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Conserved domains on  [gi|1235630504|ref|WP_094782645|]
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cupredoxin domain-containing protein [Paraburkholderia ribeironis]

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 ...
 6-109 1.35e-48

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: 150.04  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   6 KIAMLAATVLLASTAHAADLPTFKLEMNDGKLNPARIEVPAGQRIKIEVRNTGKGAAEFESVQLRKEKVLAPGADSFVVI 85
Cdd:pfam13473   1 LIAALAVLFWLSKPAAAADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITI 80

                          90       100
                  ....*....|....*....|....
gi 1235630504  86 APLEPGEYKFFDDFHQQAQGVIVA 109
Cdd:pfam13473  81 PPLKPGEYDFFCDMHMDAKGKLIV 104
 
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 ...
 6-109 1.35e-48

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: 150.04  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   6 KIAMLAATVLLASTAHAADLPTFKLEMNDGKLNPARIEVPAGQRIKIEVRNTGKGAAEFESVQLRKEKVLAPGADSFVVI 85
Cdd:pfam13473   1 LIAALAVLFWLSKPAAAADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITI 80

                          90       100
                  ....*....|....*....|....
gi 1235630504  86 APLEPGEYKFFDDFHQQAQGVIVA 109
Cdd:pfam13473  81 PPLKPGEYDFFCDMHMDAKGKLIV 104
Cupredoxin_like_3 cd04203
Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are ...
 29-101 5.96e-14

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: 61.86  E-value: 5.96e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1235630504  29 KLEMNDGKLNPARIEVPAGQRIKIEVRNTGKGAAEFESVQLRKEKVLAPGADSFVVIAPLEPGEYKFFDDFHQ 101
Cdd:cd04203     3 KITLNDDYFNPNVITVPINEKTTLILHNKGQKSEETETIKKLGIDVVVESEEINITVKPLSPGTYELICRYHL 75
PRK10378 PRK10378
inactive ferrous ion transporter periplasmic protein EfeO; Provisional
 1-93 5.28e-07

inactive ferrous ion transporter periplasmic protein EfeO; Provisional


Pssm-ID: 236677 [Multi-domain]  Cd Length: 375  Bit Score: 46.30  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   1 MRNNRKIAMLAATVLL---ASTAHAADLPTFKLEMNDGKLNPARIEVPAGQRIKIeVRNTGKGAAEFESVQ----LRKEK 73
Cdd:PRK10378    2 TINFRRNALQLALAALfssAFMANAADIPQVKVTVNDKQCEPMTLTVNAGKTQFI-IQNHSQKALEWEILKgvmvVEERE 80

                          90       100
                  ....*....|....*....|
gi 1235630504  74 VLAPGAdSFVVIAPLEPGEY 93
Cdd:PRK10378   81 NIAPGF-SQKMTANLQPGEY 99
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 1-95 1.15e-06

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 44.18  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   1 MRNNRKIAMLAATVLLASTAHAADLP----------------TFKLEMNDG-KLNPARIEVPAGQRIKIEVRNTGKGAAE 63
Cdd:COG4454     1 MKRTLALLLALALALLATAALAAGDShasaigkpgdaakvtrTITVTMGDTmRFTPDSIEVKAGETVRFVVTNPGKLKHE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1235630504  64 FESVQL------RKEKV--------------LAPGADSFVVIAPLEPGEYKF 95
Cdd:COG4454    81 FVLGTFaelaehAKVMAkmpdmehgdpneveLAPGETGELVWTFTKAGTFEF 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 ...
 6-109 1.35e-48

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: 150.04  E-value: 1.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   6 KIAMLAATVLLASTAHAADLPTFKLEMNDGKLNPARIEVPAGQRIKIEVRNTGKGAAEFESVQLRKEKVLAPGADSFVVI 85
Cdd:pfam13473   1 LIAALAVLFWLSKPAAAADDPTVEITVKDGGFSPSRITVPAGTPVKLEFKNKDKTPAEFESPDLGIEKVLAPGKTSTITI 80

