plastocyanin; Members of this family are plastocyanin, a blue copper protein related to pseudoazurin, halocyanin, amicyanin, etc. This protein, located in the thylakoid luman, performs electron transport to photosystem I in Cyanobacteria and chloroplasts. [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  69 VEVLLGADDGGLVFQPSTFSVASGEKIVFKNNAGFPHNVIFDEDEVPSGVDVSKISMSDEDLLNGPGESYAVTLTEKGTY 148
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1895870110 149 SFYCSPHAGAGMVGKVTVN 167
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99

Plastocyanin [Energy production and conversion];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  80 LVFQPSTFSVASGEKIVFKNNAGFPHNVIFDEDevPSGVDVSKISmsdedllnGPGESYAVTLTEKGTYSFYCSPHagAG 159
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDG--PDGAFDSGLL--------APGETFSVTFDEPGTYDYYCTPH--PW 68

                  ....*..
gi 1895870110 160 MVGKVTV 166
Cdd:COG3794    69 MVGTIVV 75

plastocyanin; Members of this family are plastocyanin, a blue copper protein related to pseudoazurin, halocyanin, amicyanin, etc. This protein, located in the thylakoid luman, performs electron transport to photosystem I in Cyanobacteria and chloroplasts. [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  69 VEVLLGADDGGLVFQPSTFSVASGEKIVFKNNAGFPHNVIFDEDEVPSGVDVSKISMSDEDLLNGPGESYAVTLTEKGTY 148
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1895870110 149 SFYCSPHAGAGMVGKVTVN 167
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99

Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The Pseudocyanin-like family of copper-binding proteins (or blue (type 1) copper domain) is a family of small proteins that bind a single copper atom and are characterized by an intense electronic absorption band near 600 nm. Pseudoazurin (PAz) has been identified as a electron donor in the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. Plastocyanin is found in cyanobacteria, higher plants, and some algae where it plays a role in photosynthesis. Plastocyanin is responsible for transporting electrons from PSII to PSI. This family also includes halocyanins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis) and amicyanin found in bacteria Paracoccus denitrificans.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  69 VEVLLGADDGGLVFQPSTFSVASGEKIVFKNNAGFPHNVIFDEDEVPSGVDVSKismsdEDLLNGPGESYAVTLTEKGTY 148
Cdd:cd04204     1 VVVKMGADNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPDGDAEFE-----SDRVDEEGFTYEQTFDEPGVY 75

                          90
                  ....*....|....*..
gi 1895870110 149 SFYCSPHAGAGMVGKVT 165
Cdd:cd04204    76 GYYCTPHRGAGMVGTVI 92

Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis). Halocyanin may serve as a mobile electron carrier at a peripheral membrane protein. The copper-binding domain is present only once in some halocyanins and is duplicated in others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  69 VEVLLGADdGGLVFQPSTFSVASGEKIVFKNNA-GFPHNVIFDEDEVPSGvdvskismSDEDLLNGPGESYAVTLTEKGT 147
Cdd:cd04220     2 VTVGVGMN-GGFAFDPAAIRVSPGTTVTWEWTGeGGGHNVVAYEDPITAF--------DSGSTDSSEGETYEHTFEETGE 72

                          90       100
                  ....*....|....*....|
gi 1895870110 148 YSFYCSPHAGAGMVGKVTVN 167
Cdd:cd04220    73 YRYVCVPHEALGMKGAIVVE 92

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. 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. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  78 GGLVFQPSTFSVASGE--KIVFKNNAGFPHNVI---FDEDEVPSGVDVSKISMSDEDLlnGPGESYAVTLTEK--GTYSF 150
Cdd:cd00920    16 GVLLFGPPVLVVPVGDtvRVQFVNKLGENHSVTiagFGVPVVAMAGGANPGLVNTLVI--GPGESAEVTFTTDqaGVYWF 93

                          90
                  ....*....|....*..
gi 1895870110 151 YCSP--HAGAGMVGKVT 165
Cdd:cd00920    94 YCTIpgHNHAGMVGTIN 110

Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has been identified as an electron donor to the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. It has been shown that pseudoazurin dramatically enhances the reaction profile of nitrite reduction by Paracoccus pantotrophus cytochrome cd1 and facilitates release of the product nitric oxide. The ability of this small redox protein to interact with a multitude of structurally different partners has been attributed to the hydrophobic character of the binding surface.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  68 AVEVLLGADDGGLVFQPSTFSVASGEKIVFKNNAGfPHNVIFDEDEVPSGVD--VSKIsmsdedllngpGESYAVTLTEK 145
Cdd:cd04218     3 EVKMLNKGAGGAMVFEPAFLRAEPGDTVTFVPTDK-SHNAASIKGMLPEGAEpfKGKI-----------NEEITVTFEKE 70

                          90       100
                  ....*....|....*....|.
gi 1895870110 146 GTYSFYCSPHAGAGMVGKVTV 166
Cdd:cd04218    71 GVYGYKCTPHYGMGMVGLIQV 91

Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as a tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1895870110 133 GPGESYAVT-----LTEKGTYSFYCS-PHAGAGMVGKVTV 166
Cdd:cd13922    86 GGGESDSVTftvskLAAGGDYTFFCSfPGHYAMMKGKLVV 125

Phytocyanins are plant blue or type I copper proteins; Phytocyanins are plant blue or type I copper proteins. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Phytocyanins are classified into four groups: stellacyanin, plantacyanin, uclacyanin and early nodulin groups. Stellacyanin appears to be associated with the plant cell wall; it may be involved in oxidative reactions to build polymeric material making up the cell wall. Plantacyanin is shown to play a role in reproduction in Arabidopsis. Plantacyanins may also be stress-related proteins and may be involved in plant defense responses. The early nodulin-like protein (OsENODL1) from Oryza sativa is expressed specifically at the late developmental stage of the seeds.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895870110  86 TFSVasGEKIVFKNNAGFpHNVIfdedEVPSGvDVSKISMSDEDLLNGPGeSYAVTLTEKGTYSFYCSP--HAGAGMvgK 163
Cdd:cd04216    25 TFRV--GDSLVFNYNAGA-HSVV----EVNEA-DYDSCDTSNPINTYTSG-NDSVTLTKPGTRYFICGVpgHCQSGM--K 93

                  ....
gi 1895870110 164 VTVN 167
Cdd:cd04216    94 LAIN 97