NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6435666|pdb|1BYO|B]
View 

Chain B, PROTEIN (PLASTOCYANIN)

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
1-99 6.21e-49

Copper binding proteins, plastocyanin/azurin family;


:

Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 150.21  E-value: 6.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B         1 AEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKISMPEEDLLNAPGEEYSVTLTEKGTY 80
Cdd:pfam00127  1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                         90
                 ....*....|....*....
1BYO_B        81 KFYCAPHAGAGMVGKVTVN 99
Cdd:pfam00127 81 GFFCTPHQGAGMVGKVTVE 99
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
1-99 6.21e-49

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 150.21  E-value: 6.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B         1 AEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKISMPEEDLLNAPGEEYSVTLTEKGTY 80
Cdd:pfam00127  1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                         90
                 ....*....|....*....
1BYO_B        81 KFYCAPHAGAGMVGKVTVN 99
Cdd:pfam00127 81 GFFCTPHQGAGMVGKVTVE 99
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 1-99 3.78e-48

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]


Pssm-ID: 274247 [Multi-domain]  Cd Length: 99  Bit Score: 148.42  E-value: 3.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B         1 AEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKISMPEEDLLNAPGEEYSVTLTEKGTY 80
Cdd:TIGR02656  1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                         90
                 ....*....|....*....
1BYO_B        81 KFYCAPHAGAGMVGKVTVN 99
Cdd:TIGR02656 81 TFYCEPHRGAGMVGKITVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 1-99 1.38e-47

Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to PSI; Plastocyanin is a small copper-containing protein found in cyanobacteria, higher plants, and some algae, where it plays a role in photosynthesis. The two photosystems that are primarily responsible for photosynthesis are photosystem I (PSI) and photosystem II (PSII). The flow of electrons begins in PSII, which acts as a proton pump. Plastocyanin is responsible for transporting electrons from PSII to PSI.


Pssm-ID: 259881 [Multi-domain]  Cd Length: 97  Bit Score: 146.75  E-value: 1.38e-47
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B       1 AEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKISMpeEDLLNAPGEEYSVTLTEKGTY 80
Cdd:cd04219  1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                       90
               ....*....|....*....
1BYO_B      81 KFYCAPHAGAGMVGKVTVN 99
Cdd:cd04219 79 TFYCEPHRGAGMVGKITVQ 97
PetE COG3794
Plastocyanin [Energy production and conversion];
12-98 1.01e-18

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 73.11  E-value: 1.01e-18
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B      12 LAFVPSDLSIASGEKITFKNNAGFPHNdlfdedevpagvdVTKISMPEEDL---LNAPGEEYSVTLTEKGTYKFYCAPHa 88
Cdd:COG3794  1 MAFEPATLTVKPGDTVTWVNTDSVPHN-------------VTSDDGPDGAFdsgLLAPGETFSVTFDEPGTYDYYCTPH- 66

                       90
               ....*....|
1BYO_B      89 gAGMVGKVTV 98
Cdd:COG3794 67 -PWMVGTIVV 75
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
1-99 6.21e-49

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 150.21  E-value: 6.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B         1 AEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKISMPEEDLLNAPGEEYSVTLTEKGTY 80
Cdd:pfam00127  1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                         90
                 ....*....|....*....
1BYO_B        81 KFYCAPHAGAGMVGKVTVN 99
Cdd:pfam00127 81 GFFCTPHQGAGMVGKVTVE 99
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 1-99 3.78e-48

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]


Pssm-ID: 274247 [Multi-domain]  Cd Length: 99  Bit Score: 148.42  E-value: 3.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B         1 AEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKISMPEEDLLNAPGEEYSVTLTEKGTY 80
Cdd:TIGR02656  1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                         90
                 ....*....|....*....
1BYO_B        81 KFYCAPHAGAGMVGKVTVN 99
Cdd:TIGR02656 81 TFYCEPHRGAGMVGKITVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 1-99 1.38e-47

Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to PSI; Plastocyanin is a small copper-containing protein found in cyanobacteria, higher plants, and some algae, where it plays a role in photosynthesis. The two photosystems that are primarily responsible for photosynthesis are photosystem I (PSI) and photosystem II (PSII). The flow of electrons begins in PSII, which acts as a proton pump. Plastocyanin is responsible for transporting electrons from PSII to PSI.


Pssm-ID: 259881 [Multi-domain]  Cd Length: 97  Bit Score: 146.75  E-value: 1.38e-47
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B       1 AEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKISMpeEDLLNAPGEEYSVTLTEKGTY 80
Cdd:cd04219  1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                       90
               ....*....|....*....
1BYO_B      81 KFYCAPHAGAGMVGKVTVN 99
Cdd:cd04219 79 TFYCEPHRGAGMVGKITVQ 97
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 2-97 9.23e-29

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.


