NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1585653129|ref|XP_028056053|]
View 

plastocyanin [Camellia sinensis]

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;
72-170 2.38e-51

Copper binding proteins, plastocyanin/azurin family;


:

Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 159.46  E-value: 2.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDATKISMSDEDLLNAPGETYAVTLTEKGSY 151
Cdd:pfam00127   1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                          90
                  ....*....|....*....
gi 1585653129 152 GFYCTPHQGAGMVGKVTVN 170
Cdd:pfam00127  81 GFFCTPHQGAGMVGKVTVE 99
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
72-170 2.38e-51

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 159.46  E-value: 2.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDATKISMSDEDLLNAPGETYAVTLTEKGSY 151
Cdd:pfam00127   1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                          90
                  ....*....|....*....
gi 1585653129 152 GFYCTPHQGAGMVGKVTVN 170
Cdd:pfam00127  81 GFFCTPHQGAGMVGKVTVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 72-170 4.81e-51

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: 158.69  E-value: 4.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDATKISMsdEDLLNAPGETYAVTLTEKGSY 151
Cdd:cd04219     1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                          90
                  ....*....|....*....
gi 1585653129 152 GFYCTPHQGAGMVGKVTVN 170
Cdd:cd04219    79 TFYCEPHRGAGMVGKITVQ 97
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 72-170 3.74e-50

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: 156.51  E-value: 3.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDATKISMSDEDLLNAPGETYAVTLTEKGSY 151
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1585653129 152 GFYCTPHQGAGMVGKVTVN 170
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99
PetE COG3794
Plastocyanin [Energy production and conversion];
83-169 1.02e-19

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 78.11  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  83 LVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDevPSGVDATKISmsdedllnAPGETYAVTLTEKGSYGFYCTPHqgAG 162
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDG--PDGAFDSGLL--------APGETFSVTFDEPGTYDYYCTPH--PW 68


                  ....*..
gi 1585653129 163 MVGKVTV 169
Cdd:COG3794    69 MVGTIVV 75
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
72-170 2.38e-51

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 159.46  E-value: 2.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDATKISMSDEDLLNAPGETYAVTLTEKGSY 151
Cdd:pfam00127   1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                          90
                  ....*....|....*....
gi 1585653129 152 GFYCTPHQGAGMVGKVTVN 170
Cdd:pfam00127  81 GFFCTPHQGAGMVGKVTVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 72-170 4.81e-51

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: 158.69  E-value: 4.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDATKISMsdEDLLNAPGETYAVTLTEKGSY 151
Cdd:cd04219     1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                          90
                  ....*....|....*....
gi 1585653129 152 GFYCTPHQGAGMVGKVTVN 170
Cdd:cd04219    79 TFYCEPHRGAGMVGKITVQ 97
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 72-170 3.74e-50

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: 156.51  E-value: 3.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDATKISMSDEDLLNAPGETYAVTLTEKGSY 151
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1585653129 152 GFYCTPHQGAGMVGKVTVN 170
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 72-168 5.09e-33

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: 112.66  E-value: 5.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDEVPSGVDAtkismSDEDLLNAPGETYAVTLTEKGSY 151
Cdd:cd04204     1 VVVKMGADNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPDGDAE-----FESDRVDEEGFTYEQTFDEPGVY 75

                          90
                  ....*....|....*..
gi 1585653129 152 GFYCTPHQGAGMVGKVT 168
Cdd:cd04204    76 GYYCTPHRGAGMVGTVI 92
PetE COG3794
Plastocyanin [Energy production and conversion];
83-169 1.02e-19

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 78.11  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  83 LVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDevPSGVDATKISmsdedllnAPGETYAVTLTEKGSYGFYCTPHqgAG 162
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDG--PDGAFDSGLL--------APGETFSVTFDEPGTYDYYCTPH--PW 68


                  ....*..
gi 1585653129 163 MVGKVTV 169
Cdd:COG3794    69 MVGTIVV 75
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 79-170 5.27e-16

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: 68.95  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  79 SDGGLVFEPSSFSVAAGEKIVFKNNA-GFPHNVVFDEDEVPSGVDATKISmsdedllnAPGETYAVTLTEKGSYGFYCTP 157
Cdd:cd04220     8 MNGGFAFDPAAIRVSPGTTVTWEWTGeGGGHNVVAYEDPITAFDSGSTDS--------SEGETYEHTFEETGEYRYVCVP 79

                          90
                  ....*....|...
gi 1585653129 158 HQGAGMVGKVTVN 170
Cdd:cd04220    80 HEALGMKGAIVVE 92
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 82-169 3.74e-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: 63.89  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  82 GLVFEPSSFSVAAGEKIVFKNNAGFPHNVVFDEDevpsgvdatkiSMSDEDLlnAPGETYAVTLTEKGSYGFYCTPHqgA 161
Cdd:cd13921     8 DFKFNPAEVTVKVGDTVTWTNKDSVPHTVTAEDG-----------AFDSGML--ATGKSFSYTFTAAGTYDYFCTIH--P 72


