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Conserved domains on  [gi|42562941|ref|NP_176645|]
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early nodulin-like protein 8 [Arabidopsis thaliana]

Protein Classification

early nodulin-like family protein( domain architecture ID 10181143)

early nodulin-like family protein belongs to the phytocyanin-like group of blue copper proteins from the cupredoxin superfamily, and may be involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OsENODL1_like cd11019
Early nodulin-like protein (OsENODL1) and similar proteins; This family includes early ...
 31-131 2.66e-50

Early nodulin-like protein (OsENODL1) and similar proteins; This family includes early nodulin-like protein (OsENODL1) from Oryza sativa and similar proteins. It belongs to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Phytocyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. OsENODL1 expression occurs specifically at the late developmental stage of the seeds. Members of this subgroup appear to have lost the T1 copper binding site.


:

Pssm-ID: 259905  Cd Length: 103  Bit Score: 157.81  E-value: 2.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGDLDAWGIPIDA-KVYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNG 109
Cdd:cd11019   1 REFKVGGKDGWKVPPSAsESYNQWAERNRFQVGDSLVFKYDKGNDSVLEVTKEDYDSCNTSSPIARFNDGNTKFTLDRSG 80

                        90       100
                ....*....|....*....|..
gi 42562941 110 TLYFTSANPGHCTKYQKLLVSV 131
Cdd:cd11019  81 PFYFISGAPGHCEKGQKLIVVV 102
 
Name Accession Description Interval E-value
OsENODL1_like cd11019
Early nodulin-like protein (OsENODL1) and similar proteins; This family includes early ...
 31-131 2.66e-50

Early nodulin-like protein (OsENODL1) and similar proteins; This family includes early nodulin-like protein (OsENODL1) from Oryza sativa and similar proteins. It belongs to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Phytocyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. OsENODL1 expression occurs specifically at the late developmental stage of the seeds. Members of this subgroup appear to have lost the T1 copper binding site.


Pssm-ID: 259905  Cd Length: 103  Bit Score: 157.81  E-value: 2.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGDLDAWGIPIDA-KVYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNG 109
Cdd:cd11019   1 REFKVGGKDGWKVPPSAsESYNQWAERNRFQVGDSLVFKYDKGNDSVLEVTKEDYDSCNTSSPIARFNDGNTKFTLDRSG 80

                        90       100
                ....*....|....*....|..
gi 42562941 110 TLYFTSANPGHCTKYQKLLVSV 131
Cdd:cd11019  81 PFYFISGAPGHCEKGQKLIVVV 102
Cu_bind_like pfam02298
Plastocyanin-like domain; This family represents a domain found in flowering plants related to ...
 41-121 1.53e-22

Plastocyanin-like domain; This family represents a domain found in flowering plants related to the copper binding protein plastocyanin. Some members of this family may not bind copper due to the lack of key residues.


Pssm-ID: 280462  Cd Length: 84  Bit Score: 86.25  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941    41 WGIPIDAKvYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNGTLYFTSANPGH 120
Cdd:pfam02298   1 WTVNAESD-YTTWAQGKTFRVGDTLVFKYDSDFHNVVEVTKADYESCDTSKPIRNYTTGSDKVTLTKPGPNYFICGVPGH 79


                  .
gi 42562941   121 C 121
Cdd:pfam02298  80 C 80
PLN03148 PLN03148
Blue copper-like protein; Provisional
 14-149 2.28e-04

Blue copper-like protein; Provisional


Pssm-ID: 178693  Cd Length: 167  Bit Score: 39.86  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941   14 VLQVMILLGQEIGKVSSTLYKVGDLDAWGIPIDakvYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPI 93
Cdd:PLN03148   4 LLLFCFFALFSASATTATDHIVGANKGWNPGIN---YTLWANNQTFYVGDLISFRYQKTQYNVFEVNQTGYDNCTTEGAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42562941   94 LYMNDGNSLFNLTQNGTLYFTSANpGHCTKYQKLLVSV------GTYSAEAEALSPSSAADA 149
Cdd:PLN03148  81 GNWTSGKDFIPLNKAKRYYFICGN-GQCFNGMKVTILVhplpppPSHTAAANGAKSHSAAPA 141
 
Name Accession Description Interval E-value
OsENODL1_like cd11019
Early nodulin-like protein (OsENODL1) and similar proteins; This family includes early ...
 31-131 2.66e-50

Early nodulin-like protein (OsENODL1) and similar proteins; This family includes early nodulin-like protein (OsENODL1) from Oryza sativa and similar proteins. It belongs to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Phytocyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. OsENODL1 expression occurs specifically at the late developmental stage of the seeds. Members of this subgroup appear to have lost the T1 copper binding site.


