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Conserved domains on  [gi|1051411357|ref|WP_065878812|]
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MULTISPECIES: cupredoxin domain-containing protein [Pseudomonas]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 10604510)

uncharacterized cupredoxin-like domain-containing protein, similar to CupA, a cell membrane-anchored Cu(I) chaperone involved in copper resistance

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 18-97 5.54e-31

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: 105.36  E-value: 5.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051411357  18 AAALPTYELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGPAEFESTPLRVEKVLSPGVTTFVVIHPLQPGVYPFFDEFNP 97
Cdd:pfam13473  17 AADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFCDMHM 96
 
Name Accession Description Interval E-value
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 18-97 5.54e-31

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: 105.36  E-value: 5.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051411357  18 AAALPTYELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGPAEFESTPLRVEKVLSPGVTTFVVIHPLQPGVYPFFDEFNP 97
Cdd:pfam13473  17 AADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFCDMHM 96
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
23-91 6.94e-06

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 41.44  E-value: 6.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051411357  23 TYELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGP--AEFESTPLRVEKVLSPGVTTFVVIHPLQPGVYPF 91
Cdd:COG4633    37 EVTITVDGGGYSPSRITVKAGIPVRLNFTRKDPSGcaEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPF 107
Cupredoxin_like_3 cd04203
Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are ...
 25-104 1.43e-05

Uncharacterized subfamiy of Cupredoxin; 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. Majority of family members contain multiple cupredoxin domain repeats: ceruloplamin 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. Proteins of this uncharacterized subfamily contain a single cupredoxin domain.


Pssm-ID: 259866 [Multi-domain]  Cd Length: 84  Bit Score: 39.90  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051411357  25 ELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGPAEFESTPLRVEKVLSPGVTTFVVIHPLQPGVYPFFDEFNPQLPEGSI 104
Cdd:cd04203     3 KITLNDDYFNPNVITVPINEKTTLILHNKGQKSEETETIKKLGIDVVVESEEINITVKPLSPGTYELICRYHLLG*EGKV 82
PLN02268 PLN02268
probable polyamine oxidase
 21-62 2.23e-03

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 35.82  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1051411357  21 LPTYELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGPAEFES 62
Cdd:PLN02268   91 LESYALFDMDGNQVPQELVTKVGETFERILEETEKVRDEHEE 132
 
Name Accession Description Interval E-value
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 18-97 5.54e-31

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: 105.36  E-value: 5.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051411357  18 AAALPTYELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGPAEFESTPLRVEKVLSPGVTTFVVIHPLQPGVYPFFDEFNP 97
Cdd:pfam13473  17 AADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFCDMHM 96
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
23-91 6.94e-06

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 41.44  E-value: 6.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051411357  23 TYELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGP--AEFESTPLRVEKVLSPGVTTFVVIHPLQPGVYPF 91
Cdd:COG4633    37 EVTITVDGGGYSPSRITVKAGIPVRLNFTRKDPSGcaEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPF 107
Cupredoxin_like_3 cd04203
Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are ...
 25-104 1.43e-05

Uncharacterized subfamiy of Cupredoxin; 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. Majority of family members contain multiple cupredoxin domain repeats: ceruloplamin 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. Proteins of this uncharacterized subfamily contain a single cupredoxin domain.


Pssm-ID: 259866 [Multi-domain]  Cd Length: 84  Bit Score: 39.90  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051411357  25 ELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGPAEFESTPLRVEKVLSPGVTTFVVIHPLQPGVYPFFDEFNPQLPEGSI 104
Cdd:cd04203     3 KITLNDDYFNPNVITVPINEKTTLILHNKGQKSEETETIKKLGIDVVVESEEINITVKPLSPGTYELICRYHLLG*EGKV 82
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 23-91 3.36e-05

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 40.33  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051411357  23 TYELSLQDG-HFTPPQLVVKAGERFKIVLKNTGLGPAEF---------ESTPLRVEKV-----------LSPGVTTFVVI 81
Cdd:COG4454    43 TITVTMGDTmRFTPDSIEVKAGETVRFVVTNPGKLKHEFvlgtfaelaEHAKVMAKMPdmehgdpneveLAPGETGELVW 122

                          90
                  ....*....|
gi 1051411357  82 HPLQPGVYPF 91
Cdd:COG4454   123 TFTKAGTFEF 132
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 33-91 7.48e-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: 36.07  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051411357  33 FTPPQLVVKAGERFKIVLKNTG-----------------------LGPAEFESTP-------LRVEKVLSPGVT-TFVVI 81
Cdd:cd04233    15 FDKTRLTVKAGSKVTLTFENPDdmphnlvivkpgslekvgeaalaMGADGPAKNYvpdspdvLAATPLVNPGETeTLTFT 94

                          90
                  ....*....|
gi 1051411357  82 HPLQPGVYPF 91
Cdd:cd04233    95 APTEPGTYPY 104
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 32-91 1.06e-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: 35.67  E-value: 1.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051411357  32 HFTPPQLVVKAGERFKIVLKNTGLGPAEF---------------ESTPLRVEKVLSPGVTTFVVIHPLQPGVYPF 91
Cdd:cd00920    19 LFGPPVLVVPVGDTVRVQFVNKLGENHSVtiagfgvpvvamaggANPGLVNTLVIGPGESAEVTFTTDQAGVYWF 93
PLN02268 PLN02268
probable polyamine oxidase
 21-62 2.23e-03

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 35.82  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1051411357  21 LPTYELSLQDGHFTPPQLVVKAGERFKIVLKNTGLGPAEFES 62
Cdd:PLN02268   91 LESYALFDMDGNQVPQELVTKVGETFERILEETEKVRDEHEE 132
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 23-60 3.83e-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: 34.19  E-value: 3.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1051411357  23 TYELSLQD-GHFTPPQLVVKAGERFKIVLKNTGLGPAEF 60
Cdd:cd04211     3 TIEVTMSDtMRFTPDSIQVKQGETVRFVVTNNGKIPHEF 41
 
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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