Pssm-ID: 259867 [Multi-domain]  Cd Length: 92  Bit Score: 99.18  E-value: 9.23e-29
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B       2 EVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTKismpeEDLLNAPGEEYSVTLTEKGTYK 81
Cdd:cd04204  2 VVKMGADNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPDGDAEFE-----SDRVDEEGFTYEQTFDEPGVYG 76

                       90
               ....*....|....*.
1BYO_B      82 FYCAPHAGAGMVGKVT 97
Cdd:cd04204 77 YYCTPHRGAGMVGTVI 92
PetE COG3794
Plastocyanin [Energy production and conversion];
12-98 1.01e-18

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 73.11  E-value: 1.01e-18
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B      12 LAFVPSDLSIASGEKITFKNNAGFPHNdlfdedevpagvdVTKISMPEEDL---LNAPGEEYSVTLTEKGTYKFYCAPHa 88
Cdd:COG3794  1 MAFEPATLTVKPGDTVTWVNTDSVPHN-------------VTSDDGPDGAFdsgLLAPGETFSVTFDEPGTYDYYCTPH- 66

                       90
               ....*....|
1BYO_B      89 gAGMVGKVTV 98
Cdd:COG3794 67 -PWMVGTIVV 75
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 8-99 2.66e-14

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.


Pssm-ID: 259882 [Multi-domain]  Cd Length: 92  Bit Score: 62.40  E-value: 2.66e-14
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B       8 SDGGLAFVPSDLSIASGEKITFKNNA-GFPHNDLFDEDEVPAGVDvtkismpeEDLLNAPGEEYSVTLTEKGTYKFYCAP 86
Cdd:cd04220  8 MNGGFAFDPAAIRVSPGTTVTWEWTGeGGGHNVVAYEDPITAFDS--------GSTDSSEGETYEHTFEETGEYRYVCVP 79

                       90
               ....*....|...
1BYO_B      87 HAGAGMVGKVTVN 99
Cdd:cd04220 80 HEALGMKGAIVVE 92
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 11-98 9.28e-14

Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i.


Pssm-ID: 259988 [Multi-domain]  Cd Length: 81  Bit Score: 60.80  E-value: 9.28e-14
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B      11 GLAFVPSDLSIASGEKITFKNNAGFPHNdlfdedevpagvdVTKISMPEEDLLNAPGEEYSVTLTEKGTYKFYCAPHagA 90
Cdd:cd13921  8 DFKFNPAEVTVKVGDTVTWTNKDSVPHT-------------VTAEDGAFDSGMLATGKSFSYTFTAAGTYDYFCTIH--P 72


               ....*...
1BYO_B      91 GMVGKVTV 98
Cdd:cd13921 73 FMKGTVTV 80
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 6-97 7.19e-11

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.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 54.16  E-value: 7.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B        6 GSSDGGLAFVPSDLSIASGE--KITFKNNAGFPHN---DLFDEDEVPAGVDVTKISMPeeDLLNAPGEEYSVTLTEK--G 78
Cdd:cd00920  12 FTYNGVLLFGPPVLVVPVGDtvRVQFVNKLGENHSvtiAGFGVPVVAMAGGANPGLVN--TLVIGPGESAEVTFTTDqaG 89

                        90       100
                ....*....|....*....|.
1BYO_B       79 TYKFYC--APHAGAGMVGKVT 97
Cdd:cd00920  90 VYWFYCtiPGHNHAGMVGTIN 110
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 2-98 1.12e-10

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.


Pssm-ID: 259880 [Multi-domain]  Cd Length: 117  Bit Score: 53.84  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B        2 EVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGfPHNDLFDEDEVPAGVDVTKISMpeedllnapGEEYSVTLTEKGTYK 81
Cdd:cd04218   5 KMLNKGAGGAMVFEPAFLRAEPGDTVTFVPTDK-SHNAASIKGMLPEGAEPFKGKI---------NEEITVTFEKEGVYG 74

                        90
                ....*....|....*..
1BYO_B       82 FYCAPHAGAGMVGKVTV 98
Cdd:cd04218  75 YKCTPHYGMGMVGLIQV 91
pseudoazurin TIGR02375
pseudoazurin; Pseudoazurin, also called cupredoxin, is a small, blue periplasmic protein with ...
 7-98 3.11e-09

pseudoazurin; Pseudoazurin, also called cupredoxin, is a small, blue periplasmic protein with a single bound copper atom. Pseudoazurin is related plastocyanins. Several examples of pseudoazurin are encoded by a neighboring gene for, or have been shown to transfer electrons to, copper-containing nitrite reductases (TIGR02376) of the same species. [Energy metabolism, Electron transport]


Pssm-ID: 131428  Cd Length: 116  Bit Score: 50.16  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B          7 SSDGGLAFVPSDLSIASGEKITF-KNNAGfpHNDLFDEDEVPAGVDVTKISMpeedllnapGEEYSVTLTEKGTYKFYCA 85
Cdd:TIGR02375   5 GAEGAMVFEPAYIRAAPGDTVTFvPTDKG--HNVETIKGMIPEGAEAFKSKI---------NEEYTVTLTKEGVYGVKCT 73

                          90
                  ....*....|...
1BYO_B         86 PHAGAGMVGKVTV 98
Cdd:TIGR02375  74 PHYGMGMVGLIQV 86
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 2-98 4.78e-08

Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.


