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Conserved domains on  [gi|1842004001|ref|YP_009791392|]
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PetE plastocyanine [Synechococcus phage Bellamy]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 139548)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions

CATH:  2.60.40.420
Gene Ontology:  GO:0005507|GO:0009055
PubMed:  21258692|35994119
SCOP:  3000886

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 20-107 2.86e-36

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.


The actual alignment was detected with superfamily member cd04219:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 97  Bit Score: 118.63  E-value: 2.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGSN-GNLVFDPEEVTISAGESVHFVNNMLPPHNVI--------VEDRPDLGHEALAMLPGEEFDVAFPEAGDYTY 90
Cdd:cd04219     1 ATVKMGSDsGALVFEPKELTVKAGDTVEFVNNKGGPHNVVfdedavpsAVDAAALSHKDLLNAPGETFSVTFPAPGTYTF 80

                          90
                  ....*....|....*..
gi 1842004001  91 WCGPHKGAGMIGTVHVE 107
Cdd:cd04219    81 YCEPHRGAGMVGKITVQ 97
 
Name Accession Description Interval E-value
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 20-107 2.86e-36

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: 118.63  E-value: 2.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGSN-GNLVFDPEEVTISAGESVHFVNNMLPPHNVI--------VEDRPDLGHEALAMLPGEEFDVAFPEAGDYTY 90
Cdd:cd04219     1 ATVKMGSDsGALVFEPKELTVKAGDTVEFVNNKGGPHNVVfdedavpsAVDAAALSHKDLLNAPGETFSVTFPAPGTYTF 80

                          90
                  ....*....|....*..
gi 1842004001  91 WCGPHKGAGMIGTVHVE 107
Cdd:cd04219    81 YCEPHRGAGMVGKITVQ 97
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 20-107 1.30e-31

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: 106.82  E-value: 1.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGS-NGNLVFDPEEVTISAGESVHFVNNMLPPHNVIV----------EDRPDLGHEALAMLPGEEFDVAFPEAGDY 88
Cdd:TIGR02656   1 VTVKMGAdKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFdedavpagvkELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1842004001  89 TYWCGPHKGAGMIGTVHVE 107
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
25-107 2.11e-23

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 85.88  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  25 GSNGNLVFDPEEVTISAGESVHFVNNMLPPHNVIVE----------DRPDLGHEALAMLPGEEFDVAFPEAGDYTYWCGP 94
Cdd:pfam00127   7 VDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDkdgvpagvdaDKVKMGDHTKLIGGGETYSVTFDLAGTYGFFCTP 86

                          90
                  ....*....|...
gi 1842004001  95 HKGAGMIGTVHVE 107
Cdd:pfam00127  87 HQGAGMVGKVTVE 99
PetE COG3794
Plastocyanin [Energy production and conversion];
30-107 3.81e-22

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 82.35  E-value: 3.81e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842004001  30 LVFDPEEVTISAGESVHFVNNMLPPHNVIVEDRPDLGHEALAMLPGEEFDVAFPEAGDYTYWCGPHKgaGMIGTVHVE 107
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDGPDGAFDSGLLAPGETFSVTFDEPGTYDYYCTPHP--WMVGTIVVG 76
 
Name Accession Description Interval E-value
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 20-107 2.86e-36

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: 118.63  E-value: 2.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGSN-GNLVFDPEEVTISAGESVHFVNNMLPPHNVI--------VEDRPDLGHEALAMLPGEEFDVAFPEAGDYTY 90
Cdd:cd04219     1 ATVKMGSDsGALVFEPKELTVKAGDTVEFVNNKGGPHNVVfdedavpsAVDAAALSHKDLLNAPGETFSVTFPAPGTYTF 80

                          90
                  ....*....|....*..
gi 1842004001  91 WCGPHKGAGMIGTVHVE 107
Cdd:cd04219    81 YCEPHRGAGMVGKITVQ 97
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 20-107 1.30e-31