Pssm-ID: 259905  Cd Length: 103  Bit Score: 157.81  E-value: 2.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGDLDAWGIPIDA-KVYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNG 109
Cdd:cd11019   1 REFKVGGKDGWKVPPSAsESYNQWAERNRFQVGDSLVFKYDKGNDSVLEVTKEDYDSCNTSSPIARFNDGNTKFTLDRSG 80

                        90       100
                ....*....|....*....|..
gi 42562941 110 TLYFTSANPGHCTKYQKLLVSV 131
Cdd:cd11019  81 PFYFISGAPGHCEKGQKLIVVV 102
Phytocyanin cd04216
Phytocyanins are plant blue or type I copper proteins; Phytocyanins are plant blue or type I ...
 31-131 9.34e-29

Phytocyanins are plant blue or type I copper proteins; Phytocyanins are plant blue or type I copper proteins. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Phytocyanins are classified into four groups: stellacyanin, plantacyanin, uclacyanin and early nodulin groups. Stellacyanin appears to be associated with the plant cell wall; it may be involved in oxidative reactions to build polymeric material making up the cell wall. Plantacyanin is shown to play a role in reproduction in Arabidopsis. Plantacyanins may also be stress-related proteins and may be involved in plant defense responses. The early nodulin-like protein (OsENODL1) from Oryza sativa is expressed specifically at the late developmental stage of the seeds.


Pssm-ID: 259878 [Multi-domain]  Cd Length: 98  Bit Score: 102.72  E-value: 9.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGDLDAWGIPIDakvYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNGT 110
Cdd:cd04216   1 TDYTVGDSNGWDLPVN---YTAWASGKTFRVGDSLVFNYNAGAHSVVEVNEADYDSCDTSNPINTYTSGNDSVTLTKPGT 77

                        90       100
                ....*....|....*....|.
gi 42562941 111 LYFTSANPGHCTKYQKLLVSV 131
Cdd:cd04216  78 RYFICGVPGHCQSGMKLAINV 98
Mavicyanin cd11014
Mavicyanin is a subclass of phytocyanins, a plant blue copper protein; Mavicyanin is a ...
 31-132 6.29e-25

Mavicyanin is a subclass of phytocyanins, a plant blue copper protein; Mavicyanin is a glycosylated protein isolated from Cucurbita pepo medullosa (zucchini) peelings. It belongs to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Mavicyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. The copper is tetrahedrally coordinated by a cysteine, 2 histidines, and a glutamine residue, like in the case of stellacyanin. The biological roles of mavicyanin have not been elucidated yet.


Pssm-ID: 259900  Cd Length: 101  Bit Score: 93.23  E-value: 6.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGDLDAWGIPiDAKVYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNGT 110
Cdd:cd11014   1 TVYKVGDSDGWTVY-DSDYYYKWSSSKTFHVGDSLIFQYNKEFHDVTEVTGEEFESCNSTSPIAVYNTGHDIIKLTKPGQ 79

                        90       100
                ....*....|....*....|..
gi 42562941 111 LYFTSANPGHCTKYQKLLVSVG 132
Cdd:cd11014  80 YYFICGVPGHCDSGQKLQVNVT 101
Stellacyanin cd13920
Stellacyanin is a subclass of phytocyanins, a plant type I copper protein; Stellacyanin is a ...
 31-131 8.07e-25

Stellacyanin is a subclass of phytocyanins, a plant type I copper protein; Stellacyanin is a subclass of the phytocyanins, a ubiquitous family of plant cupredoxins. Stellacyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. The copper is tetrahedrally coordinated by a cysteine, 2 histidines, and a glutamine residue. The glutamine residue substitutes for a methione ligand typically found in other blue copper proteins. The exact function of stellacyanin is unknown. However, stellacyanin appears to be associated with the plant cell wall; it may be involved in oxidative reactions to build polymeric material making up the cell wall.


Pssm-ID: 259987 [Multi-domain]  Cd Length: 101  Bit Score: 92.76  E-value: 8.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGDLDAWGIPIDAKVYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNGT 110
Cdd:cd13920   1 TDHIVGGSLGWSIPPNASFYTDWAANRTFRVGDSLVFNFEAGVHNVVEVSKEEYDNCTTTNPIKVFTTGPVIITLNETGT 80

                        90       100
                ....*....|....*....|.
gi 42562941 111 LYFTSANPGHCTKYQKLLVSV 131
Cdd:cd13920  81 RYFICTVGNHCSLGQKVSINV 101
Cu_bind_like pfam02298
Plastocyanin-like domain; This family represents a domain found in flowering plants related to ...
 41-121 1.53e-22

Plastocyanin-like domain; This family represents a domain found in flowering plants related to the copper binding protein plastocyanin. Some members of this family may not bind copper due to the lack of key residues.


