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Conserved domains on  [gi|1012261357|ref|XP_015946173|]
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lamin-like protein [Arachis duranensis]

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 ...
 1-164 1.55e-38

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 PLN03148:

Pssm-ID: 473140  Cd Length: 167  Bit Score: 129.22  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357   1 MKRVLLLLVFVAFAfivmVPEASAKRWLVGDNMGWSSsyGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKC 80
Cdd:PLN03148    1 SAHLLLFCFFALFS----ASATTATDHIVGANKGWNP--GINYTLWANNQTFYVGDLISFRYQKTQYNVFEVNQTGYDNC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  81 NSDHPLHNWTTGagRDVVPLNVTRNYYFISGKGFCFGGMKLAVHVENLPPPPKASPEVAGAP-----PALYSRSQVVLLP 155
Cdd:PLN03148   75 TTEGAAGNWTSG--KDFIPLNKAKRYYFICGNGQCFNGMKVTILVHPLPPPPSHTAAANGAKshsaaPAAFHKGLVALRG 152


                  ....*....
gi 1012261357 156 VVFAVGAAW 164
Cdd:PLN03148  153 LVLWMASIW 161
 
Name Accession Description Interval E-value
PLN03148 PLN03148
Blue copper-like protein; Provisional
 1-164 1.55e-38

Blue copper-like protein; Provisional


Pssm-ID: 178693  Cd Length: 167  Bit Score: 129.22  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357   1 MKRVLLLLVFVAFAfivmVPEASAKRWLVGDNMGWSSsyGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKC 80
Cdd:PLN03148    1 SAHLLLFCFFALFS----ASATTATDHIVGANKGWNP--GINYTLWANNQTFYVGDLISFRYQKTQYNVFEVNQTGYDNC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  81 NSDHPLHNWTTGagRDVVPLNVTRNYYFISGKGFCFGGMKLAVHVENLPPPPKASPEVAGAP-----PALYSRSQVVLLP 155
Cdd:PLN03148   75 TTEGAAGNWTSG--KDFIPLNKAKRYYFICGNGQCFNGMKVTILVHPLPPPPSHTAAANGAKshsaaPAAFHKGLVALRG 152


                  ....*....
gi 1012261357 156 VVFAVGAAW 164
Cdd:PLN03148  153 LVLWMASIW 161
Phytocyanin_like_1 cd11017
A subclass of phytocyanins, plant blue or type I copper proteins; Phytocyanins are plant blue ...
 29-125 7.18e-38

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: 125.20  E-value: 7.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  29 VGDNM-GWSSsyGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLhNWTTGAGRDVVPLNVTRNYY 107
Cdd:cd11017     5 VGGNRiGWNP--NINYTDWAKMHGFYSGDWLVFRYQRGRHNVVQVNETGYDNCDASNPI-SNYSSGGRDIFQLNETKRYY 81

                          90
                  ....*....|....*...
gi 1012261357 108 FISGKGFCFGGMKLAVHV 125
Cdd:cd11017    82 FICGRGYCYGGMKLAITV 99
Cu_bind_like pfam02298
Plastocyanin-like domain; This family represents a domain found in flowering plants related to ...
 35-119 7.52e-31

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: 107.05  E-value: 7.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  35 WSSSYGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLHNWTTgaGRDVVPLNVTRNYYFISGK-G 113
Cdd:pfam02298   1 WTVNAESDYTTWAQGKTFRVGDTLVFKYDSDFHNVVEVTKADYESCDTSKPIRNYTT--GSDKVTLTKPGPNYFICGVpG 78


                  ....*.
gi 1012261357 114 FCFGGM 119
Cdd:pfam02298  79 HCKFGM 84
 
Name Accession Description Interval E-value
PLN03148 PLN03148
Blue copper-like protein; Provisional
 1-164 1.55e-38

Blue copper-like protein; Provisional


Pssm-ID: 178693  Cd Length: 167  Bit Score: 129.22  E-value: 1.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357   1 MKRVLLLLVFVAFAfivmVPEASAKRWLVGDNMGWSSsyGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKC 80
Cdd:PLN03148    1 SAHLLLFCFFALFS----ASATTATDHIVGANKGWNP--GINYTLWANNQTFYVGDLISFRYQKTQYNVFEVNQTGYDNC 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  81 NSDHPLHNWTTGagRDVVPLNVTRNYYFISGKGFCFGGMKLAVHVENLPPPPKASPEVAGAP-----PALYSRSQVVLLP 155
Cdd:PLN03148   75 TTEGAAGNWTSG--KDFIPLNKAKRYYFICGNGQCFNGMKVTILVHPLPPPPSHTAAANGAKshsaaPAAFHKGLVALRG 152


                  ....*....
gi 1012261357 156 VVFAVGAAW 164
Cdd:PLN03148  153 LVLWMASIW 161
Phytocyanin_like_1 cd11017
A subclass of phytocyanins, plant blue or type I copper proteins; Phytocyanins are plant blue ...
 29-125 7.18e-38

