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Conserved domains on  [gi|1572928001|gb|RZC14607|]
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Plastocyanin, chloroplastic [Glycine soja]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
67-165 3.38e-51

Copper binding proteins, plastocyanin/azurin family;


:

Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 158.69  E-value: 3.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMSDEDLLNAPGETYSVTLDAKGTY 146
Cdd:pfam00127   1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                          90
                  ....*....|....*....
gi 1572928001 147 SFFCSPHQGAGMVGKVTVN 165
Cdd:pfam00127  81 GFFCTPHQGAGMVGKVTVE 99
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
67-165 3.38e-51

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 158.69  E-value: 3.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMSDEDLLNAPGETYSVTLDAKGTY 146
Cdd:pfam00127   1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                          90
                  ....*....|....*....
gi 1572928001 147 SFFCSPHQGAGMVGKVTVN 165
Cdd:pfam00127  81 GFFCTPHQGAGMVGKVTVE 99
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 67-165 3.68e-51

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: 158.82  E-value: 3.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMSDEDLLNAPGETYSVTLDAKGTY 146
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1572928001 147 SFFCSPHQGAGMVGKVTVN 165
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 67-165 7.35e-50

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: 155.61  E-value: 7.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMsdEDLLNAPGETYSVTLDAKGTY 146
Cdd:cd04219     1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                          90
                  ....*....|....*....
gi 1572928001 147 SFFCSPHQGAGMVGKVTVN 165
Cdd:cd04219    79 TFYCEPHRGAGMVGKITVQ 97
PetE COG3794
Plastocyanin [Energy production and conversion];
78-164 1.30e-19

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 77.73  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  78 LAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDeiPSGVDAGKISmsdedllnAPGETYSVTLDAKGTYSFFCSPHqgAG 157
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDG--PDGAFDSGLL--------APGETFSVTFDEPGTYDYYCTPH--PW 68


                  ....*..
gi 1572928001 158 MVGKVTV 164
Cdd:COG3794    69 MVGTIVV 75
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
67-165 3.38e-51

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 158.69  E-value: 3.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMSDEDLLNAPGETYSVTLDAKGTY 146
Cdd:pfam00127   1 AEVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTY 80

                          90
                  ....*....|....*....
gi 1572928001 147 SFFCSPHQGAGMVGKVTVN 165
Cdd:pfam00127  81 GFFCTPHQGAGMVGKVTVE 99
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 67-165 3.68e-51

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: 158.82  E-value: 3.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMSDEDLLNAPGETYSVTLDAKGTY 146
Cdd:TIGR02656   1 VTVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1572928001 147 SFFCSPHQGAGMVGKVTVN 165
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 67-165 7.35e-50

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: 155.61  E-value: 7.35e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMsdEDLLNAPGETYSVTLDAKGTY 146
Cdd:cd04219     1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                          90
                  ....*....|....*....
gi 1572928001 147 SFFCSPHQGAGMVGKVTVN 165
Cdd:cd04219    79 TFYCEPHRGAGMVGKITVQ 97
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 67-163 4.83e-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: 104.96  E-value: 4.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGVDAgkismSDEDLLNAPGETYSVTLDAKGTY 146
Cdd:cd04204     1 VVVKMGADNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPDGDAE-----FESDRVDEEGFTYEQTFDEPGVY 75

                          90
                  ....*....|....*..
gi 1572928001 147 SFFCSPHQGAGMVGKVT 163
Cdd:cd04204    76 GYYCTPHRGAGMVGTVI 92
PetE COG3794
Plastocyanin [Energy production and conversion];
78-164 1.30e-19

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 77.73  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  78 LAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDeiPSGVDAGKISmsdedllnAPGETYSVTLDAKGTYSFFCSPHqgAG 157
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDG--PDGAFDSGLL--------APGETFSVTFDEPGTYDYYCTPH--PW 68


                  ....*..
gi 1572928001 158 MVGKVTV 164
Cdd:COG3794    69 MVGTIVV 75
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 73-165 1.35e-17

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: 73.19  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  73 GDDGSLAFVPNNFSVASGEKIVFKNNA-GFPHNVVFDEDEIPSGvDAGKISMSdedllnaPGETYSVTLDAKGTYSFFCS 151
Cdd:cd04220     7 GMNGGFAFDPAAIRVSPGTTVTWEWTGeGGGHNVVAYEDPITAF-DSGSTDSS-------EGETYEHTFEETGEYRYVCV 78

                          90
                  ....*....|....
gi 1572928001 152 PHQGAGMVGKVTVN 165
Cdd:cd04220    79 PHEALGMKGAIVVE 92
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 77-164 1.18e-12

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: 60.03  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  77 SLAFVPNNFSVASGEKIVFKNNAGFPHNVVFDEDEIPSGvdagkismsdedlLNAPGETYSVTLDAKGTYSFFCSPHqgA 156
Cdd:cd13921     8 DFKFNPAEVTVKVGDTVTWTNKDSVPHTVTAEDGAFDSG-------------MLATGKSFSYTFTAAGTYDYFCTIH--P 72


                  ....*...
gi 1572928001 157 GMVGKVTV 164
Cdd:cd13921    73 FMKGTVTV 80
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 72-163 1.39e-12

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: 60.71  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  72 GGDDGSLAFVPNNFSVASGE--KIVFKNNAGFPHNVV---FDEDEIPSGVDAGKISMSDEDLlnAPGETYSVTLDAK--G 144
Cdd:cd00920    12 FTYNGVLLFGPPVLVVPVGDtvRVQFVNKLGENHSVTiagFGVPVVAMAGGANPGLVNTLVI--GPGESAEVTFTTDqaG 89

                          90       100
                  ....*....|....*....|.
gi 1572928001 145 TYSFFCSP--HQGAGMVGKVT 163
Cdd:cd00920    90 VYWFYCTIpgHNHAGMVGTIN 110
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 66-164 7.14e-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: 58.80  E-value: 7.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  66 AIEVLLGGDDGSLAFVPNNFSVASGEK--IVFKNNAGFPHNVVF---DEDE---------IPSGVDAGKISMSDE----- 126
Cdd:cd04233     1 ATTITIKAVPGELKFDKTRLTVKAGSKvtLTFENPDDMPHNLVIvkpGSLEkvgeaalamGADGPAKNYVPDSPDvlaat 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1572928001 127 DLLNaPGETYSVTLDA---KGTYSFFCS-PHQGAGMVGKVTV 164
Cdd:cd04233    81 PLVN-PGETETLTFTAptePGTYPYVCTyPGHWAIMKGVLIV 121
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 66-164 1.25e-07

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: 47.68  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  66 AIEVLLGGDDGSLAFVPNNFSVASGEKIVFKNNAGfPHNVVFDEDEIPSGVDA--GKIsmsdedllnapGETYSVTLDAK 143
Cdd:cd04218     3 EVKMLNKGAGGAMVFEPAFLRAEPGDTVTFVPTDK-SHNAASIKGMLPEGAEPfkGKI-----------NEEITVTFEKE 70

                          90       100
                  ....*....|....*....|.
gi 1572928001 144 GTYSFFCSPHQGAGMVGKVTV 164
Cdd:cd04218    71 GVYGYKCTPHYGMGMVGLIQV 91
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 68-164 4.37e-05

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: 41.00  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  68 EVLLGGDDgSLAFVPNNFSVASGEK---IVFKNNAGFP-----HNVV---------FDEDEIPSGVDAGKISMSDEDLLN 130
Cdd:cd13922     2 EVTIEGND-QMKFDTKEITVKAGCKeftVTLKHTGKLPknvmgHNWVllktgdvqaVANDGAAAGADNDYVPPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1572928001 131 A-----PGETYSVTLD-----AKGTYSFFCS-PHQGAGMVGKVTV 164
Cdd:cd13922    81 HtkligGGESDSVTFTvsklaAGGDYTFFCSfPGHYAMMKGKLVV 125
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 80-164 5.88e-05

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: 40.26  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  80 FVPNNFSVASGE--KIVFKNNAGFPHNVVFDEDEIpsgvdagkismsDEDLlnAPGETYSVTL--DAKGTYSFFCSPHQg 155
Cdd:pfam13473  32 FSPSRITVPAGTpvKLEFKNKDKTPAEFESPDLGI------------EKVL--APGKTSTITIppLKPGEYDFFCDMHM- 96


                  ....*....
gi 1572928001 156 aGMVGKVTV 164
Cdd:pfam13473  97 -DAKGKLIV 104
Cupredoxin_like_1 cd04210
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 67-164 2.99e-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: 38.22  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572928001  67 IEVLLGGDDGSLAFVPNNFSVASGE--KIVFKNNAGFPHnvVFDEDEIPSG-----VDAGKISM--SDEDLLNAPGET-- 135
Cdd:cd04210     3 IKISLGNAANALRFFPDQLEFEAGKryKLHLHNPSQLKH--YFTAKDFADAiwtrkVDAGGVEIkgAIRELELKPGAEae 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1572928001 136 YSVTLDAKGTYSFFCS--PHQGAGMVGKVTV 164
Cdd:cd04210    81 WQFVPLKTGKYDLRCTipGHAEAGMTGQITI 111
 
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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