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Conserved domains on  [gi|648465673|ref|WP_026157424|]
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SCO family protein [Rhizobium leguminosarum]

Protein Classification

SCO family protein( domain architecture ID 11133300)

SCO (Synthesis of Cytochrome c Oxidase) family protein is required for the proper assembly of cytochrome c oxidase

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 39-176 2.14e-65

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: 197.40  E-value: 2.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673   39 GVPFTLVSQNGQPITEQALRGKPTALFFGFTHCPEVCPTTLFELNGWMEKVDPKGDKLQAYFVTVDPERDTPEIMNEYVS 118
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 648465673  119 NVSKRITGISGAPDKIAEVIKGFRVYAKKVPvdekDPNGDYTMDHTASVFLLDSAGRF 176
Cdd:pfam02630  81 AFGPRIIGLTGSPEQIAAAARAFRVYYEKVP----DDGGDYTVDHTASVYLVDPDGRF 134
 
Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 39-176 2.14e-65

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: 197.40  E-value: 2.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673   39 GVPFTLVSQNGQPITEQALRGKPTALFFGFTHCPEVCPTTLFELNGWMEKVDPKGDKLQAYFVTVDPERDTPEIMNEYVS 118
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 648465673  119 NVSKRITGISGAPDKIAEVIKGFRVYAKKVPvdekDPNGDYTMDHTASVFLLDSAGRF 176
Cdd:pfam02630  81 AFGPRIIGLTGSPEQIAAAARAFRVYYEKVP----DDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 43-198 4.45e-59

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 182.02  E-value: 4.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673  43 TLVSQNGQPITEQALRGKPTALFFGFTHCPEVCPTTLFELNGWMEKVDPKG-DKLQAYFVTVDPERDTPEIMNEYVSNVS 121
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGgDDVQVLFISVDPERDTPEVLKAYAEAFG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648465673 122 -KRITGISGAPDKIAEVIKGFRVYAkkvpvdEKDPNGDYTMDHTASVFLLDSAGRFSGTIAYGENPDTAVKKLENLVN 198
Cdd:COG1999   84 aPRWIGLTGDPEEIAALAKAFGVYY------EKVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLE 155
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 41-182 1.07e-56

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: 175.48  E-value: 1.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673  41 PFTLVSQNGQPITEQALRGKPTALFFGFTHCPEVCPTTLFELNGWMEKVDPKG-DKLQAYFVTVDPERDTPEIMNEYVSN 119
Cdd:cd02968    4 DFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGgDDVQVVFISVDPERDTPEVLKAYAKA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648465673 120 VSKRITGISGAPDKIAEVIKGFRVYAKKVPVDEkdpnGDYTMDHTASVFLLDSAGRFSGTIAY 182
Cdd:cd02968   84 FGPGWIGLTGTPEEIEALAKAFGVYYEKVPEDD----GDYLVDHSAAIYLVDPDGKLVRYYGG 142
 
Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 39-176 2.14e-65

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: 197.40  E-value: 2.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673   39 GVPFTLVSQNGQPITEQALRGKPTALFFGFTHCPEVCPTTLFELNGWMEKVDPKGDKLQAYFVTVDPERDTPEIMNEYVS 118
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 648465673  119 NVSKRITGISGAPDKIAEVIKGFRVYAKKVPvdekDPNGDYTMDHTASVFLLDSAGRF 176
Cdd:pfam02630  81 AFGPRIIGLTGSPEQIAAAARAFRVYYEKVP----DDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 43-198 4.45e-59

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 182.02  E-value: 4.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673  43 TLVSQNGQPITEQALRGKPTALFFGFTHCPEVCPTTLFELNGWMEKVDPKG-DKLQAYFVTVDPERDTPEIMNEYVSNVS 121
Cdd:COG1999    4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGgDDVQVLFISVDPERDTPEVLKAYAEAFG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648465673 122 -KRITGISGAPDKIAEVIKGFRVYAkkvpvdEKDPNGDYTMDHTASVFLLDSAGRFSGTIAYGENPDTAVKKLENLVN 198
Cdd:COG1999   84 aPRWIGLTGDPEEIAALAKAFGVYY------EKVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLE 155
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 41-182 1.07e-56

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: 175.48  E-value: 1.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673  41 PFTLVSQNGQPITEQALRGKPTALFFGFTHCPEVCPTTLFELNGWMEKVDPKG-DKLQAYFVTVDPERDTPEIMNEYVSN 119
Cdd:cd02968    4 DFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGgDDVQVVFISVDPERDTPEVLKAYAKA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648465673 120 VSKRITGISGAPDKIAEVIKGFRVYAKKVPVDEkdpnGDYTMDHTASVFLLDSAGRFSGTIAY 182
Cdd:cd02968   84 FGPGWIGLTGTPEEIEALAKAFGVYYEKVPEDD----GDYLVDHSAAIYLVDPDGKLVRYYGG 142
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 42-157 9.51e-05

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 40.67  E-value: 9.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673   42 FTLVSQNGQPITEQALRGKPTALFF-GFTHCPeVCPTTLFELNGWMEKVDPKGdkLQAYFVTVdperDTPEIMNEYVSNV 120
Cdd:pfam00578   8 FELPDGDGGTVSLSDYRGKWVVLFFyPADWTP-VCTTELPALADLYEEFKKLG--VEVLGVSV----DSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 648465673  121 SKRITGISgapDKIAEVIKGFRVYAKKVPVDEK-----DPNG 157
Cdd:pfam00578  81 GLPFPLLS---DPDGEVARAYGVLNEEEGGALRatfviDPDG 119
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 42-199 1.03e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.83  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648465673  42 FTLVSQNGQPITEQALRGKPTALFFGFTHCPeVCPTTLFELNGWMEKVdpkgDKLQAYFVTVDperDTPEIMNEYVSNvs 121
Cdd:COG0526   11 FTLTDLDGKPLSLADLKGKPVLVNFWATWCP-PCRAEMPVLKELAEEY----GGVVFVGVDVD---ENPEAVKAFLKE-- 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648465673 122 KRITGISGApDKIAEVIKGFRVYAkkVPvdekdpngdytmdhtaSVFLLDSAGRFSGTIAYGENPDTAVKKLENLVNK 199
Cdd:COG0526   81 LGLPYPVLL-DPDGELAKAYGVRG--IP----------------TTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
42-93 1.87e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.85  E-value: 1.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 648465673  42 FTLVSQNGQPITEQALRGKPTALFFGFTHCPeVCPTTLFELNGWMEKVDPKG 93
Cdd:COG1225    4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCP-GCTAELPELRDLYEEFKDKG 54
 
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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