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: 125.20  E-value: 7.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  29 VGDNM-GWSSsyGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLhNWTTGAGRDVVPLNVTRNYY 107
Cdd:cd11017     5 VGGNRiGWNP--NINYTDWAKMHGFYSGDWLVFRYQRGRHNVVQVNETGYDNCDASNPI-SNYSSGGRDIFQLNETKRYY 81

                          90
                  ....*....|....*...
gi 1012261357 108 FISGKGFCFGGMKLAVHV 125
Cdd:cd11017    82 FICGRGYCYGGMKLAITV 99
Cu_bind_like pfam02298
Plastocyanin-like domain; This family represents a domain found in flowering plants related to ...
 35-119 7.52e-31

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: 107.05  E-value: 7.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  35 WSSSYGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLHNWTTgaGRDVVPLNVTRNYYFISGK-G 113
Cdd:pfam02298   1 WTVNAESDYTTWAQGKTFRVGDTLVFKYDSDFHNVVEVTKADYESCDTSKPIRNYTT--GSDKVTLTKPGPNYFICGVpG 78


                  ....*.
gi 1012261357 114 FCFGGM 119
Cdd:pfam02298  79 HCKFGM 84
Phytocyanin cd04216
Phytocyanins are plant blue or type I copper proteins; Phytocyanins are plant blue or type I ...
 25-125 1.55e-30

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: 106.58  E-value: 1.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  25 KRWLVGDNMGWSssYGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLHNWTTgaGRDVVPLNVTR 104
Cdd:cd04216     1 TDYTVGDSNGWD--LPVNYTAWASGKTFRVGDSLVFNYNAGAHSVVEVNEADYDSCDTSNPINTYTS--GNDSVTLTKPG 76

                          90       100
                  ....*....|....*....|..
gi 1012261357 105 NYYFISGKGF-CFGGMKLAVHV 125
Cdd:cd04216    77 TRYFICGVPGhCQSGMKLAINV 98
Mavicyanin cd11014
Mavicyanin is a subclass of phytocyanins, a plant blue copper protein; Mavicyanin is a ...
 29-125 2.02e-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: 93.61  E-value: 2.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  29 VGDNMGWSSSYGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLHNWTTGAgrDVVPLNVTRNYYF 108
Cdd:cd11014     5 VGDSDGWTVYDSDYYYKWSSSKTFHVGDSLIFQYNKEFHDVTEVTGEEFESCNSTSPIAVYNTGH--DIIKLTKPGQYYF 82

                          90
                  ....*....|....*...
gi 1012261357 109 ISGK-GFCFGGMKLAVHV 125
Cdd:cd11014    83 ICGVpGHCDSGQKLQVNV 100
OsENODL1_like cd11019
Early nodulin-like protein (OsENODL1) and similar proteins; This family includes early ...
 29-125 1.96e-21

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: 83.47  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  29 VGDNMGWS--SSYGVNYTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLHNWTtgAGRDVVPLNVTRNY 106
Cdd:cd11019     5 VGGKDGWKvpPSASESYNQWAERNRFQVGDSLVFKYDKGNDSVLEVTKEDYDSCNTSSPIARFN--DGNTKFTLDRSGPF 82

                          90       100
                  ....*....|....*....|
gi 1012261357 107 YFISG-KGFCFGGMKLAVHV 125
Cdd:cd11019    83 YFISGaPGHCEKGQKLIVVV 102
Stellacyanin cd13920
Stellacyanin is a subclass of phytocyanins, a plant type I copper protein; Stellacyanin is a ...
 29-125 1.39e-19

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: 78.51  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  29 VGDNMGWSSSYGVN-YTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSDHPLHNWTTGAGrdVVPLNVTRNYY 107
Cdd:cd13920     5 VGGSLGWSIPPNASfYTDWAANRTFRVGDSLVFNFEAGVHNVVEVSKEEYDNCTTTNPIKVFTTGPV--IITLNETGTRY 82

                          90
                  ....*....|....*....
gi 1012261357 108 FISG-KGFCFGGMKLAVHV 125
Cdd:cd13920    83 FICTvGNHCSLGQKVSINV 101
Plantacyanin cd11013
Plantacyanin is a subclass of phytocyanins, plant type I copper proteins; Plantacyanins belong ...
 27-123 2.62e-17

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: 72.77  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1012261357  27 WLVGDNMGWSssYGVnyTNWAKGKHFYNGDWLFFVYDRNQMNVLEVNKTDYEKCNSdhPLHNWTTGAGRDVVPLNVTRNY 106
Cdd:cd11013     3 YVVGDSIGWT--FGV--VGWPNGKTFRAGDVLVFNYDPSAHNVVVVDEGGYRTCKA--PPGAIVYTSGDDKITLPKGVNY 76

                          90
                  ....*....|....*..
gi 1012261357 107 YFISGKGFCFGGMKLAV 123
Cdd:cd11013    77 FICSFPGHCTSGMKIAV 93
 
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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