cytoplasmic part |
1 |
0.2605 |
Least Informative |
INHERITED FROM: lipid particle |
| Cellular Component (CC) |
extracellular region |
1.47e-13 |
0.9505 |
Moderately Informative |
DIRECT |
| Cellular Component (CC) |
extracellular space |
3.688e-05 |
1.395 |
Informative |
DIRECT |
| Cellular Component (CC) |
lipid particle |
6.413e-08 |
2.064 |
Highly Informative |
DIRECT |
Document: GO annotation of SCOP domains
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
Fly Phenotype (FP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: FP annotation of SCOP domains
Fly Anatomy (FA) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: FA annotation of SCOP domains
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
UniProtKB KeyWords (KW) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: KW annotation of SCOP domains
InterPro annotation
| Cross references | IPR005204 SSF48050 Protein matches |
| Abstract | Haemocyanins are copper-containing oxygen transport proteins found in the haemolymph of many invertebrates. They are divided into 2 main groups, arthropodan and molluscan. These have structurally similar oxygen-binding centres, which are similar to the oxygen-binding centre of tyrosinases
[], but their quaternary structures are arranged differently. The arthropodan proteins exist as hexamers comprising 3 heterogeneous subunits (a, b and c) and possess 1 oxygen-binding centre per
subunit; and the molluscan proteins exist as cylindrical oligomers of 10 to 20 subunits and possess 7 or 8 oxygen-binding centres per subunit [ 3207675]. Although the proteins have similar amino acid
compositions, the only real similarity in their primary sequences is in the region corresponding to the second copper-binding domain, which also shows similarity to the copper-binding domain of tyrosinases.
Larval storage proteins (LSP) [2808410] are proteins from the hemolymph of insects, which may serve as a store of amino acids for synthesis of adult proteins. There are two classes of LSP's, arylphorins, which are rich in aromatic amino acids, and methionine-rich LSP's. LSP's forms
hexameric complexes. LSP's are structurally related to arthropods hemocyanins. |
InterPro database
PDBeMotif information about ligands, sequence and structure motifs
PDBeMotif resource
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Gene Ontology (high-coverage) · Enzyme Commission (EC) · Fly Phenotype (FP) · Fly Anatomy (FA) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) ]
Internal database links
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Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.
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Alignments of sequences to 2 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.
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Browse and view proteins in genomes which have
different domain combinations including a Hemocyanin, N-terminal domain domain.
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Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
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Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.
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There are 2 hidden Markov models representing the Hemocyanin, N-terminal domain superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.
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Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Gene Ontology (high-coverage) · Enzyme Commission (EC) · Fly Phenotype (FP) · Fly Anatomy (FA) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) · Internal database links ]
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