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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
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC 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
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 · Enzyme Commission (EC) · Fly Anatomy (FA) · Enzyme Commission (EC) ]
Internal database links
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 · Enzyme Commission (EC) · Fly Anatomy (FA) · Enzyme Commission (EC) · Internal database links ]
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