                  ....*...
gi 1585653129 162 GMVGKVTV 169
Cdd:cd13921    73 FMKGTVTV 80
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 77-168 3.63e-13

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: 62.25  E-value: 3.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  77 GSSDGGLVFEPSSFSVAAGE--KIVFKNNAGFPHNVV---FDEDEVPSGVDATKISMSDEDLlnAPGETYAVTLTEK--G 149
Cdd:cd00920    12 FTYNGVLLFGPPVLVVPVGDtvRVQFVNKLGENHSVTiagFGVPVVAMAGGANPGLVNTLVI--GPGESAEVTFTTDqaG 89

                          90       100
                  ....*....|....*....|.
gi 1585653129 150 SYGFYCTP--HQGAGMVGKVT 168
Cdd:cd00920    90 VYWFYCTIpgHNHAGMVGTIN 110
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 71-169 7.77e-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: 59.18  E-value: 7.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  71 AIEVLLGSSDGGLVFEPSSFSVAAGEK--IVFKNNAGFPHNVVF----DEDEV--------PSGVDATKISMSDE----- 131
Cdd:cd04233     1 ATTITIKAVPGELKFDKTRLTVKAGSKvtLTFENPDDMPHNLVIvkpgSLEKVgeaalamgADGPAKNYVPDSPDvlaat 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1585653129 132 DLLNaPGETYAVTLT---EKGSYGFYCT-PHQGAGMVGKVTV 169
Cdd:cd04233    81 PLVN-PGETETLTFTaptEPGTYPYVCTyPGHWAIMKGVLIV 121
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 71-169 4.85e-11

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: 56.92  E-value: 4.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  71 AIEVLLGSSDGGLVFEPSSFSVAAGEKIVFKNNAGfPHNVVFDEDEVPSGVDATKISMSDEdllnapgetYAVTLTEKGS 150
Cdd:cd04218     3 EVKMLNKGAGGAMVFEPAFLRAEPGDTVTFVPTDK-SHNAASIKGMLPEGAEPFKGKINEE---------ITVTFEKEGV 72

                          90
                  ....*....|....*....
gi 1585653129 151 YGFYCTPHQGAGMVGKVTV 169
Cdd:cd04218    73 YGYKCTPHYGMGMVGLIQV 91
pseudoazurin TIGR02375
pseudoazurin; Pseudoazurin, also called cupredoxin, is a small, blue periplasmic protein with ...
 78-169 4.90e-11

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: 56.71  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  78 SSDGGLVFEPSSFSVAAGEKIVF-KNNAGfpHNVVFDEDEVPSGVDATKISMsdedllnapGETYAVTLTEKGSYGFYCT 156
Cdd:TIGR02375   5 GAEGAMVFEPAYIRAAPGDTVTFvPTDKG--HNVETIKGMIPEGAEAFKSKI---------NEEYTVTLTKEGVYGVKCT 73

                          90
                  ....*....|...
gi 1585653129 157 PHQGAGMVGKVTV 169
Cdd:TIGR02375  74 PHYGMGMVGLIQV 86
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 72-170 1.84e-08

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 50.73  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  72 IEVLLGSSdggLVFEPSSFSVAAGE--KIVFKNNAGFPHNVVFDEdevPSGVDATKISMS----------DEDLLnAPGE 139
Cdd:COG4454    44 ITVTMGDT---MRFTPDSIEVKAGEtvRFVVTNPGKLKHEFVLGT---FAELAEHAKVMAkmpdmehgdpNEVEL-APGE 116

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1585653129 140 TYAVTLT--EKGSYGFYCT-P-HQGAGMVGKVTVN 170
Cdd:COG4454   117 TGELVWTftKAGTFEFACLiPgHYEAGMTGKIVVK 151
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 73-169 2.15e-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: 38.72  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  73 EVLLGSSDGGlvFEPSSFSVAAGE--KIVFKNNAGFPHNVVFDEDEVpsgvdatkismsDEDLlnAPGETYAVTLT--EK 148
Cdd:pfam13473  22 TVEITVKDGG--FSPSRITVPAGTpvKLEFKNKDKTPAEFESPDLGI------------EKVL--APGKTSTITIPplKP 85

                          90       100
                  ....*....|....*....|.
gi 1585653129 149 GSYGFYCTPHQgaGMVGKVTV 169
Cdd:pfam13473  86 GEYDFFCDMHM--DAKGKLIV 104
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 85-169 1.16e-03

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: 36.89  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585653129  85 FEPSSFSVAAGEKIVF--KNNAGFPHNVVFDEDEvpsGVDATKISMSDEDLLN---------APGETYAV--TLTEKGSY 151
Cdd:cd04211    14 FTPDSIQVKQGETVRFvvTNNGKIPHEFVIGTAA---ELKEHAEMMRKHPGMEhdepnmvslAPGKSGEIvwTFTKAGTF 90

                          90       100
                  ....*....|....*....|
gi 1585653129 152 GFYC-TP-HQGAGMVGKVTV 169
Cdd:cd04211    91 EFAClIPgHYEAGMVGKVTV 110
 
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