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Conserved domains on  [gi|281182716|ref|NP_001162580|]
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protein SCO2 homolog, mitochondrial precursor [Homo sapiens]

Protein Classification

SCO family protein( domain architecture ID 10121908)

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

PubMed:  10954195
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 ...
 101-242 1.35e-64

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: 198.21  E-value: 1.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 101 QGDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGlPPVQPVFITVDPERDDVEAMARY 180
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGG-DDVQVVFISVDPERDTPEVLKAY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281182716 181 VQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 242
Cdd:cd02968   81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141
 
Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 101-242 1.35e-64

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: 198.21  E-value: 1.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 101 QGDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGlPPVQPVFITVDPERDDVEAMARY 180
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGG-DDVQVVFISVDPERDTPEVLKAY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281182716 181 VQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 242
Cdd:cd02968   81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 102-237 1.80e-63

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: 195.09  E-value: 1.80e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716  102 GDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPglPPVQPVFITVDPERDDVEAMARYV 181
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEG--IDVQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281182716  182 QDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPkDEDQDYIVDHSIAIYLLNPDGLF 237
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAAARAFRVYYEKVP-DDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 106-260 1.59e-53

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 170.47  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 106 LLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGlPPVQPVFITVDPERDDVEAMARYVQDFH 185
Cdd:COG1999    5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGG-DDVQVLFISVDPERDTPEVLKAYAEAFG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182716 186 -PRLLGLTGSTKQVAQASHSYRVYYNagpKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQISDSVRRHMAA 260
Cdd:COG1999   84 aPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
 
Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 101-242 1.35e-64

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: 198.21  E-value: 1.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 101 QGDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGlPPVQPVFITVDPERDDVEAMARY 180
Cdd:cd02968    2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGG-DDVQVVFISVDPERDTPEVLKAY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281182716 181 VQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 242
Cdd:cd02968   81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 102-237 1.80e-63

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: 195.09  E-value: 1.80e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716  102 GDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPglPPVQPVFITVDPERDDVEAMARYV 181
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEG--IDVQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281182716  182 QDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPkDEDQDYIVDHSIAIYLLNPDGLF 237
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAAARAFRVYYEKVP-DDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 106-260 1.59e-53

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 170.47  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 106 LLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGlPPVQPVFITVDPERDDVEAMARYVQDFH 185
Cdd:COG1999    5 LTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGG-DDVQVLFISVDPERDTPEVLKAYAEAFG 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281182716 186 -PRLLGLTGSTKQVAQASHSYRVYYNagpKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQISDSVRRHMAA 260
Cdd:COG1999   84 aPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
103-235 2.24e-08

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 51.79  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 103 DFHLLDHRGRARCKADFRGQWVLMYFGFTHCPdICPDELEKLVQVVRQLEAEpGLppvqpVFITVDPerDDVEAMARYVQ 182
Cdd:COG1225    3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCP-GCTAELPELRDLYEEFKDK-GV-----EVLGVSS--DSDEAHKKFAE 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 281182716 183 DFHPRLLGLTGSTKQVAQAshsYRVYynAGPkdedqdyivdhsiAIYLLNPDG 235
Cdd:COG1225   74 KYGLPFPLLSDPDGEVAKA---YGVR--GTP-------------TTFLIDPDG 108
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 103-260 1.11e-07

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 49.69  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 103 DFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDiCPDELEKLVQVVRQleaepgLPPVQPVFITVDperDDVEAMARYVQ 182
Cdd:COG0526   10 DFTLTDLDGKPLSLADLKGKPVLVNFWATWCPP-CRAEMPVLKELAEE------YGGVVFVGVDVD---ENPEAVKAFLK 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281182716 183 DFHPRLLGLTGSTKQVAQAshsYRVYynagpkdedqdyivdhSI-AIYLLNPDGLFTDYYGRSRSAEQISDSVRRHMAA 260
Cdd:COG0526   80 ELGLPYPVLLDPDGELAKA---YGVR----------------GIpTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 117-209 3.03e-04

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 39.53  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716 117 ADFRGQWVLMYFGFTHCPdICPDELEKLVQVVRQLeAEPGLPpvqpvFITVDPERDDVEAMARYVQDFHPRLLGLTGSTK 196
Cdd:cd02966   15 SDLKGKVVLVNFWASWCP-PCRAEMPELEALAKEY-KDDGVE-----VVGVNVDDDDPAAVKAFLKKYGITFPVLLDPDG 87

                         90
                 ....*....|...
gi 281182716 197 QVAQAshsYRVYY 209
Cdd:cd02966   88 ELAKA---YGVRG 97
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 121-235 8.45e-04

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 37.67  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716  121 GQWVLMYFGFTHCPDiCPDELEKLVQVVRQLEAEPGlppVQPVFITVDperDDVEAMARYVQDFHPRLlgltgstkqvaq 200
Cdd:pfam13905   1 GKVVLLYFGASWCKP-CRRFTPLLKELYEKLKKKKN---VEIVFVSLD---RDLEEFKDYLKKMPKDW------------ 61

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 281182716  201 ashsYRVYYNAGPKDEDQD-YIVDHSIAIYLLNPDG 235
Cdd:pfam13905  62 ----LSVPFDDDERNELKRkYGVNAIPTLVLLDPNG 93
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 103-223 1.17e-03

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: 37.97  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281182716  103 DFHLLDHRGRARCKADFRGQW-VLMYFGFTHCPdICPDELEKLVQVVRQLEAEpGlppVQPVFITVdperDDVEAMARYV 181
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKWvVLFFYPADWTP-VCTTELPALADLYEEFKKL-G---VEVLGVSV----DSPESHKAFA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 281182716  182 QDfhprlLGLT-----GSTKQVAQAshsYRVYYNAGPKDEDQDYIVD 223
Cdd:pfam00578  78 EK-----YGLPfpllsDPDGEVARA---YGVLNEEEGGALRATFVID 116
 
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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