SUPERFAMILY 1.75 HMM library and genome assignments server


Hemocyanin, N-terminal domain superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All alpha proteins [ 46456] (284)
Fold:   Hemocyanin, N-terminal domain [ 48049]
Superfamily:   Hemocyanin, N-terminal domain [ 48050]
Families:   Hemocyanin, N-terminal domain [ 48051]


Superfamily statistics
Genomes (41) Uniprot 2014_06 PDB chains (SCOP 1.75)
Domains 337 1,034 4
Proteins 331 1,029 4


Functional annotation
General category Metabolism
Detailed category Energy

Document:
Function annotation of SCOP domain superfamilies

Gene Ontology (high-coverage)

(show details)
GO term FDR (all) SDFO level Annotation (direct or inherited)
Biological Process (BP) single-organism metabolic process 0.2716 Least Informative Inherited
Biological Process (BP) cellular aromatic compound metabolic process 0.07821 Least Informative Inherited
Biological Process (BP) organic cyclic compound metabolic process 0.1113 Least Informative Inherited
Biological Process (BP) response to stimulus 0.8114 Least Informative Inherited
Biological Process (BP) organic hydroxy compound metabolic process 1.61e-06 Moderately Informative Direct
Biological Process (BP) pigment metabolic process 6.935e-09 Informative Direct
Biological Process (BP) secondary metabolic process 3.883e-07 Informative Direct
Biological Process (BP) defense response 0.0005554 Informative Direct
Biological Process (BP) phenol-containing compound metabolic process 3.016e-12 Highly Informative Direct
Molecular Function (MF) binding 9.8e-07 Least Informative Direct
Molecular Function (MF) cation binding 0 Moderately Informative Direct
Molecular Function (MF) anion binding 0 Moderately Informative Direct
Molecular Function (MF) oxidoreductase activity 0.0001262 Moderately Informative Direct
Molecular Function (MF) copper ion binding 0 Highly Informative Direct
Molecular Function (MF) monooxygenase activity 2.726e-05 Highly Informative Direct
Molecular Function (MF) oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxyge 0.0001728 Highly Informative Direct
Cellular Component (CC) cytoplasmic part 1 Least Informative Inherited
Cellular Component (CC) extracellular region part 0.00175 Moderately Informative Inherited
Cellular Component (CC) extracellular space 3.317e-05 Informative Direct

Document: GO annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Oxidoreductases0Least InformativeDirect
Enzyme Commission (EC)Acting on paired donors, with incorporation or red0Moderately InformativeDirect
Enzyme Commission (EC)Monophenol monooxygenase0Highly InformativeDirect

Document: EC annotation of SCOP domains

Fly Phenotype (FP)

(show details)
FP termFDR (all)SDFP levelAnnotation (direct or inherited)
Fly Phenotype (FP)electrophoretic variant2.175e-06InformativeDirect

Document: FP annotation of SCOP domains

Fly Anatomy (FA)

(show details) Document: FA annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Oxidoreductases0Least InformativeDirect
Enzyme Commission (EC)Acting on paired donors, with incorporation or reduction of molecular oxygen0InformativeDirect
Enzyme Commission (EC)With another compound as one donor, and incorporation of one atom of oxygen0Highly InformativeDirect

Document: EC annotation of SCOP domains

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processTransport8.985e-11Least InformativeDirect
Biological processOxygen transport0Highly InformativeDirect
Cellular componentSecreted0Moderately InformativeDirect
DomainSignal0Least InformativeDirect
Molecular functionMetal-binding4.626e-07Least InformativeDirect
Molecular functionCopper0InformativeDirect
Post-translational modificationOxidoreductase0.05465Moderately InformativeInherited
Post-translational modificationStorage protein0Highly InformativeDirect
Post-translational modificationMonooxygenase2.498e-09Highly InformativeDirect
Post-translational modificationGlycoprotein4.595e-16Least InformativeDirect
Post-translational modificationDisulfide bond1.991e-05Least InformativeDirect

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 [PubMed3207675]. 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) [PubMed2808410] 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
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural 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

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.


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.


Browse and view proteins in genomes which have different domain combinations including a Hemocyanin, N-terminal domain domain.


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.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

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.


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 ]