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Conserved domains on  [gi|6319511|ref|NP_009593|]
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Cu-binding protein SCO1 [Saccharomyces cerevisiae S288C]

Protein Classification

SCO family protein( domain architecture ID 10121908)

SCO (Synthesis of Cytochrome c Oxidase) family protein belonging to the thioredoxin superfamily, similar to mitochondrial SCO1 and SCO2 that function as copper chaperones required for the maturation and proper assembly of cytochrome c oxidase

CATH:  3.40.30.10
Gene Ontology:  GO:0046872
PubMed:  10954195|10049365|15558583
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 115-257 5.20e-61

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


:

Pssm-ID: 239266  Cd Length: 142  Bit Score: 190.12  E-value: 5.20e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511  115 LGGPFHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKYGITLQPLFITCDPARDSPAVLKEY 194
Cdd:cd02968   1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDDVQVVFISVDPERDTPEVLKAY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319511  195 LSDFHPSILGLTGTFDEVKNACKKYRVYFSTPPnvKPGQDYLVDHSIFFYLMDPEGQFVDALG 257
Cdd:cd02968  81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVP--EDDGDYLVDHSAAIYLVDPDGKLVRYYG 141
 
Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 115-257 5.20e-61

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 190.12  E-value: 5.20e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511  115 LGGPFHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKYGITLQPLFITCDPARDSPAVLKEY 194
Cdd:cd02968   1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDDVQVVFISVDPERDTPEVLKAY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319511  195 LSDFHPSILGLTGTFDEVKNACKKYRVYFSTPPnvKPGQDYLVDHSIFFYLMDPEGQFVDALG 257
Cdd:cd02968  81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVP--EDDGDYLVDHSAAIYLVDPDGKLVRYYG 141
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 116-252 1.71e-58

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 183.54  E-value: 1.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511    116 GGPFHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKyGITLQPLFITCDPARDSPAVLKEYL 195
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEE-GIDVQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6319511    196 SDFHPSILGLTGTFDEVKNACKKYRVYFSTPPNvkPGQDYLVDHSIFFYLMDPEGQF 252
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAAARAFRVYYEKVPD--DGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 121-274 8.55e-47

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 154.29  E-value: 8.55e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511  121 LEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKYGITLQPLFITCDPARDSPAVLKEYLSDFH- 199
Cdd:COG1999   5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDDVQVLFISVDPERDTPEVLKAYAEAFGa 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319511  200 PSILGLTGTFDEVKNACKKYRVYFSTPpnvkPGQDYLVDHSIFFYLMDPEGQFVdalgRNYDEKTGVDKIVEHVK 274
Cdd:COG1999  85 PRWIGLTGDPEEIAALAKAFGVYYEKV----PDGDYTFDHSAAVYLVDPDGRLR----GYYPAGEDPEELAADLK 151
 
Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 115-257 5.20e-61

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 190.12  E-value: 5.20e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511  115 LGGPFHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKYGITLQPLFITCDPARDSPAVLKEY 194
Cdd:cd02968   1 IGPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDDVQVVFISVDPERDTPEVLKAY 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319511  195 LSDFHPSILGLTGTFDEVKNACKKYRVYFSTPPnvKPGQDYLVDHSIFFYLMDPEGQFVDALG 257
Cdd:cd02968  81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVP--EDDGDYLVDHSAAIYLVDPDGKLVRYYG 141
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 116-252 1.71e-58

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 183.54  E-value: 1.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511    116 GGPFHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKyGITLQPLFITCDPARDSPAVLKEYL 195
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEE-GIDVQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6319511    196 SDFHPSILGLTGTFDEVKNACKKYRVYFSTPPNvkPGQDYLVDHSIFFYLMDPEGQF 252
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAAARAFRVYYEKVPD--DGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 121-274 8.55e-47

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 154.29  E-value: 8.55e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511  121 LEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKYGITLQPLFITCDPARDSPAVLKEYLSDFH- 199
Cdd:COG1999   5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDDVQVLFISVDPERDTPEVLKAYAEAFGa 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319511  200 PSILGLTGTFDEVKNACKKYRVYFSTPpnvkPGQDYLVDHSIFFYLMDPEGQFVdalgRNYDEKTGVDKIVEHVK 274
Cdd:COG1999  85 PRWIGLTGDPEEIAALAKAFGVYYEKV----PDGDYTFDHSAAVYLVDPDGRLR----GYYPAGEDPEELAADLK 151
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 119-253 2.43e-04

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.44  E-value: 2.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511  119 FHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDiCPDELDKlglwLNTLSSKYGiTLQPLFITCDparDSPAVLKEYLSDF 198
Cdd:COG0526  11 FTLTDLDGKPLSLADLKGKPVLVNFWATWCPP-CRAEMPV----LKELAEEYG-GVVFVGVDVD---ENPEAVKAFLKEL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319511  199 HpsiLGLTGTFDEVKNACKKYRVYfSTPpnvkpgqdylvdhsiFFYLMDPEGQFV 253
Cdd:COG0526  82 G---LPYPVLLDPDGELAKAYGVR-GIP---------------TTVLIDKDGKIV 117
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
119-271 3.32e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.85  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319511  119 FHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPdICPDELDKLGLWLNTLSSKyGITLqpLFItcdpARDSPAVLKEYLSDF 198
Cdd:COG1225   4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCP-GCTAELPELRDLYEEFKDK-GVEV--LGV----SSDSDEAHKKFAEKY 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319511  199 hpsilGLTGT--FDEVKNACKKYRVYfSTPpnvkpgqdylvdhsiFFYLMDPEGQFVDALGRNYDEKTGVDKIVE 271
Cdd:COG1225  76 -----GLPFPllSDPDGEVAKAYGVR-GTP---------------TTFLIDPDGKIRYVWVGPVDPRPHLEEVLE 129
 
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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