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Conserved domains on  [gi|663517764|gb|AIF08175|]
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hypothetical protein SCO1/SenC/PrrC, involved in biogenesis of respiratory and photosynthetic systems [uncultured marine group II/III euryarchaeote KM3_27_D07]

Protein Classification

SCO family protein( domain architecture ID 10005092)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 50-226 2.85e-36

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


:

Pssm-ID: 441602  Cd Length: 156  Bit Score: 125.01  E-value: 2.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764  50 LVAHDGTNYSSENFDGKVVIVVFMFTRCPDVCPVVSANTKWLYSQLTEDEQSNVEVISITVDPWTDNITELATYKENMTL 129
Cdd:COG1999    5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDDVQVLFISVDPERDTPEVLKAYAEAFGA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764 130 D-WNHLTGEVDVLEPVWGNFDVGLRTVSSDeygyqnntdntsgsdetsgrhhpafDYLVDHSTGTILVDKNGY-QRVWWG 207
Cdd:COG1999   85 PrWIGLTGDPEEIAALAKAFGVYYEKVPDG-------------------------DYTFDHSAAVYLVDPDGRlRGYYPA 139

                        170
                 ....*....|....*....
gi 663517764 208 DVDwiPDLVLADVRELLSE 226
Cdd:COG1999  140 GED--PEELAADLKALLEE 156
 
Name Accession Description Interval E-value
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 50-226 2.85e-36

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 125.01  E-value: 2.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764  50 LVAHDGTNYSSENFDGKVVIVVFMFTRCPDVCPVVSANTKWLYSQLTEDEQSNVEVISITVDPWTDNITELATYKENMTL 129
Cdd:COG1999    5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDDVQVLFISVDPERDTPEVLKAYAEAFGA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764 130 D-WNHLTGEVDVLEPVWGNFDVGLRTVSSDeygyqnntdntsgsdetsgrhhpafDYLVDHSTGTILVDKNGY-QRVWWG 207
Cdd:COG1999   85 PrWIGLTGDPEEIAALAKAFGVYYEKVPDG-------------------------DYTFDHSAAVYLVDPDGRlRGYYPA 139

                        170
                 ....*....|....*....
gi 663517764 208 DVDwiPDLVLADVRELLSE 226
Cdd:COG1999  140 GED--PEELAADLKALLEE 156
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 45-200 1.70e-34

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: 120.02  E-value: 1.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764  45 VEPFDLVAHDGTNYSSENFDGKVVIVVFMFTRCPDVCPVVSANTKWLYSQLTEDEQSNVEVISITVDPWTDNITELATYK 124
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDDVQVVFISVDPERDTPEVLKAYA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663517764 125 ENMTLDWNHLTGEVDVLEPVWGNFDVGLRTVSSDEYgyqnntdntsgsdetsgrhhpafDYLVDHSTGTILVDKNG 200
Cdd:cd02968   82 KAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPEDDG-----------------------DYLVDHSAAIYLVDPDG 134
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 45-200 2.32e-24

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: 93.78  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764   45 VEPFDLVAHDGTNYSSENFDGKVVIVVFMFTRCPDVCPVVSANTKWLYSQLTEDEQSnVEVISITVDPWTDNITELATYK 124
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGID-VQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663517764  125 ENMTLDWNHLTGEVDVLEPVwgnfdvglrtvsSDEYGYQNNTDNTSGSdetsgrhhpafDYLVDHSTGTILVDKNG 200
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAA------------ARAFRVYYEKVPDDGG-----------DYTVDHTASVYLVDPDG 132
 
Name Accession Description Interval E-value
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 50-226 2.85e-36

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 125.01  E-value: 2.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764  50 LVAHDGTNYSSENFDGKVVIVVFMFTRCPDVCPVVSANTKWLYSQLTEDEQSNVEVISITVDPWTDNITELATYKENMTL 129
Cdd:COG1999    5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDDVQVLFISVDPERDTPEVLKAYAEAFGA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764 130 D-WNHLTGEVDVLEPVWGNFDVGLRTVSSDeygyqnntdntsgsdetsgrhhpafDYLVDHSTGTILVDKNGY-QRVWWG 207
Cdd:COG1999   85 PrWIGLTGDPEEIAALAKAFGVYYEKVPDG-------------------------DYTFDHSAAVYLVDPDGRlRGYYPA 139

                        170
                 ....*....|....*....
gi 663517764 208 DVDwiPDLVLADVRELLSE 226
Cdd:COG1999  140 GED--PEELAADLKALLEE 156
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 45-200 1.70e-34

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: 120.02  E-value: 1.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764  45 VEPFDLVAHDGTNYSSENFDGKVVIVVFMFTRCPDVCPVVSANTKWLYSQLTEDEQSNVEVISITVDPWTDNITELATYK 124
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGGDDVQVVFISVDPERDTPEVLKAYA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663517764 125 ENMTLDWNHLTGEVDVLEPVWGNFDVGLRTVSSDEYgyqnntdntsgsdetsgrhhpafDYLVDHSTGTILVDKNG 200
Cdd:cd02968   82 KAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPEDDG-----------------------DYLVDHSAAIYLVDPDG 134
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 45-200 2.32e-24

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: 93.78  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764   45 VEPFDLVAHDGTNYSSENFDGKVVIVVFMFTRCPDVCPVVSANTKWLYSQLTEDEQSnVEVISITVDPWTDNITELATYK 124
Cdd:pfam02630   1 GGPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGID-VQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663517764  125 ENMTLDWNHLTGEVDVLEPVwgnfdvglrtvsSDEYGYQNNTDNTSGSdetsgrhhpafDYLVDHSTGTILVDKNG 200
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAA------------ARAFRVYYEKVPDDGG-----------DYTVDHTASVYLVDPDG 132
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
48-215 2.46e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 42.54  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764  48 FDLVAHDGTNYSSENFDGKVVIVVFMFTRCPdVCPVVSANTKWLYSQLTEDeqsNVEVISITVdpwtDNITELATYKENM 127
Cdd:COG1225    4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCP-GCTAELPELRDLYEEFKDK---GVEVLGVSS----DSDEAHKKFAEKY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764 128 TLDWNHLtgeVDVLEPVWGNFDV-GLRTvssdeygyqnntdntsgsdetsgrhhpafdylvdhstgTILVDKNGY-QRVW 205
Cdd:COG1225   76 GLPFPLL---SDPDGEVAKAYGVrGTPT--------------------------------------TFLIDPDGKiRYVW 114

                        170
                 ....*....|
gi 663517764 206 WGDVDWIPDL 215
Cdd:COG1225  115 VGPVDPRPHL 124
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 44-150 9.87e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.21  E-value: 9.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663517764  44 AVEPFDLVAHDGTNYSSENFDGKVVIVVFMFTRCPDvCPVVSANTKWLYsqlteDEQSNVEVISITVDpwtDNITELATY 123
Cdd:COG0526    7 PAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPP-CRAEMPVLKELA-----EEYGGVVFVGVDVD---ENPEAVKAF 77

                         90       100
                 ....*....|....*....|....*..
gi 663517764 124 KENMTLDWNHLtgeVDVLEPVWGNFDV 150
Cdd:COG0526   78 LKELGLPYPVL---LDPDGELAKAYGV 101
 
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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