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Conserved domains on  [gi|502810899|ref|WP_013045875|]
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SCO family protein [Candidatus Puniceispirillum marinum]

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. ...
 56-187 3.96e-68

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: 205.11  E-value: 3.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899   56 SFSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDVCPTTLADISGWLDDLGDEADEMNVVFITVDPERDTVETMAEYVGYF 135
Cdd:pfam02630   3 PFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLEAF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502810899  136 HPAIRGWTGPEEQIARVADGFRATYERVPTGSGDYTMNHTASVFLFAASGRF 187
Cdd:pfam02630  83 GPRIIGLTGSPEQIAAAARAFRVYYEKVPDDGGDYTVDHTASVYLVDPDGRF 134
 
Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 56-187 3.96e-68

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: 205.11  E-value: 3.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899   56 SFSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDVCPTTLADISGWLDDLGDEADEMNVVFITVDPERDTVETMAEYVGYF 135
Cdd:pfam02630   3 PFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLEAF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502810899  136 HPAIRGWTGPEEQIARVADGFRATYERVPTGSGDYTMNHTASVFLFAASGRF 187
Cdd:pfam02630  83 GPRIIGLTGSPEQIAAAARAFRVYYEKVPDDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 55-210 2.06e-59

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 183.56  E-value: 2.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899  55 MSFSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDVCPTTLADISGWLDDLGDEA-DEMNVVFITVDPERDTVETMAEYVG 133
Cdd:COG1999    1 MRRTLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGgDDVQVLFISVDPERDTPEVLKAYAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502810899 134 YFH-PAIRGWTGPEEQIARVADGFRATYERVPtgSGDYTMNHTASVFLFAASGRFVTMIDYHEPREFAVPKIRRAMEE 210
Cdd:COG1999   81 AFGaPRWIGLTGDPEEIAALAKAFGVYYEKVP--DGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 57-193 3.69e-57

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: 177.41  E-value: 3.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899  57 FSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDVCPTTLADISGWLDDLGDEA-DEMNVVFITVDPERDTVETMAEYVGYF 135
Cdd:cd02968    5 FTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGgDDVQVVFISVDPERDTPEVLKAYAKAF 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502810899 136 HPAIRGWTGPEEQIARVADGFRATYERVPTGSGDYTMNHTASVFLFAASGRFVTMIDY 193
Cdd:cd02968   85 GPGWIGLTGTPEEIEALAKAFGVYYEKVPEDDGDYLVDHSAAIYLVDPDGKLVRYYGG 142
 
Name Accession Description Interval E-value
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 56-187 3.96e-68

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: 205.11  E-value: 3.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899   56 SFSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDVCPTTLADISGWLDDLGDEADEMNVVFITVDPERDTVETMAEYVGYF 135
Cdd:pfam02630   3 PFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGIDVQPVFITVDPERDTPEVLAEYLEAF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502810899  136 HPAIRGWTGPEEQIARVADGFRATYERVPTGSGDYTMNHTASVFLFAASGRF 187
Cdd:pfam02630  83 GPRIIGLTGSPEQIAAAARAFRVYYEKVPDDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 55-210 2.06e-59

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


Pssm-ID: 441602  Cd Length: 156  Bit Score: 183.56  E-value: 2.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899  55 MSFSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDVCPTTLADISGWLDDLGDEA-DEMNVVFITVDPERDTVETMAEYVG 133
Cdd:COG1999    1 MRRTLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGgDDVQVLFISVDPERDTPEVLKAYAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502810899 134 YFH-PAIRGWTGPEEQIARVADGFRATYERVPtgSGDYTMNHTASVFLFAASGRFVTMIDYHEPREFAVPKIRRAMEE 210
Cdd:COG1999   81 AFGaPRWIGLTGDPEEIAALAKAFGVYYEKVP--DGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 57-193 3.69e-57

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: 177.41  E-value: 3.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899  57 FSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDVCPTTLADISGWLDDLGDEA-DEMNVVFITVDPERDTVETMAEYVGYF 135
Cdd:cd02968    5 FTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADGgDDVQVVFISVDPERDTPEVLKAYAKAF 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502810899 136 HPAIRGWTGPEEQIARVADGFRATYERVPTGSGDYTMNHTASVFLFAASGRFVTMIDY 193
Cdd:cd02968   85 GPGWIGLTGTPEEIEALAKAFGVYYEKVPEDDGDYLVDHSAAIYLVDPDGKLVRYYGG 142
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 56-210 1.70e-06

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 45.84  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899  56 SFSLTDHEGNAVGPETLIGRPTMAFFGFTYCPDvCPTTLADISGWLDDLGDeadeMNVVFITVDPERDTVETMAEYVGYF 135
Cdd:COG0526   10 DFTLTDLDGKPLSLADLKGKPVLVNFWATWCPP-CRAEMPVLKELAEEYGG----VVFVGVDVDENPEAVKAFLKELGLP 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502810899 136 HPAIRGWTGpeeqiaRVADGFRATYerVPTgsgdytmnhtasVFLFAASG----RFVTMIDYHEPREFavpkIRRAMEE 210
Cdd:COG0526   85 YPVLLDPDG------ELAKAYGVRG--IPT------------TVLIDKDGkivaRHVGPLSPEELEEA----LEKLLAK 139
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
57-132 2.54e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.85  E-value: 2.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502810899  57 FSLTDHEGNAVGPETLIGRPTMAFFGFTYCPdVCPTTLADISGWLDDLGDEademNVVFITVDPerDTVETMAEYV 132
Cdd:COG1225    4 FTLPDLDGKTVSLSDLRGKPVVLYFYATWCP-GCTAELPELRDLYEEFKDK----GVEVLGVSS--DSDEAHKKFA 72
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 57-165 6.44e-03

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: 35.29  E-value: 6.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502810899  57 FSLTDHEGNAVGPETLIGRPTMAFFGFTYCPdVCPTTLADisgwLDDLGDEADEMNVVFITV---DPERDTVETMAEYVG 133
Cdd:cd02966    2 FSLPDLDGKPVSLSDLKGKVVLVNFWASWCP-PCRAEMPE----LEALAKEYKDDGVEVVGVnvdDDDPAAVKAFLKKYG 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 502810899 134 YFHPAIRGWTGpeeqiaRVADGFRATYerVPT 165
Cdd:cd02966   77 ITFPVLLDPDG------ELAKAYGVRG--LPT 100
 
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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