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: 106.82  E-value: 1.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGS-NGNLVFDPEEVTISAGESVHFVNNMLPPHNVIV----------EDRPDLGHEALAMLPGEEFDVAFPEAGDY 88
Cdd:TIGR02656   1 VTVKMGAdKGALVFEPAKISIAAGDTVEWVNNKGGPHNVVFdedavpagvkELAKSLSHKDLLNSPGESYEVTFSTPGTY 80

                          90
                  ....*....|....*....
gi 1842004001  89 TYWCGPHKGAGMIGTVHVE 107
Cdd:TIGR02656  81 TFYCEPHRGAGMVGKITVE 99
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
25-107 2.11e-23

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 85.88  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  25 GSNGNLVFDPEEVTISAGESVHFVNNMLPPHNVIVE----------DRPDLGHEALAMLPGEEFDVAFPEAGDYTYWCGP 94
Cdd:pfam00127   7 VDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVVFDkdgvpagvdaDKVKMGDHTKLIGGGETYSVTFDLAGTYGFFCTP 86

                          90
                  ....*....|...
gi 1842004001  95 HKGAGMIGTVHVE 107
Cdd:pfam00127  87 HQGAGMVGKVTVE 99
PetE COG3794
Plastocyanin [Energy production and conversion];
30-107 3.81e-22

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 82.35  E-value: 3.81e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842004001  30 LVFDPEEVTISAGESVHFVNNMLPPHNVIVEDRPDLGHEALAMLPGEEFDVAFPEAGDYTYWCGPHKgaGMIGTVHVE 107
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTDSVPHNVTSDDGPDGAFDSGLLAPGETFSVTFDEPGTYDYYCTPHP--WMVGTIVVG 76
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 20-104 1.02e-18

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: 74.14  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGS-NGNLVFDPEEVTISAGESVHFVNNMLPPHNV-----IVEDRPDLGHEALAMLPGEEFDVAFPEAGDYTYWCG 93
Cdd:cd04204     1 VVVKMGAdNGAMAFEPAAIRVDAGETVEFVNTGGGPHNVvfdkeIVPDGDAEFESDRVDEEGFTYEQTFDEPGVYGYYCT 80

                          90
                  ....*....|.
gi 1842004001  94 PHKGAGMIGTV 104
Cdd:cd04204    81 PHRGAGMVGTV 91
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 20-107 9.37e-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: 68.95  E-value: 9.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGSNGNLVFDPEEVTISAGESVHFVNN-MLPPHNVIVEDRP--DLGHEALAMLPGEEFDVAFPEAGDYTYWCGPHK 96
Cdd:cd04220     2 VTVGVGMNGGFAFDPAAIRVSPGTTVTWEWTgEGGGHNVVAYEDPitAFDSGSTDSSEGETYEHTFEETGEYRYVCVPHE 81

                          90
                  ....*....|.
gi 1842004001  97 GAGMIGTVHVE 107
Cdd:cd04220    82 ALGMKGAIVVE 92
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 29-107 1.24e-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: 63.12  E-value: 1.24e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842004001  29 NLVFDPEEVTISAGESVHFVNNMLPPHNVIVEDRpdlGHEALAMLPGEEFDVAFPEAGDYTYWCGPHkgAGMIGTVHVE 107
Cdd:cd13921     8 DFKFNPAEVTVKVGDTVTWTNKDSVPHTVTAEDG---AFDSGMLATGKSFSYTFTAAGTYDYFCTIH--PFMKGTVTVE 81
Pseudoazurin cd04218
Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has ...
 20-106 8.54e-10

Pseudoazurin (Paz) is a type I blue copper electron-transfer protein; Pseudoazurin (PAz) has been identified as an electron donor to the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. It has been shown that pseudoazurin dramatically enhances the reaction profile of nitrite reduction by Paracoccus pantotrophus cytochrome cd1 and facilitates release of the product nitric oxide. The ability of this small redox protein to interact with a multitude of structurally different partners has been attributed to the hydrophobic character of the binding surface.


