Protein Domain : IPR008972

Type:  Domain Name:  Cupredoxin
Description:  Copper is one of the most prevalent transition metals in living organisms and its biological function is intimately related to its redox properties. Since free copper is toxic, even at very low concentrations, its homeostasis in living organisms is tightly controlled by subtle molecular mechanisms. In eukaryotes, before being transported inside the cell via the high-affinity copper transporters of the CTR family, the copper (II) ion is reduced to copper (I). In blue copper proteins such as Cupredoxin, the copper (I) ion form is stabilised by a constrained His2Cys coordination environment.This entry represents cupredoxin proteins, as well as structural homologues to cupredoxin. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel []. Some of these proteins have lost the ability to bind copper. Proteins with a cupredoxin-type fold are found in the following family groups: Mono-domain cupredoxins, such as amicyanin, plastocyanin, pseudoazurin, plantacyanin, azurin, auracyanin, rusticyanin, stellacyanin, and mavicyanin.Multi-domain cupredoxins, such as nitrite reductase (2 domains of this fold), multicopper oxidase CueO, spore coat protein A, ascorbate oxidase (3 domains of this fold), laccase (3 domains of this fold), ceruloplamin (6 domains of this fold), and coagulation factor V.Red copper protein nitrocyanin and the C-terminal of nitrous oxide reductase.Quinol oxidase and the periplasmic domain of cytochrome c oxidase subunit II.Ephrin-a5 and ephrin-b2 ectodomain, which are related to cupredoxins but lack the metal-binding site.The N-terminal domain of protein arginine deiminase Pad4, which is related to cupredoxin but lacks the metal-biding site. Short Name:  Cupredoxin
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4 Child Features

DB identifier Type Name
IPR000923 Domain Blue (type 1) copper domain
IPR002429 Domain Cytochrome c oxidase subunit II C-terminal
IPR028096 Domain EfeO-type cupredoxin-like domain
IPR013732 Domain Protein-arginine deiminase (PAD) N-terminal

8 Contains

DB identifier Type Name
IPR001117 Domain Multicopper oxidase, type 1
IPR011707 Domain Multicopper oxidase, type 3
IPR011706 Domain Multicopper oxidase, type 2
IPR003245 Domain Phytocyanin domain
IPR010514 Domain COX aromatic rich motif
IPR002355 Binding_site Multicopper oxidase, copper-binding site
IPR001505 Binding_site Copper centre Cu(A)
IPR019765 Conserved_site Ephrin, conserved site

2 Cross Referencess

Identifier
G3DSA:2.60.40.420
SSF49503

10 Found Ins

DB identifier Type Name
IPR001235 Family Blue (type 1) copper protein, plastocyanin-type
IPR017761 Family Laccase
IPR017760 Family L-ascorbate oxidase, plants
IPR001287 Family Nitrite reductase, copper-type
IPR006376 Family Copper-resistance protein CopA
IPR001799 Domain Ephrin receptor-binding domain
IPR010532 Family Sulfocyanin
IPR017762 Family L-ascorbate oxidase, fungi
IPR014707 Family Coagulation factor 8
IPR017527 Family Nitrosocyanin

0 GO Annotation

0 Ontology Annotations

0 Parent Features

37718 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
430328 D8T923 PAC:15419278 Selaginella moellendorffii 111  
410532 D8RF19 PAC:15406387 Selaginella moellendorffii 537  
431097 D8TBI3 PAC:15420065 Selaginella moellendorffii 280  
431735 D8TDL9 PAC:15402881 Selaginella moellendorffii 282  
95740 D8RKK0 PAC:15407038 Selaginella moellendorffii 562  
19117 D8RLJ8 PAC:15423483 Selaginella moellendorffii 103  
165365 D8QU76 PAC:15412743 Selaginella moellendorffii 578  
404075 D8QU74 PAC:15407082 Selaginella moellendorffii 570  
404333 D8QV04 PAC:15409398 Selaginella moellendorffii 589  
438115 D8QU75 PAC:15418798 Selaginella moellendorffii 589  
78002 D8QV03 PAC:15418410 Selaginella moellendorffii 533  
78404 D8QV05 PAC:15421352 Selaginella moellendorffii 582  
19307 D8RTQ5 PAC:15402679 Selaginella moellendorffii 101  
39173 D8RUP8 PAC:15415832 Selaginella moellendorffii 84  
404967 D8QXY5 PAC:15414154 Selaginella moellendorffii 3075  
405136 D8QYI7 PAC:15410837 Selaginella moellendorffii 235  
405234 D8QWP7 PAC:15411596 Selaginella moellendorffii 252  
80214 D8QXR5 PAC:15403685 Selaginella moellendorffii 532  
80405 D8QXB9 PAC:15405211 Selaginella moellendorffii 52  
104957 D8RZ50 PAC:15415877 Selaginella moellendorffii 582  
105894 D8S0U4 PAC:15418074 Selaginella moellendorffii 566  
443452 D8S1K8 PAC:15413844 Selaginella moellendorffii 287  
37976 D8S3E3 PAC:15416110 Selaginella moellendorffii 135  
418427 D8S5N7 PAC:15406664 Selaginella moellendorffii 588  
230356 PAC:15413166 Selaginella moellendorffii 566  
27471 D8QZ20 PAC:15404938 Selaginella moellendorffii 99  
406169 D8R1H5 PAC:15413903 Selaginella moellendorffii 385  
24493 D8SK39 PAC:15418656 Selaginella moellendorffii 258  
422957 D8SK35 PAC:15422525 Selaginella moellendorffii 179  
167855 D8R485 PAC:15422272 Selaginella moellendorffii 173  

1 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11867755