Pssm-ID: 259895 [Multi-domain]  Cd Length: 121  Bit Score: 46.86  E-value: 4.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B        2 EVLLGSSDGGLAFVPSDLSIASGEK--ITFKNNAGFPHN---------------------DLFDEDEVPAGVDV---TKI 55
Cdd:cd04233   3 TITIKAVPGELKFDKTRLTVKAGSKvtLTFENPDDMPHNlvivkpgslekvgeaalamgaDGPAKNYVPDSPDVlaaTPL 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1BYO_B       56 SmpeedllnAPGEEYSVTLT---EKGTYKFYCA-PHAGAGMVGKVTV 98
Cdd:cd04233  83 V--------NPGETETLTFTaptEPGTYPYVCTyPGHWAIMKGVLIV 121
Cupredoxin_like_1 cd04210
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 3-98 1.24e-04

Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins because they have 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. Majority of family members contain multiple cupredoxin domain repeats; ceruloplasmin and coagulation factors V/VIII have six repeats; Laccase, ascorbate oxidase, and 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.


Pssm-ID: 259872 [Multi-domain]  Cd Length: 111  Bit Score: 37.83  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B        3 VLLGSSDGGLAFVPSDLSIASGE--KITFKNNAGFPH----NDLFD---EDEVPAGVDVTKISMPEEDLLNAPGEEYSVT 73
Cdd:cd04210   5 ISLGNAANALRFFPDQLEFEAGKryKLHLHNPSQLKHyftaKDFADaiwTRKVDAGGVEIKGAIRELELKPGAEAEWQFV 84

                        90       100
                ....*....|....*....|....*..
1BYO_B       74 LTEKGTYKFYC--APHAGAGMVGKVTV 98
Cdd:cd04210  85 PLKTGKYDLRCtiPGHAEAGMTGQITI 111
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 2-98 2.09e-04

Cupredoxin-like domain; 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.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 37.18  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B          2 EVLLGSSDGGlaFVPSDLSIASGE--KITFKNNagfphndlfdeDEVPAGVDVTKISMpEEDLlnAPGEEYSVTLT--EK 77
Cdd:pfam13473  22 TVEITVKDGG--FSPSRITVPAGTpvKLEFKNK-----------DKTPAEFESPDLGI-EKVL--APGKTSTITIPplKP 85

                          90       100
                  ....*....|....*....|....*
1BYO_B         78 GTYKFYCaphagaGMV----GKVTV 98
Cdd:pfam13473  86 GEYDFFC------DMHmdakGKLIV 104
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 14-98 2.31e-04

Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins because they have 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. Majority of family members contain multiple cupredoxin domain repeats; ceruloplasmin and coagulation factors V/VIII have six repeats; Laccase, ascorbate oxidase, and 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.


Pssm-ID: 259873 [Multi-domain]  Cd Length: 110  Bit Score: 37.27  E-value: 2.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B       14 FVPSDLSIASGEKITF--KNNAGFPHN-DLFDEDEVPAGVDVTKiSMP--EEDLLN----APGEEYSV--TLTEKGTYKF 82
Cdd:cd04211  14 FTPDSIQVKQGETVRFvvTNNGKIPHEfVIGTAAELKEHAEMMR-KHPgmEHDEPNmvslAPGKSGEIvwTFTKAGTFEF 92

                        90
                ....*....|....*...
1BYO_B       83 YC--APHAGAGMVGKVTV 98
Cdd:cd04211  93 ACliPGHYEAGMVGKVTV 110
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 32-98 5.51e-04

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 36.23  E-value: 5.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BYO_B       32 NAGFPHNDLFDEDE--VPAGVDVTkISMPEEDLLNA-------------PGEEYSV--TLTEKGTYKFYCAPHAGAG--- 91
Cdd:cd13914  13 EFSYPEANVTTSEQlvIPADRPVY-FRITSRDVIHAfhvpelglkqdafPGQYNTIktEATEEGEYQLYCAEYCGAGhsq 91


                ....*..
1BYO_B       92 MVGKVTV 98
Cdd:cd13914  92 MLSTVTV 98
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 41-96 8.09e-03

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 32.65  E-value: 8.09e-03
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1BYO_B      41 FDEDEVPAGVDVTkISMPEEDLLNA-------------PGEEYSVTLT--EKGTYKFYCAPHAGAG---MVGKV 96
Cdd:cd13842 22 PNEIVVPAGTPVR-FRVTSPDVIHGfyipnlgvkvdavPGYTSELWFVadKPGTYTIICAEYCGLGhsyMLGKV 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH