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Conserved domains on  [gi|262118413]
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Chain B, Plastocyanin

Protein Classification

similar to plastocyanin( domain architecture ID 10798394)

protein similar to plastocyanin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 4-105 4.29e-58

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: 173.84  E-value: 4.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413    4 FTVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDKQVPGASKELADKLSHSQLMFSPGESYEITFSSdfpA 83
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFST---P 77

                          90       100
                  ....*....|....*....|..
gi 262118413   84 GTYTYYCAPHRGAGMVGKITVE 105
Cdd:TIGR02656  78 GTYTFYCEPHRGAGMVGKITVE 99
 
Name Accession Description Interval E-value
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 4-105 4.29e-58

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: 173.84  E-value: 4.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413    4 FTVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDKQVPGASKELADKLSHSQLMFSPGESYEITFSSdfpA 83
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFST---P 77

                          90       100
                  ....*....|....*....|..
gi 262118413   84 GTYTYYCAPHRGAGMVGKITVE 105
Cdd:TIGR02656  78 GTYTFYCEPHRGAGMVGKITVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 5-105 8.94e-49

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: 150.21  E-value: 8.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   5 TVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDkqVPGASKELADKLSHSQLMFSPGESYEITFSSdfpAG 84
Cdd:cd04219    2 TVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDE--DAVPSAVDAAALSHKDLLNAPGETFSVTFPA---PG 76

                         90       100
                 ....*....|....*....|.
gi 262118413  85 TYTYYCAPHRGAGMVGKITVE 105
Cdd:cd04219   77 TYTFYCEPHRGAGMVGKITVQ 97
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
5-105 1.63e-36

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 119.40  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413    5 TVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDKQVPGASKELADKLSHSQLMFSPGESYEITFSsdfPAG 84
Cdd:pfam00127   2 EVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFD---LAG 78

                          90       100
                  ....*....|....*....|.
gi 262118413   85 TYTYYCAPHRGAGMVGKITVE 105
Cdd:pfam00127  79 TYGFFCTPHQGAGMVGKVTVE 99
PetE COG3794
Plastocyanin [Energy production and conversion];
15-105 2.57e-24

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 87.74  E-value: 2.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  15 LQFEPANVTVHPGDTVKWVNNKLPPHNILFDDkqvpGASKELADKlshsqlMFSPGESYEITFSSdfpAGTYTYYCAPHR 94
Cdd:COG3794    1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDD----GPDGAFDSG------LLAPGETFSVTFDE---PGTYDYYCTPHP 67

                         90
                 ....*....|.
gi 262118413  95 gaGMVGKITVE 105
Cdd:COG3794   68 --WMVGTIVVG 76
 
Name Accession Description Interval E-value
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 4-105 4.29e-58

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: 173.84  E-value: 4.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413    4 FTVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDKQVPGASKELADKLSHSQLMFSPGESYEITFSSdfpA 83
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFST---P 77

                          90       100
                  ....*....|....*....|..
gi 262118413   84 GTYTYYCAPHRGAGMVGKITVE 105
Cdd:TIGR02656  78 GTYTFYCEPHRGAGMVGKITVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 5-105 8.94e-49

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: 150.21  E-value: 8.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   5 TVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDkqVPGASKELADKLSHSQLMFSPGESYEITFSSdfpAG 84
Cdd:cd04219    2 TVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDE--DAVPSAVDAAALSHKDLLNAPGETFSVTFPA---PG 76

                         90       100
                 ....*....|....*....|.
gi 262118413  85 TYTYYCAPHRGAGMVGKITVE 105
Cdd:cd04219   77 TYTFYCEPHRGAGMVGKITVQ 97
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
5-105 1.63e-36

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 119.40  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413    5 TVKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDKQVPGASKELADKLSHSQLMFSPGESYEITFSsdfPAG 84
Cdd:pfam00127   2 EVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFD---LAG 78

                          90       100
                  ....*....|....*....|.
gi 262118413   85 TYTYYCAPHRGAGMVGKITVE 105
Cdd:pfam00127  79 TYGFFCTPHQGAGMVGKVTVE 99
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 6-103 2.76e-30

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: 103.42  E-value: 2.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   6 VKMGADSGLLQFEPANVTVHPGDTVKWVNNKLPPHNILFDDKQVPGaskelADKLSHSQLMFSPGESYEITFSSdfpAGT 85
Cdd:cd04204    3 VKMGADNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPD-----GDAEFESDRVDEEGFTYEQTFDE---PGV 74

                         90
                 ....*....|....*...
gi 262118413  86 YTYYCAPHRGAGMVGKIT 103
Cdd:cd04204   75 YGYYCTPHRGAGMVGTVI 92
PetE COG3794
Plastocyanin [Energy production and conversion];
15-105 2.57e-24

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 87.74  E-value: 2.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  15 LQFEPANVTVHPGDTVKWVNNKLPPHNILFDDkqvpGASKELADKlshsqlMFSPGESYEITFSSdfpAGTYTYYCAPHR 94
Cdd:COG3794    1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDD----GPDGAFDSG------LLAPGETFSVTFDE---PGTYDYYCTPHP 67

                         90
                 ....*....|.
gi 262118413  95 gaGMVGKITVE 105
Cdd:COG3794   68 --WMVGTIVVG 76
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 3-105 3.05e-20

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: 77.81  E-value: 3.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   3 TFTVKMGADsGLLQFEPANVTVHPGDTVKWVNN-KLPPHNILF-DDKQVPGASKELADklshsqlmfSPGESYEITFSSd 80
Cdd:cd04220    1 TVTVGVGMN-GGFAFDPAAIRVSPGTTVTWEWTgEGGGHNVVAyEDPITAFDSGSTDS---------SEGETYEHTFEE- 69

                         90       100
                 ....*....|....*....|....*
gi 262118413  81 fpAGTYTYYCAPHRGAGMVGKITVE 105
Cdd:cd04220   70 --TGEYRYVCVPHEALGMKGAIVVE 92
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 15-105 6.62e-19

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: 73.90  E-value: 6.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  15 LQFEPANVTVHPGDTVKWVNNKLPPHNILFDDKQvpGASKELAdklshsqlmfsPGESYEITFSSdfpAGTYTYYCAPHr 94
Cdd:cd13921    9 FKFNPAEVTVKVGDTVTWTNKDSVPHTVTAEDGA--FDSGMLA-----------TGKSFSYTFTA---AGTYDYFCTIH- 71

                         90
                 ....*....|.
gi 262118413  95 gAGMVGKITVE 105
Cdd:cd13921   72 -PFMKGTVTVE 81
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 17-103 6.86e-15

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: 64.56  E-value: 6.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  17 FEPANVTVHPGDTVKW--VNNKLPPHNILFDDKQVPG-ASKELADKLSHSQLMFSPGESYEITFSSDFPaGTYTYYC--A 91
Cdd:cd00920   20 FGPPVLVVPVGDTVRVqfVNKLGENHSVTIAGFGVPVvAMAGGANPGLVNTLVIGPGESAEVTFTTDQA-GVYWFYCtiP 98

                         90
                 ....*....|..
gi 262118413  92 PHRGAGMVGKIT 103
Cdd:cd00920   99 GHNHAGMVGTIN 110
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 3-104 9.43e-14

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: 61.93  E-value: 9.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   3 TFTVKM--GADSGLLQFEPANVTVHPGDTVKWVNnKLPPHNILFDDKQVPGASKELADKLshsqlmfspGESYEITFSSD 80
Cdd:cd04218    1 EHEVKMlnKGAGGAMVFEPAFLRAEPGDTVTFVP-TDKSHNAASIKGMLPEGAEPFKGKI---------NEEITVTFEKE 70

                         90       100
                 ....*....|....*....|....
gi 262118413  81 fpaGTYTYYCAPHRGAGMVGKITV 104
Cdd:cd04218   71 ---GVYGYKCTPHYGMGMVGLIQV 91
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 5-104 8.44e-12

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: 56.87  E-value: 8.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   5 TVKMGADSGLLQFEPANVTVHPGDTVKWV--NNKLPPHNILFDDkqvPGASKELADK--------------------LSH 62
Cdd:cd04233    3 TITIKAVPGELKFDKTRLTVKAGSKVTLTfeNPDDMPHNLVIVK---PGSLEKVGEAalamgadgpaknyvpdspdvLAA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 262118413  63 SQLMfSPGESYEITFSSDFPAGTYTYYCA-PHRGAGMVGKITV 104
Cdd:cd04233   80 TPLV-NPGETETLTFTAPTEPGTYPYVCTyPGHWAIMKGVLIV 121
pseudoazurin TIGR02375
pseudoazurin; Pseudoazurin, also called cupredoxin, is a small, blue periplasmic protein with ...
 12-104 3.97e-10

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: 52.47  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   12 SGLLQFEPANVTVHPGDTVKWVNNKlPPHNILFDDKQVPGASKELADKLshsqlmfspGESYEITFSSDfpaGTYTYYCA 91
Cdd:TIGR02375   7 EGAMVFEPAYIRAAPGDTVTFVPTD-KGHNVETIKGMIPEGAEAFKSKI---------NEEYTVTLTKE---GVYGVKCT 73

                          90
                  ....*....|...
gi 262118413   92 PHRGAGMVGKITV 104
Cdd:TIGR02375  74 PHYGMGMVGLIQV 86
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 17-104 1.27e-08

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: 48.45  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  17 FEPANVTVHPGDTVKWV--NNKLPPHNILFDDKQVPGASKEL---ADKLSHSQ---LMFSPGESYEI--TFSSdfpAGTY 86
Cdd:cd04211   14 FTPDSIQVKQGETVRFVvtNNGKIPHEFVIGTAAELKEHAEMmrkHPGMEHDEpnmVSLAPGKSGEIvwTFTK---AGTF 90

                         90       100
                 ....*....|....*....|
gi 262118413  87 TYYC--APHRGAGMVGKITV 104
Cdd:cd04211   91 EFACliPGHYEAGMVGKVTV 110
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 3-105 3.93e-08

Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction only];


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 48.03  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   3 TFTVKMGADsglLQFEPANVTVHPGDTVKWV-NNKLP-PHNIlfddkqvpgASKELADKLSHSQLM-------------- 66
Cdd:COG4454   43 TITVTMGDT---MRFTPDSIEVKAGETVRFVvTNPGKlKHEF---------VLGTFAELAEHAKVMakmpdmehgdpnev 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 262118413  67 -FSPGESYEITFSsdFP-AGTYTYYC--APHRGAGMVGKITVE 105
Cdd:COG4454  111 eLAPGETGELVWT--FTkAGTFEFACliPGHYEAGMTGKIVVK 151
BlueCu COG3241
Azurin [Energy production and conversion];
5-105 1.14e-06

Azurin [Energy production and conversion];


Pssm-ID: 442473 [Multi-domain]  Cd Length: 158  Bit Score: 44.13  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413   5 TVKMGADSGLlQFEPANVTVHPGDTVKWV---NNKLP----PHNILF---DDKQVPGASKELADK------------LSH 62
Cdd:COG3241   36 EITIEANDAM-KFDKKEITVKAGKEVTLTlknTGKLPkdamGHNWVLtkpGDDQAVGAAGAAAGAdnnyvppdddrvIAH 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 262118413  63 SQLMfSPGESYEITFSSDFPAGTYTYYCA-PHRGAGMVGKITVE 105
Cdd:COG3241  115 TKLI-GGGESDTITFTAPKEPGDYPFFCSfPGHWALMKGTLIVE 157
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 3-104 6.28e-06

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: 41.42  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413    3 TFTVKMGADsgllQFEPANVTVHPGD--TVKWVNNKLPPHNILFDDKqvpGASKELAdklshsqlmfsPGESYEITFSSD 80
Cdd:pfam13473  22 TVEITVKDG----GFSPSRITVPAGTpvKLEFKNKDKTPAEFESPDL---GIEKVLA-----------PGKTSTITIPPL 83

                          90       100
                  ....*....|....*....|....*...
gi 262118413   81 fPAGTYTYYCaphrgaGMV----GKITV 104
Cdd:pfam13473  84 -KPGEYDFFC------DMHmdakGKLIV 104
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 24-105 1.59e-05

The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 40.70  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  24 VHPGDTVK-WVNNKLPPHNILFDDKQVPGA----------------SKELADK-LSHsqlmFSPGES--YEITFSSDFPA 83
Cdd:cd13853   36 VRPGDTLRiTLKNDLPPEGAANEAPAPNTPhcpnttnlhfhglhvsPTGNSDNvFLT----IAPGESftYEYDIPADHPP 111

                         90       100       110
                 ....*....|....*....|....*....|
gi 262118413  84 GTYTYYcaPHR--------GAGMVGKITVE 105
Cdd:cd13853  112 GTYWYH--PHLhgstalqvAGGMAGALVVE 139
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 24-105 2.80e-05

Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles two domain nitrite reductase in both sequence homology and structure similarity. It consists of two domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of larger laccases.


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 39.78  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  24 VHPGDTVK--WVNNK--LPPHNILFDdkqvpGASKELADKLSHSqlmFSPGESYEITFSSdFPAGTYTYYCA-----PHR 94
Cdd:cd04201   37 VREGDTVElhFSNNPssTMPHNIDFH-----AATGAGGGAGATF---IAPGETSTFSFKA-TQPGLYVYHCAvapvpMHI 107

                         90
                 ....*....|.
gi 262118413  95 GAGMVGKITVE 105
Cdd:cd04201  108 ANGMYGLILVE 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 24-106 5.88e-05

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 40.30  E-value: 5.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  24 VHPGDTVK-WVNNKLPP------HNIlfddkQVPGASkelaDklSHSQLMFSPGESYEITFSSDFPAGTYTYYcaPHR-- 94
Cdd:COG2132   49 VREGDRVRvRVTNRLPEpttvhwHGL-----RVPNAM----D--GVPGDPIAPGETFTYEFPVPQPAGTYWYH--PHThg 115

                         90
                 ....*....|....*...
gi 262118413  95 ------GAGMVGKITVEG 106
Cdd:COG2132  116 staeqvYRGLAGALIVED 133
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 22-105 2.41e-04

Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 37.27  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  22 VTVHPGDTVKW-VNNKLP--PHNILFDDKQVPGASkeLAD-KLSHSQLMFSPGESYEITFSSDFPAGTYTYYCAPH--RG 95
Cdd:cd04206   33 IRVKEGDTVEVtVTNNLPnePTSIHWHGLRQPGTN--DGDgVAGLTQCPIPPGESFTYRFTVDDQAGTFWYHSHVGgqRA 110

                         90
                 ....*....|
gi 262118413  96 AGMVGKITVE 105
Cdd:cd04206  111 DGLYGPLIVE 120
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 34-104 9.85e-04

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.


Pssm-ID: 259989 [Multi-domain]  Cd Length: 125  Bit Score: 35.99  E-value: 9.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262118413  34 NNKLPPhnilfDDKQVPGASKeladklshsqlMFSPGESYEITF--SSDFPAGTYTYYCA-PHRGAGMVGKITV 104
Cdd:cd13922   68 NDYVPP-----GDARVIAHTK-----------LIGGGESDSVTFtvSKLAAGGDYTFFCSfPGHYAMMKGKLVV 125
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 16-105 2.88e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 34.13  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262118413  16 QFEPANVTVHPGDTVKWvnnklpphnILFDDKQVPGASKELADKLSHSQLMFSPGESYEITFSSDFPaGTYTYYC----- 90
Cdd:cd04223   12 HFTPDIIEVKEGDEVTV---------HLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKP-GVYPYYCtefcs 81

                         90
                 ....*....|....*
gi 262118413  91 APHRgaGMVGKITVE 105
Cdd:cd04223   82 ALHL--EMQGYLIVE 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.
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