Pssm-ID: 280462  Cd Length: 84  Bit Score: 86.25  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941    41 WGIPIDAKvYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQNGTLYFTSANPGH 120
Cdd:pfam02298   1 WTVNAESD-YTTWAQGKTFRVGDTLVFKYDSDFHNVVEVTKADYESCDTSKPIRNYTTGSDKVTLTKPGPNYFICGVPGH 79


                  .
gi 42562941   121 C 121
Cdd:pfam02298  80 C 80
Phytocyanin_like_1 cd11017
A subclass of phytocyanins, plant blue or type I copper proteins; Phytocyanins are plant blue ...
 31-131 1.18e-10

A subclass of phytocyanins, plant blue or type I copper proteins; Phytocyanins are plant blue or type I copper proteins. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Phytocyanins are classified into four groups: stellacyanin, plantacyanin, uclacyanin and early nodulin groups. Members of this unknown subgroup appear to have lost the T1 copper binding site.


Pssm-ID: 259903  Cd Length: 99  Bit Score: 55.86  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGD-LDAWGIPIDakvYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPIL-YMNDGNSLFNLTQN 108
Cdd:cd11017   1 TLHTVGGnRIGWNPNIN---YTDWAKMHGFYSGDWLVFRYQRGRHNVVQVNETGYDNCDASNPISnYSSGGRDIFQLNET 77

                        90       100
                ....*....|....*....|...
gi 42562941 109 GTLYFTSANpGHCTKYQKLLVSV 131
Cdd:cd11017  78 KRYYFICGR-GYCYGGMKLAITV 99
Plantacyanin cd11013
Plantacyanin is a subclass of phytocyanins, plant type I copper proteins; Plantacyanins belong ...
 31-131 1.07e-09

Plantacyanin is a subclass of phytocyanins, plant type I copper proteins; Plantacyanins belong to the phytocyanin family of blue copper proteins, a ubiquitous family of plant cupredoxins. Plantacyanin is involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. The exact function of plantacyanin is unknown. However plantacyanin is shown to play a role in reproduction in Arabidopsis. Plantacyanins may also be stress-related proteins and be involved in plant defense responses.


Pssm-ID: 259899  Cd Length: 95  Bit Score: 53.13  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  31 TLYKVGDLDAWGIPIDAkvyskWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPILYMNDGNSLFNLTQnGT 110
Cdd:cd11013   1 ATYVVGDSIGWTFGVVG-----WPNGKTFRAGDVLVFNYDPSAHNVVVVDEGGYRTCKAPPGAIVYTSGDDKITLPK-GV 74

                        90       100
                ....*....|....*....|.
gi 42562941 111 LYFTSANPGHCTKYQKLLVSV 131
Cdd:cd11013  75 NYFICSFPGHCTSGMKIAVTA 95
PLN03148 PLN03148
Blue copper-like protein; Provisional
 14-149 2.28e-04

Blue copper-like protein; Provisional


Pssm-ID: 178693  Cd Length: 167  Bit Score: 39.86  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941   14 VLQVMILLGQEIGKVSSTLYKVGDLDAWGIPIDakvYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFKSCNTKDPI 93
Cdd:PLN03148   4 LLLFCFFALFSASATTATDHIVGANKGWNPGIN---YTLWANNQTFYVGDLISFRYQKTQYNVFEVNQTGYDNCTTEGAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42562941   94 LYMNDGNSLFNLTQNGTLYFTSANpGHCTKYQKLLVSV------GTYSAEAEALSPSSAADA 149
Cdd:PLN03148  81 GNWTSGKDFIPLNKAKRYYFICGN-GQCFNGMKVTILVhplpppPSHTAAANGAKSHSAAPA 141
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 33-129 1.33e-03

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: 36.83  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42562941  33 YKVGDLDAWGIPIDAKVYSKWPKSHSFKIGDSLLFLYPPSEDSLIQVTPSNFK----SCNTKDPILYMND--------GN 100
Cdd:cd00920   1 ITVTASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVNKLGENHSVTIAGFGvpvvAMAGGANPGLVNTlvigpgesAE 80

                        90       100
                ....*....|....*....|....*....
gi 42562941 101 SLFNLTQNGTLYFTSANPGHCTKYQKLLV 129
Cdd:cd00920  81 VTFTTDQAGVYWFYCTIPGHNHAGMVGTI 109
 
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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