                          90       100
                  ....*....|....*....|....
gi 1235630504  86 APLEPGEYKFFDDFHQQAQGVIVA 109
Cdd:pfam13473  81 PPLKPGEYDFFCDMHMDAKGKLIV 104
Cupredoxin_like_3 cd04203
Uncharacterized subfamiy of Cupredoxin; Cupredoxins contain type I copper centers and are ...
 29-101 5.96e-14

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: 61.86  E-value: 5.96e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1235630504  29 KLEMNDGKLNPARIEVPAGQRIKIEVRNTGKGAAEFESVQLRKEKVLAPGADSFVVIAPLEPGEYKFFDDFHQ 101
Cdd:cd04203     3 KITLNDDYFNPNVITVPINEKTTLILHNKGQKSEETETIKKLGIDVVVESEEINITVKPLSPGTYELICRYHL 75
PRK10378 PRK10378
inactive ferrous ion transporter periplasmic protein EfeO; Provisional
 1-93 5.28e-07

inactive ferrous ion transporter periplasmic protein EfeO; Provisional


Pssm-ID: 236677 [Multi-domain]  Cd Length: 375  Bit Score: 46.30  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   1 MRNNRKIAMLAATVLL---ASTAHAADLPTFKLEMNDGKLNPARIEVPAGQRIKIeVRNTGKGAAEFESVQ----LRKEK 73
Cdd:PRK10378    2 TINFRRNALQLALAALfssAFMANAADIPQVKVTVNDKQCEPMTLTVNAGKTQFI-IQNHSQKALEWEILKgvmvVEERE 80

                          90       100
                  ....*....|....*....|
gi 1235630504  74 VLAPGAdSFVVIAPLEPGEY 93
Cdd:PRK10378   81 NIAPGF-SQKMTANLQPGEY 99
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 1-95 1.15e-06

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 44.18  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   1 MRNNRKIAMLAATVLLASTAHAADLP----------------TFKLEMNDG-KLNPARIEVPAGQRIKIEVRNTGKGAAE 63
Cdd:COG4454     1 MKRTLALLLALALALLATAALAAGDShasaigkpgdaakvtrTITVTMGDTmRFTPDSIEVKAGETVRFVVTNPGKLKHE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1235630504  64 FESVQL------RKEKV--------------LAPGADSFVVIAPLEPGEYKF 95
Cdd:COG4454    81 FVLGTFaelaehAKVMAkmpdmehgdpneveLAPGETGELVWTFTKAGTFEF 132
PetE COG3794
Plastocyanin [Energy production and conversion];
39-108 1.85e-05

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 39.59  E-value: 1.85e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1235630504  39 PARIEVPAGQRIKIE--------VRNTGKGAAEFESvqlrkeKVLAPGaDSFVVIAPlEPGEYKFFDDFHQQAQGVIV 108
Cdd:COG3794     5 PATLTVKPGDTVTWVntdsvphnVTSDDGPDGAFDS------GLLAPG-ETFSVTFD-EPGTYDYYCTPHPWMVGTIV 74
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
1-92 5.96e-04

P pilus assembly protein, chaperone PapD [Extracellular structures];


Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 37.28  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235630504   1 MRNNRKIAMLAATVLLASTAHAADLptfklemndgKLNPARIEVPAGQR-IKIEVRNTGKGAAefeSVQLR----KEKVL 75
Cdd:COG3121     1 MKRLLRLLLLALLLLLASAAAAAGI----------SISPTRVIYPAGDKeASLTLTNTGDTPY---LVQSWvddwDQDAG 67

                          90       100
                  ....*....|....*....|.
gi 1235630504  76 APGADSFVVIAP----LEPGE 92
Cdd:COG3121    68 PDKATAPFVVTPplfrLEPGK 88
 
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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