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Conserved domains on  [gi|1965327819|ref|XP_039049336|]
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plastocyanin [Hibiscus syriacus]

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;
70-167 3.23e-51

Copper binding proteins, plastocyanin/azurin family;


:

Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 159.07  E-value: 3.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKISMPEEDLLNAPGETYAVTLTEKGSYS 149
Cdd:pfam00127   2 EVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTYG 81

                          90
                  ....*....|....*...
gi 1965327819 150 FYCSPHQGAGMVGKVTVN 167
Cdd:pfam00127  82 FFCTPHQGAGMVGKVTVE 99
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
70-167 3.23e-51

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 159.07  E-value: 3.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKISMPEEDLLNAPGETYAVTLTEKGSYS 149
Cdd:pfam00127   2 EVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTYG 81

                          90
                  ....*....|....*...
gi 1965327819 150 FYCSPHQGAGMVGKVTVN 167
Cdd:pfam00127  82 FFCTPHQGAGMVGKVTVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 69-167 8.49e-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: 157.92  E-value: 8.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  69 LEVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKISMpeEDLLNAPGETYAVTLTEKGSY 148
Cdd:cd04219     1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                          90
                  ....*....|....*....
gi 1965327819 149 SFYCSPHQGAGMVGKVTVN 167
Cdd:cd04219    79 TFYCEPHRGAGMVGKITVQ 97
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 70-167 1.40e-49

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: 154.97  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKISMPEEDLLNAPGETYAVTLTEKGSYS 149
Cdd:TIGR02656   2 TVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTYT 81

                          90
                  ....*....|....*...
gi 1965327819 150 FYCSPHQGAGMVGKVTVN 167
Cdd:TIGR02656  82 FYCEPHRGAGMVGKITVE 99
PetE COG3794
Plastocyanin [Energy production and conversion];
80-166 9.23e-20

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 78.11  E-value: 9.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  80 LAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDevPSGVDASKISmpeedllnAPGETYAVTLTEKGSYSFYCSPHqgAG 159
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDG--PDGAFDSGLL--------APGETFSVTFDEPGTYDYYCTPH--PW 68


                  ....*..
gi 1965327819 160 MVGKVTV 166
Cdd:COG3794    69 MVGTIVV 75
 
Name Accession Description Interval E-value
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
70-167 3.23e-51

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 159.07  E-value: 3.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKISMPEEDLLNAPGETYAVTLTEKGSYS 149
Cdd:pfam00127   2 EVLLGVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDKDGVPAGVDADKVKMGDHTKLIGGGETYSVTFDLAGTYG 81

                          90
                  ....*....|....*...
gi 1965327819 150 FYCSPHQGAGMVGKVTVN 167
Cdd:pfam00127  82 FFCTPHQGAGMVGKVTVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 69-167 8.49e-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: 157.92  E-value: 8.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  69 LEVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKISMpeEDLLNAPGETYAVTLTEKGSY 148
Cdd:cd04219     1 ATVKMGSDSGALVFEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSH--KDLLNAPGETFSVTFPAPGTY 78

                          90
                  ....*....|....*....
gi 1965327819 149 SFYCSPHQGAGMVGKVTVN 167
Cdd:cd04219    79 TFYCEPHRGAGMVGKITVQ 97
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 70-167 1.40e-49

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: 154.97  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKISMPEEDLLNAPGETYAVTLTEKGSYS 149
Cdd:TIGR02656   2 TVKMGADKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLSHKDLLNSPGESYEVTFSTPGTYT 81

                          90
                  ....*....|....*...
gi 1965327819 150 FYCSPHQGAGMVGKVTVN 167
Cdd:TIGR02656  82 FYCEPHRGAGMVGKITVE 99
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 70-165 1.02e-32

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: 111.89  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGVDASKismpeEDLLNAPGETYAVTLTEKGSYS 149
Cdd:cd04204     2 VVKMGADNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPDGDAEFE-----SDRVDEEGFTYEQTFDEPGVYG 76

                          90
                  ....*....|....*.
gi 1965327819 150 FYCSPHQGAGMVGKVT 165
Cdd:cd04204    77 YYCTPHRGAGMVGTVI 92
PetE COG3794
Plastocyanin [Energy production and conversion];
80-166 9.23e-20

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 78.11  E-value: 9.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  80 LAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDevPSGVDASKISmpeedllnAPGETYAVTLTEKGSYSFYCSPHqgAG 159
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDG--PDGAFDSGLL--------APGETFSVTFDEPGTYDYYCTPH--PW 68


                  ....*..
gi 1965327819 160 MVGKVTV 166
Cdd:COG3794    69 MVGTIVV 75
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 75-167 4.46e-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: 71.65  E-value: 4.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  75 GDDGSLAFIPREFSVSSGEKIVFKNNA-GFPHNVVFDEDEVPSGVDASKISmpeedllnAPGETYAVTLTEKGSYSFYCS 153
Cdd:cd04220     7 GMNGGFAFDPAAIRVSPGTTVTWEWTGeGGGHNVVAYEDPITAFDSGSTDS--------SEGETYEHTFEETGEYRYVCV 78

                          90
                  ....*....|....
gi 1965327819 154 PHQGAGMVGKVTVN 167
Cdd:cd04220    79 PHEALGMKGAIVVE 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 74-165 4.13e-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: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  74 GGDDGSLAFIPREFSVSSGE--KIVFKNNAGFPHNVV---FDEDEVPSGVDASKISMPeeDLLNAPGETYAVTLTEK--G 146
Cdd:cd00920    12 FTYNGVLLFGPPVLVVPVGDtvRVQFVNKLGENHSVTiagFGVPVVAMAGGANPGLVN--TLVIGPGESAEVTFTTDqaG 89

                          90       100
                  ....*....|....*....|.
gi 1965327819 147 SYSFYCSP--HQGAGMVGKVT 165
Cdd:cd00920    90 VYWFYCTIpgHNHAGMVGTIN 110
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 79-166 5.46e-13

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: 5.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  79 SLAFIPREFSVSSGEKIVFKNNAGFPHNVVFDEDEVPSGvdaskismpeedlLNAPGETYAVTLTEKGSYSFYCSPHqgA 158
Cdd:cd13921     8 DFKFNPAEVTVKVGDTVTWTNKDSVPHTVTAEDGAFDSG-------------MLATGKSFSYTFTAAGTYDYFCTIH--P 72


                  ....*...
gi 1965327819 159 GMVGKVTV 166
Cdd:cd13921    73 FMKGTVTV 80
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 70-166 2.21e-10

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: 54.95  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEK--IVFKNNAGFPHNVVF-DEDEVPSGVDASkISMPEE-----------------D 129
Cdd:cd04233     3 TITIKAVPGELKFDKTRLTVKAGSKvtLTFENPDDMPHNLVIvKPGSLEKVGEAA-LAMGADgpaknyvpdspdvlaatP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1965327819 130 LLNaPGETYAVTLT---EKGSYSFYCS-PHQGAGMVGKVTV 166
Cdd:cd04233    82 LVN-PGETETLTFTaptEPGTYPYVCTyPGHWAIMKGVLIV 121
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 70-166 1.19e-06

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: 44.98  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDGSLAFIPREFSVSSGEKIVFKNNAGfPHNVVFDEDEVPSGVDASKISMPEEdllnapgetYAVTLTEKGSYS 149
Cdd:cd04218     5 KMLNKGAGGAMVFEPAFLRAEPGDTVTFVPTDK-SHNAASIKGMLPEGAEPFKGKINEE---------ITVTFEKEGVYG 74

                          90
                  ....*....|....*..
gi 1965327819 150 FYCSPHQGAGMVGKVTV 166
Cdd:cd04218    75 YKCTPHYGMGMVGLIQV 91
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 70-166 4.68e-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: 37.92  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  70 EVLLGGDDgSLAFIPREFSVSSGEK---IVFKNNAGFP-----HNVV---------FDEDEVPSGVDASKIsmPEED--- 129
Cdd:cd13922     2 EVTIEGND-QMKFDTKEITVKAGCKeftVTLKHTGKLPknvmgHNWVllktgdvqaVANDGAAAGADNDYV--PPGDarv 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1965327819 130 -----LLnAPGETYAVT-----LTEKGSYSFYCS-PHQGAGMVGKVTV 166
Cdd:cd13922    79 iahtkLI-GGGESDSVTftvskLAAGGDYTFFCSfPGHYAMMKGKLVV 125
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 82-166 4.29e-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: 35.35  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965327819  82 FIPREFSVSSGEKIVF--KNNAGFPHNVVFDEDEvpsGVDASK---ISMP--EEDLLN----APGETYAV--TLTEKGSY 148
Cdd:cd04211    14 FTPDSIQVKQGETVRFvvTNNGKIPHEFVIGTAA---ELKEHAemmRKHPgmEHDEPNmvslAPGKSGEIvwTFTKAGTF 90

                          90       100
                  ....*....|....*....|
gi 1965327819 149 SFYCS-P-HQGAGMVGKVTV 166
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.
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