Pssm-ID: 259880 [Multi-domain]  Cd Length: 117  Bit Score: 51.53  E-value: 8.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQM---GSNGNLVFDPEEVTISAGESVHFVNNMlPPHNV--IVEDRPDlGHEALAMLPGEEFDVAFPEAGDYTYWCGP 94
Cdd:cd04218     2 HEVKMlnkGAGGAMVFEPAFLRAEPGDTVTFVPTD-KSHNAasIKGMLPE-GAEPFKGKINEEITVTFEKEGVYGYKCTP 79

                          90
                  ....*....|..
gi 1842004001  95 HKGAGMIGTVHV 106
Cdd:cd04218    80 HYGMGMVGLIQV 91
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 22-104 3.58e-07

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: 44.91  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  22 VQMGSNGNLVFDPEEVTISAGESV--HFVNNMLPPHNVIVEDRPDLGHEA-----------LAMLPGEEFDVAFPE--AG 86
Cdd:cd00920    10 WSFTYNGVLLFGPPVLVVPVGDTVrvQFVNKLGENHSVTIAGFGVPVVAMagganpglvntLVIGPGESAEVTFTTdqAG 89

                          90       100
                  ....*....|....*....|
gi 1842004001  87 DYTYWCGPHKG--AGMIGTV 104
Cdd:cd00920    90 VYWFYCTIPGHnhAGMVGTI 109
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 20-107 2.83e-06

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 43.02  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  20 VDVQMGSNgnLVFDPEEVTISAGESVHFV--NNMLPPHNVIVEDR-------------PDLGHEALAML---PGE--EFD 79
Cdd:COG4454    44 ITVTMGDT--MRFTPDSIEVKAGETVRFVvtNPGKLKHEFVLGTFaelaehakvmakmPDMEHGDPNEVelaPGEtgELV 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1842004001  80 VAFPEAGDYTYWC---GpHKGAGMIGTVHVE 107
Cdd:COG4454   122 WTFTKAGTFEFAClipG-HYEAGMTGKIVVK 151
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 19-106 2.30e-04

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: 37.61  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  19 AVDVQMGS-NGNLVFDPEEVTISAGESVH--FVNNMLPPHN-VIVED--RPDLGHEALAML------------------- 73
Cdd:cd04233     1 ATTITIKAvPGELKFDKTRLTVKAGSKVTltFENPDDMPHNlVIVKPgsLEKVGEAALAMGadgpaknyvpdspdvlaat 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1842004001  74 ----PGEEFDVAF--P-EAGDYTYWCG-PHKGAGMIGTVHV 106
Cdd:cd04233    81 plvnPGETETLTFtaPtEPGTYPYVCTyPGHWAIMKGVLIV 121
MauL cd04221
Methylamine utilization protein MauL; MauL is one of the products from the methylamine ...
 32-106 7.95e-04

Methylamine utilization protein MauL; MauL is one of the products from the methylamine utilization gene cluster in Methylobacterium extorquens AM1. Mutants generated by insertions in mauL were not able to grow on methylamine or any other primary amine as carbon sources. MauL belongs to the blue or type I copper protein family. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form.


Pssm-ID: 259883 [Multi-domain]  Cd Length: 83  Bit Score: 35.42  E-value: 7.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842004001  32 FDPEEVTISAGESVHFVNNMLPPHNVIVeDRPDLGHEALAMLPGEEFDVAFP-EAGDYTYWCGPHKgaGMIGTVHV 106
Cdd:cd04221    11 FEPHVLVIKPGDTVSFPNSDDIRHNVYS-FSPAKIFELLDQPPGTTKDVVLFdKAGVVVVGCNIHP--IMRAWILV 83
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 31-95 2.10e-03

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: 34.87  E-value: 2.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842004001  31 VFDPEEVTISAGESV--HFVNNMLPPHNVIVedrPDLG-HEALAmlPGEEFDVAFP--EAGDYTYWCGPH 95
Cdd:pfam13473  31 GFSPSRITVPAGTPVklEFKNKDKTPAEFES---PDLGiEKVLA--PGKTSTITIPplKPGEYDFFCDMH 95
 
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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